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吉田賀弥

徳島大学

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Jグローバル
KAKEN
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2024年11月21日更新

職名: 准教授
電話: 088-6337322
電子メール: kaya@dent.tokushima-u.ac.jp
学歴: 1999/3: 徳島大学歯学部卒業
2003/3: 徳島大学大学院歯学研究科博士課程修了
学位: 博士(歯学) (徳島大学) (2003年3月)
職歴・経歴: 2003/4: 徳島大学助手，歯学部歯学科

専門分野・研究分野: 口腔解剖学 (Oral Anatomy)
口腔組織学 (Oral Histology)
細胞生物学 (Cell Biology)
骨代謝学

研究者総覧で最新データを確認する

2024年11月21日更新

専門分野・研究分野: 口腔解剖学 (Oral Anatomy)
口腔組織学 (Oral Histology)
細胞生物学 (Cell Biology)
骨代謝学
担当経験のある授業科目: 卒業研究 (学部)
卒業研究(4年生) (学部)
口腔保健医療管理学 (大学院)
口腔保健医療管理学特別演習 (大学院)
口腔保健医療管理学特別研究 (大学院)
口腔保健学教育・研究系課題実習 (大学院)
口腔保健学臨床系課題実習 (大学院)
口腔保健学課題研究演習 (大学院)
口腔保健支援学特別演習 (大学院)
口腔保健支援学特別研究 (大学院)
口腔保健衛生学基礎実習 (学部)
口腔健康管理学特論 (大学院)
歯の解剖学 (学部)
歯型彫刻 (学部)
解剖学 (学部)
骨学・系統解剖見学 (学部)
高齢者・障害者口腔機能管理学 (大学院)
高齢者・障害者口腔機能管理学演習 (大学院)
指導経験: 2人 (修士), 2人 (博士)

研究者総覧で最新データを確認する

2024年11月21日更新

専門分野・研究分野: 口腔解剖学 (Oral Anatomy)
口腔組織学 (Oral Histology)
細胞生物学 (Cell Biology)
骨代謝学

研究テーマ: 骨芽細胞の分化機構, 歯周病と全身疾患の関連性, 歯周病における細胞外小胞の役割

著書

Bruna Rabelo Amorim, Hirohiko Okamura, Kaya Yoshida, Lihong Qiu, Jie Wang and Tatsuji Haneji :
Oral Oncology 12, --- The transcriptional factor Osterix directly interacts with RNA helicase A ---,
Ocean Papers & Printers, New Delhi, India, May 2008.

論文

Mana Mekata, Kaya Yoshida, Takai Ayu, Yuka Hiroshima, Ayu Ikuta, Kayo Yoshida and Kazumi Ozaki :
Porphyromonas gingivalis outer membrane vesicles increase vascular permeability by inducing stress fiber formation and degrading vascular endothelial-cadherin in endothelial cells.,
The FEBS Journal, Vol.in press, Yuka Hiroshima, Rie Kido, Jun-ichi Kido, Mika Bandou, Kaya Yoshida, Akikazu Murakami and Yasuo Shinohara :
Synthesis of secretory leukocyte protease inhibitor using cell-free protein synthesis system,
Odontology, Vol.112, No.4, 1103-1112, 2024.

(要約): Secretory leukocyte protease inhibitor (SLPI) functions as a protease inhibitor that modulates excessive proteolysis in the body, exhibits broad-spectrum antimicrobial activity, regulates inflammatory responses, and plays an important role in the innate immunity. The purpose of the study was to artificially synthesize a SLPI, an antimicrobial peptide, and investigate its effect on antimicrobial activity against Porphyromonas gingivalis and interleukin-6 (IL-6) production. SLPI protein with a molecular weight of approximately 13 kDa was artificially synthesized using a cell-free protein synthesis (CFPS) system and investigated by western blotting and enzyme-linked immunosorbent assay (ELISA). Disulfide bond isomerase in the protein synthesis mixture increased the amount of SLPI synthesized. The synthesized SLPI (sSLPI) protein was purified and its antimicrobial activity was investigated based on the growth of Porphyromonas gingivalis and bacterial adhesion to oral epithelial cells. The effect of sSLPI on IL-6 production in human periodontal ligament fibroblasts (HPLFs) was examined by ELISA. Our results showed that sSLPI significantly inhibited the growth of Porphyromonas gingivalis and bacterial adhesion to oral epithelial cells and further inhibited IL-6 production by HPLFs. These results suggested that SLPI artificially synthesized using the CFPS system may play a role in the prevention of periodontal diseases through its antimicrobial and anti-inflammatory effects.
(徳島大学機関リポジトリ): ● Metadata: 119164
(出版サイトへのリンク): ● Publication site (DOI): 10.1007/s10266-024-00910-8
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 38502469; ● Search Scopus @ Elsevier (PMID): 38502469; ● Search Scopus @ Elsevier (DOI): 10.1007/s10266-024-00910-8

(徳島大学機関リポジトリ: 119164, DOI: 10.1007/s10266-024-00910-8, PubMed: 38502469) Kayo Yoshida, Kaya Yoshida, Yasuhiro Mouri, Ayu Takai, Mariko Seyama, Mana Mekata, Noriko Mizusawa, Keiko Miyoshi, Yasusei Kudo and Kazumi Ozaki :
Porphyromonas gingivalis infection alters microRNA composition in extracellular vesicles.,
Journal of Oral Biosciences, Vol.66, No.2, 365-372, 2024. Kayo Yoshida, Kaya Yoshida, Mariko Seyama, Yuka Hiroshima, Mana Mekata, Natsumi Fujiwara, Yasusei Kudo and Kazumi Ozaki :
Porphyromonas gingivalis outer membrane vesicles in cerebral ventricles activate microglia in mice,
Oral Diseases, Vol.29, No.8, 3688-3697, 2023.

(要約): Objective: Porphyromonas gingivalis (Pg) is thought to be involved in the progression of Alzheimer's disease (AD). Whether Pg or its contents can reach the brain and directly affect neuropathology is, however, unknown. Here, we investigated whether outer membrane vesicles (OMVs) of Pg translocate to the brain and induce the pathogenic features of AD. Material and Methods: Pg OMVs were injected into the abdominal cavity of mice for 12 weeks. Pg OMV translocation to the brain was detected by immunohistochemistry using an anti-gingipain antibody. Tau protein and microglial activation in the mouse brain were examined by western blotting and immunohistochemistry. The effect of gingipains on inflammation was assessed by real-time polymerase chain reaction using human microglial HMC3 cells. Results: Gingipains were detected in the region around cerebral ventricles, choroid plexus, and ventricular ependymal cells in Pg OMV-administered mice. Tau and phosphorylated Tau protein increased and microglia were activated. Pg OMVs also increased the gene expression of proinflammatory cytokines in HMC3 cells in a gingipain-dependent manner. Conclusion: Pg OMVs, including gingipains, can reach the cerebral ventricle and induce neuroinflammation by activating microglia. Pg OMVs may provide a better understanding of the implications of periodontal diseases in neurodegenerative conditions such as AD.
(キーワード): cerebral ventricle / gingipain / microglia / neuroinflammation / outer membrane vesicle / Porphyromonas gingivalis
(徳島大学機関リポジトリ): ● Metadata: 118518
(出版サイトへのリンク): ● Publication site (DOI): 10.1111/odi.14413
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36266256; ● CiNii @ 国立情報学研究所 (CRID): 1050861074220169344; ● Summary page in Scopus @ Elsevier: 2-s2.0-85141542224

(徳島大学機関リポジトリ: 118518, DOI: 10.1111/odi.14413, PubMed: 36266256, CiNii: 1050861074220169344, Elsevier: Scopus) Yaqiong Yu, Yoko Uchida-Fukuhara, Yao Weng, Yuhan He, Mika Ikegame, Ziyi Wang, Kaya Yoshida, Hirohiko Okamura and Lihong Qiu :
Neuropilin 1 (NRP1) Positively Regulates Adipogenic Differentiation in C3H10T1/2 Cells,
International Journal of Molecular Sciences, Vol.17, No.24 (8), 7394, 2023.

(要約): Neuropilin 1 (NRP1), a non-tyrosine kinase receptor for several ligands, is highly expressed in many kinds of mesenchymal stem cells (MSCs), but its function is poorly understood. In this study, we explored the roles of full-length NRP1 and glycosaminoglycan (GAG)-modifiable NRP1 in adipogenesis in C3H10T1/2 cells. The expression of full-length NRP1 and GAG-modifiable NRP1 increased during adipogenic differentiation in C3H10T1/2 cells. NRP1 knockdown repressed adipogenesis while decreasing the levels of Akt and ERK1/2 phosphorylation. Moreover, the scaffold protein JIP4 was involved in adipogenesis in C3H10T1/2 cells by interacting with NRP1. Furthermore, overexpression of non-GAG-modifiable NRP1 mutant (S612A) greatly promoted adipogenic differentiation, accompanied by upregulation of the phosphorylated Akt and ERK1/2. Taken together, these results indicate that NRP1 is a key regulator that promotes adipogenesis in C3H10T1/2 cells by interacting with JIP4 and activating the Akt and ERK1/2 pathway. Non-GAG-modifiable NRP1 mutant (S612A) accelerates the process of adipogenic differentiation, suggesting that GAG glycosylation is a negative post-translational modification of NRP1 in adipogenic differentiation.
(キーワード): Adipogenesis / Neuropilin-1 / Proto-Oncogene Proteins c-akt / Cell Differentiation / Mesenchymal Stem Cells
(徳島大学機関リポジトリ): ● Metadata: 119248
(出版サイトへのリンク): ● Publication site (DOI): 10.3390/ijms24087394
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 37108554; ● CiNii @ 国立情報学研究所 (CRID): 1050014713340241792; ● Search Scopus @ Elsevier (PMID): 37108554; ● Search Scopus @ Elsevier (DOI): 10.3390/ijms24087394

(徳島大学機関リポジトリ: 119248, DOI: 10.3390/ijms24087394, PubMed: 37108554, CiNii: 1050014713340241792) Jun-ichi Kido, Yuka Hiroshima, Rie Kido, Kaya Yoshida, Yuji Inagaki, Koji Naruishi, Kazuaki Kajimoto, Masatoshi Kataoka, Yasuo Shinohara and Hiromichi Yumoto :
Lipocalin 2, synthesized using a cell-free protein synthesis system and encapsulated into liposomes, inhibits the adhesion of Porphyromonas gingivalis to human oral epithelial cells.,
Journal of Periodontal Research, Vol.58, No.2, 262-273, 2023.

(徳島大学機関リポジトリ): ● Metadata: 119199
(出版サイトへのリンク): ● Publication site (DOI): 10.1111/jre.13088
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36579753; ● Search Scopus @ Elsevier (PMID): 36579753; ● Search Scopus @ Elsevier (DOI): 10.1111/jre.13088

(徳島大学機関リポジトリ: 119199, DOI: 10.1111/jre.13088, PubMed: 36579753) Yuka Hiroshima, Jun-ichi Kido, Rie Kido, Kaya Yoshida, Mika Bandou, Kazuaki Kajimoto, Hiromichi Yumoto and Yasuo Shinohara :
β-defensin 2 synthesized by a cell-free protein synthesis system and encapsulated in liposomes inhibits adhesion of Porphyromonas gingivalis to oral epithelial cells.,
Odontology, Vol.111, 830-838, 2023.

(徳島大学機関リポジトリ): ● Metadata: 119198
(出版サイトへのリンク): ● Publication site (DOI): 10.1007/s10266-023-00789-x
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36745267; ● Search Scopus @ Elsevier (PMID): 36745267; ● Search Scopus @ Elsevier (DOI): 10.1007/s10266-023-00789-x

(徳島大学機関リポジトリ: 119198, DOI: 10.1007/s10266-023-00789-x, PubMed: 36745267) Yuta Uemura, Yuka Hiroshima, Ayano Tada, Keiji Murakami, Kaya Yoshida, Yuji Inagaki, Tomomi Kuwahara, Akikazu Murakami, Hideki Fujii and Hiromichi Yumoto :
Porphyromonas gingivalis Outer Membrane Vesicles Stimulate Gingival Epithelial Cells to Induce Pro-Inflammatory Cytokines via the MAPK and STING Pathways,
Biomedicines, Vol.10, No.10, 2643, 2022.

(要約): () is a keystone pathogen associated with chronic periodontitis and produces outer membrane vesicles (OMVs) that contain lipopolysaccharide (LPS), gingipains, and pathogen-derived DNA and RNA. -OMVs are involved in the pathogenesis of periodontitis. -OMV-activated pathways that induce the production of the pro-inflammatory cytokines, interleukin (IL)-6, and IL-8 in the human gingival epithelial cell line, OBA-9, were investigated. The role of mitogen-activated protein kinase (MAPK) and nuclear factor (NF)-κB in levels of -OMV-induced pro-inflammatory cytokines was investigated using Western blot analysis and specific pathway inhibitors. -OMVs induced IL-6 and IL-8 production via the extracellular signal-regulated kinase (Erk) 1/2, c-Jun N-terminal kinase (JNK), p38 MAPK, and NF-κB signaling pathways in OBA-9 cells. In addition, the stimulator of interferon genes (STING), an essential innate immune signaling molecule, was triggered by a cytosolic pathogen DNA. -OMV-induced IL-6 and IL-8 mRNA expression and production were significantly suppressed by STING-specific small interfering RNA. Taken together, these results demonstrated that -OMV-activated Erk1/2, JNK, p38 MAPK, STING, and NF-κB signaling pathways resulting in increased IL-6 and IL-8 expression in human gingival epithelial cells. These results suggest that -OMVs may play important roles in periodontitis exacerbation by stimulating various pathways.
(徳島大学機関リポジトリ): ● Metadata: 117616
(出版サイトへのリンク): ● Publication site (DOI): 10.3390/biomedicines10102643
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36289904; ● Search Scopus @ Elsevier (PMID): 36289904; ● Search Scopus @ Elsevier (DOI): 10.3390/biomedicines10102643

(徳島大学機関リポジトリ: 117616, DOI: 10.3390/biomedicines10102643, PubMed: 36289904) Weng Yao, Yang Ziyi, Fukuhara Yoko, Tanai Airi, Ikegame Mika, Yamada Daisuke, Takarada Takeshi, Izawa Takashi, Hayano Satoru, Kaya Yoshida, Kamioka Hiroshi and Hirohiko Okamura :
O-GlcNAcylation drives calcium signaling toward osteoblast differentiation: A bioinformatics-oriented study,
BioFactors, Vol.47, No.6, 992-1015, 2021.

(出版サイトへのリンク): ● Publication site (DOI): 10.1002/biof.1774
(文献検索サイトへのリンク): ● Summary page in Scopus @ Elsevier: 2-s2.0-85113175332

(DOI: 10.1002/biof.1774, Elsevier: Scopus) Yoshida Kayo, Kaya Yoshida, Natsumi Fujiwara, Mariko Seyama, Ono Kisho, Kawai Hotaka, Guo Jiajie, Wang Ziyi, Weng Yao, Yu Yaqiong, Uchida-Fukuhara Yoko, Ikegame Mika, Sasaki Akira, Nagatsuka Hitoshi, Kamioka Hiroshi, Hirohiko Okamura and Kazumi Ozaki :
Extracellular vesicles of P. gingivalis-infected macrophages induce lung injury,
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, Vol.1867, No.11, 166236, 2021.

(要約): Periodontal diseases are common inflammatory diseases that are induced by infection with periodontal bacteria such as Porphyromonas gingivalis (Pg). The association between periodontal diseases and many types of systemic diseases has been demonstrated; the term "periodontal medicine" is used to describe how periodontal infection/inflammation may impact extraoral health. However, the molecular mechanisms by which the factors produced in the oral cavity reach multiple distant organs and impact general health have not been elucidated. Extracellular vesicles (EVs) are nano-sized spherical structures secreted by various types of cells into the tissue microenvironment, and influence pathophysiological conditions by delivering their cargo. However, a detailed understanding of the effect of EVs on periodontal medicine is lacking. In this study, we investigated whether EVs derived from Pg-infected macrophages reach distant organs in mice and influence the pathophysiological status. EVs were isolated from human macrophages, THP-1 cells, infected with Pg. We observed that EVs from Pg-infected THP-1 cells (Pg-inf EVs) contained abundant core histone proteins such as histone H3 and translocated to the lungs, liver, and kidneys of mice. Pg-inf EVs also induced pulmonary injury, including edema, vascular congestion, inflammation, and collagen deposition causing alveoli destruction. The Pg-inf EVs or the recombinant histone H3 activated the NF-κB pathway, leading to increase in the levels of pro-inflammatory cytokines in human lung epithelial A549 cells. Our results suggest a possible mechanism by which EVs produced in periodontal diseases contribute to the progression of periodontal medicine.
(徳島大学機関リポジトリ): ● Metadata: 116182
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbadis.2021.166236
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34389473; ● Search Scopus @ Elsevier (PMID): 34389473; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbadis.2021.166236

(徳島大学機関リポジトリ: 116182, DOI: 10.1016/j.bbadis.2021.166236, PubMed: 34389473) Wenhua Shao, Natsumi Fujiwara, Yasuhiro Mouri, Satoru Kisoda, Kayo Yoshida, Kaya Yoshida, Hiromichi Yumoto, Kazumi Ozaki, Naozumi Ishimaru and Yasusei Kudo :
Conversion from epithelial to partial-EMT phenotype by Fusobacterium nucleatum infection promotes invasion of oral cancer cells.,
Scientific Reports, Vol.11, No.1, 14943, 2021.

(要約): The ability of cancer cells to undergo partial-epithelial mesenchymal transition (p-EMT), rather than complete EMT, poses a higher metastatic risk. Although Fusobacterium nucleatum mainly inhabits in oral cavity, attention has been focused on the F. nucleatum involvement in colorectal cancer development. Here we examined the p-EMT regulation by F. nucleatum in oral squamous cell carcinoma (OSCC) cells. We cultured OSCC cells with epithelial, p-EMT or EMT phenotype with live or heat-inactivated F. nucleatum. Expression of the genes involved in epithelial differentiation, p-EMT and EMT were examined in OSCC cells after co-culture with F. nucleatum by qPCR. Cell growth and invasion of OSCC cells were also examined. Both live and heat-inactivated F. nucleatum upregulated the expression of p-EMT-related genes in OSCC cells with epithelial phenotype, but not with p-EMT or EMT phenotype. Moreover, F. nucleatum promoted invasion of OSCC cells with epithelial phenotype. Co-culture with other strains of bacteria other than Porphyromonas gingivalis did not alter p-EMT-related genes in OSCC cells with epithelial phenotype. F. nucleatum infection may convert epithelial to p-EMT phenotype via altering gene expression in OSCC. Oral hygiene managements against F. nucleatum infection may contribute to reduce the risk for an increase in metastatic ability of OSCC.
(徳島大学機関リポジトリ): ● Metadata: 116445
(出版サイトへのリンク): ● Publication site (DOI): 10.1038/s41598-021-94384-1
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 34294795; ● Summary page in Scopus @ Elsevier: 2-s2.0-85111135598

(徳島大学機関リポジトリ: 116445, DOI: 10.1038/s41598-021-94384-1, PubMed: 34294795, Elsevier: Scopus) Natsumi Fujiwara, Naoya Kitamura, Kaya Yoshida, Tetsuya Yamamoto, Kazumi Ozaki and Yasusei Kudo :
Involvement of Fusobacterium Species in Oral Cancer Progression: A Literature Review Including Other Types of Cancer,
International Journal of Molecular Sciences, Vol.21, No.17, 6207, 2020.

(要約): Chronic inflammation caused by infections has been suggested to be one of the most important cause of cancers. It has recently been shown that there is correlation between intestinal bacteria and cancer development including metastasis. As over 700 bacterial species exist in an oral cavity, it has been concerning that bacterial infection may cause oral cancer. However, the role of bacteria regarding tumorigenesis of oral cancer remains unclear. Several papers have shown that species deriving the oral cavities, especially, play a crucial role for the development of colorectal and esophageal cancer. is a well-known oral bacterium involved in formation of typical dental plaque on human teeth and causing periodontal diseases. The greatest characteristic of is its ability to adhere to various bacteria and host cells. Interestingly, is frequently detected in oral cancer tissues. Moreover, detection of is correlated with the clinical stage of oral cancer. Although the detailed mechanism is still unclear, species have been suggested to be associated with cell adhesion, tumorigenesis, epithelial-to-mesenchymal transition, inflammasomes, cell cycle, etc. in oral cancer. In this review, we introduce the reports focused on the association of species with cancer development and progression including oral, esophageal, and colon cancers.
(キーワード): Cell Adhesion / Colonic Neoplasms / Disease Progression / Epithelial-Mesenchymal Transition / Esophageal Neoplasms / Fusobacterium / Fusobacterium Infections / Humans / Inflammasomes / Mouth / Mouth Neoplasms
(徳島大学機関リポジトリ): ● Metadata: 115246
(出版サイトへのリンク): ● Publication site (DOI): 10.3390/ijms21176207
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32867334; ● Summary page in Scopus @ Elsevier: 2-s2.0-85090108629

(徳島大学機関リポジトリ: 115246, DOI: 10.3390/ijms21176207, PubMed: 32867334, Elsevier: Scopus) Jiajie Guo, Ziyi Wang, Yao Weng, Haoze Yuan, Kaya Yoshida, Mika Ikegame, Kenta Uchibe, Hiroshi Kamioka, Kazuhiko Ochiai, Hirohiko Okamura and Lihong Qiu :
N-(3-oxododecanoyl)-homoserine lactone regulates osteoblast apoptosis and differentiation by mediating intracellular calcium,
Cellular Signalling, Vol.75, 109740, 2020.

(要約): Pseudomonas aeruginosa (P. aeruginosa) is associated with periapical periodontitis. The lesions are characterized by a disorder in osteoblast metabolism. Quorum sensing molecular N-(3-oxododecanoyl)-homoserine lactone (AHL) is secreted by P. aeruginosa and governs the expression of numerous virulence factors. AHL can trigger intracellular calcium ([Ca]) fluctuations in many host cells. However, it is unclear whether AHL can regulate osteoblast metabolism by affecting [Ca] changes or its spatial correlation. We explored AHL-induced apoptosis and differentiation in pre-osteoblastic MC3T3-E1 cells and evaluated [Ca] mobilization using several extraction methods. The spatial distribution pattern of [Ca] among cells was investigated by Moran's I, an index of spatial autocorrelation. We found that 30 μM and 50 μM AHL triggered opposing osteoblast fates. At 50 μM, AHL inhibited osteoblast differentiation by promoting mitochondrial-dependent apoptosis and negatively regulating osteogenic marker genes, including Runx2, Osterix, bone sialoprotein (Bsp), and osteocalcin (OCN). In contrast, prolonged treatment with 30 μM AHL promoted osteoblast differentiation concomitantly with cell apoptosis. The elevation of [Ca] levels in osteoblasts treated with 50 μM AHL was spatially autocorrelated, while no such phenomenon was observed in 30 μM AHL-treated osteoblasts. The blocking of cell-to-cell spatial autocorrelation in the osteoblasts provoked by 50 μM AHL significantly inhibited apoptosis and partially restored differentiation. Our observations suggest that AHL affects the fate of osteoblasts (apoptosis and differentiation) by affecting the spatial correlation of [Ca] changes. Thus, AHL acts as a double-edged sword for osteoblast function.
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.cellsig.2020.109740
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32818672; ● Search Scopus @ Elsevier (PMID): 32818672; ● Search Scopus @ Elsevier (DOI): 10.1016/j.cellsig.2020.109740

(DOI: 10.1016/j.cellsig.2020.109740, PubMed: 32818672) Yuhan He, Noriko Shiotsu, Yoko Uchida-Fukuhara, Jiajie Guo, Yao Weng, Mika Ikegame, Ziyi Wang, Kisho Ono, Hiroshi Kamioka, Yasuhiro Torii, Akira Sasaki, Kaya Yoshida and Hirohiko Okamura :
Outer membrane vesicles derived from Porphyromonas gingivalis induced cell death with disruption of tight junctions in human lung epithelial cells.,
Archives of Oral Biology, Vol.118, 104841, 2020.

(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.archoralbio.2020.104841
(文献検索サイトへのリンク): ● Summary page in Scopus @ Elsevier: 2-s2.0-85088395011

(DOI: 10.1016/j.archoralbio.2020.104841, Elsevier: Scopus) Natsumi Fujiwara, Keiji Murakami, Kaya Yoshida, Shunsuke Sakurai, Yasusei Kudo, Kazumi Ozaki, Katsuhiko Hirota, Hideki Fujii, Maiko Suzuki, Yoichiro Miyake and Hiromichi Yumoto :
Suppresive effects of 2-methacryloyloxyethyl phosphorylcholine (MPC)-polymer on the adherence of Candida species and MRSA to acrylic denture resin.,
Heliyon, Vol.6, e04211, 2020.

(徳島大学機関リポジトリ): ● Metadata: 115916
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.heliyon.2020.e04211
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32577575; ● Summary page in Scopus @ Elsevier: 2-s2.0-85086425832

(徳島大学機関リポジトリ: 115916, DOI: 10.1016/j.heliyon.2020.e04211, PubMed: 32577575, Elsevier: Scopus) Yuka Okusha, Takanori Eguchi, Manh T Tran, Chiharu Sogawa, Kaya Yoshida, Mami Itagaki, Eman A Taha, Kisho Ono, Eriko Aoyama, Hirohiko Okamura, Ken-ichi Kozaki, Stuart K Calderwood, Masaharu Takigawa and Kuniaki Okamoto :
Extracellular Vesicles Enriched With Moonlighting Metalloproteinase Are Highly Transmissive, Pro-Tumorigenic, and Trans-Activates Cellular Communication Network Factor ( CCN2/CTGF): CRISPR Against Cancer,
Cancers, Vol.12, No.(4), E881, 2020.

(要約): Matrix metalloproteinase 3 (MMP3) plays multiple roles in extracellular proteolysis as well as intracellular transcription, prompting a new definition of moonlighting metalloproteinase (MMP), according to a definition of protein moonlighting (or gene sharing), a phenomenon by which a protein can perform more than one function. Indeed, connective tissue growth factor (CTGF, aka cellular communication network factor 2 (CCN2)) is transcriptionally induced as well as cleaved by MMP3. Moreover, several members of the MMP family have been found within tumor-derived extracellular vesicles (EVs). We here investigated the roles of MMP3-rich EVs in tumor progression, molecular transmission, and gene regulation. EVs derived from a rapidly metastatic cancer cell line (LuM1) were enriched in MMP3 and a C-terminal half fragment of CCN2/CTGF. MMP3-rich, LuM1-derived EVs were disseminated to multiple organs through body fluid and were pro-tumorigenic in an allograft mouse model, which prompted us to define LuM1-EVs as oncosomes in the present study. Oncosome-derived MMP3 was transferred into recipient cell nuclei and thereby trans-activated the promoter, and induced CCN2/CTGF production in vitro. TRENDIC and other cis-elements in the promoter were essential for the oncosomal responsivity. The CRISPR/Cas9-mediated knockout of MMP3 showed significant anti-tumor effects such as the inhibition of migration and invasion of tumor cells, and a reduction in CCN2/CTGF promoter activity and fragmentations in vitro. A high expression level of MMP3 or CCN2/CTGF mRNA was prognostic and unfavorable in particular types of cancers including head and neck, lung, pancreatic, cervical, stomach, and urothelial cancers. These data newly demonstrate that oncogenic EVs-derived MMP is a transmissive trans-activator for the cellular communication network gene and promotes tumorigenesis at distant sites.
(徳島大学機関リポジトリ): ● Metadata: 115042
(出版サイトへのリンク): ● Publication site (DOI): 10.3390/cancers12040881
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32260433; ● Summary page in Scopus @ Elsevier: 2-s2.0-85083239499

(徳島大学機関リポジトリ: 115042, DOI: 10.3390/cancers12040881, PubMed: 32260433, Elsevier: Scopus) Yusuke Sumitani, Kenta Uchibe, Kaya Yoshida, Yao Weng, Jiajie Guo, Haoze Yuan, Mika Ikegame, Hiroshi Kamioka and Hirohiko Okamura :
Inhibitory effect of retinoic acid receptor agonists on in vitro chondrogenic differentiation.,
Anatomical Science International, Vol.95, No.2, 202-208, 2020.

(要約): Retinoic acid (RA), an active metabolite of vitamin A, plays pivotal roles in a wide variety of biological processes, such as body patterning, organ development, and cell differentiation and proliferation. RA signaling is mediated by nuclear retinoic acid receptors, α, β, and γ (RARα, RARβ, and RARγ). RA is a well-known regulator of cartilage and skeleton formation and RARs are also essential for skeletal growth and hypertrophic chondrocyte-specific gene expression. These important roles of RA and RARs in chondrogenesis have been widely investigated using in vivo mouse models. However, few reports are available on the function of each subtype of RARs on in vitro chondrocyte differentiation. Here, we examined the effect of specific agonists of RARs on chondrogenic differentiation of ATDC5 and C3H10T1/2 cells. Subtype-specific RAR agonists as well as RA decreased the expressions of chondrogenic differentiation marker genes and inhibited chondrogenic differentiation, which was accompanied with morphological change to spindle-shaped cells. Among RAR agonists, RARα and RARγ agonists revealed a strong inhibitory effect on chondrogenic differentiation. RARα and RARγ agonists also hampered viability of ATDC5 cells. These observations suggested that RARα and RARγ are dominant receptors of RA signaling that negatively regulate chondrogenic differentiation.
(出版サイトへのリンク): ● Publication site (DOI): 10.1007/s12565-019-00512-3
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31732869; ● Search Scopus @ Elsevier (PMID): 31732869; ● Search Scopus @ Elsevier (DOI): 10.1007/s12565-019-00512-3

(DOI: 10.1007/s12565-019-00512-3, PubMed: 31732869) Jiajie Guo, Kaya Yoshida, Mika Ikegame and Hirohiko Okamura :
Quorum sensing molecule N-(3-oxododecanoyl)-L-homoserine lactone: An all-rounder in mammalian cell modification.,
Journal of Oral Biosciences, Vol.S1349-0079, No.(20), 30001-30003, 2020.

(要約): BACKGROUND: Bacteria exhibit multi-cellular social behavior, such as biofilm formation, virulence generation, bioluminescence, or sporulation, through cell-to-cell communication involving a quorum sensing (QS) system capable of sensing species density. Pseudomonas aeruginosa (P. aeruginosa) is a ubiquitous gram-negative opportunistic pathogen that is frequently isolated from immunocompromised patients. It is particularly detected in patients with severe periodontitis and persistent endodontic infections, forcing a rethink of the role of this opportunistic pathogen in oral lesions.HIGHLIGHT: N-(3-oxododecanoyl)-L-homoserine lactone (OdDHL) is a pivotal QS molecule, which regulates numerous virulence genes in P. aeruginosa and exhibits broad biological modulation effects in mammalian cells. In this review, we highlight the diverse OdDHL-mediated apoptosis and immunomodulatory effects on host cells. The structural properties, signaling pathways, targeted genes and proteins, and intracellular metabolism of OdDHL are also discussed to clarify the interactions between P. aeruginosa and the host.CONCLUSION: The purpose of this review is to identify a valid target for quenching OdDHL, which could potentially eliminate the pathogenic effect of P. aeruginosa.
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.job.2020.01.001
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31982630; ● Summary page in Scopus @ Elsevier: 2-s2.0-85078818697

(DOI: 10.1016/j.job.2020.01.001, PubMed: 31982630, Elsevier: Scopus) Mariko Seyama, Kaya Yoshida, Kayo Yoshida, Natsumi Fujiwara, Kisho Ono, Takanori Eguchi, Hotaka Kawai, Jiajie Guo, Yao Weng, Yuan Haoze, Kenta Uchibe, Mika Ikegame, Akira Sasaki, Hitoshi Nagatsuka, Kuniaki Okamoto, Hirohiko Okamura and Kazumi Ozaki :
Outer membrane vesicles of Porphyromonas gingivalis attenuate insulin sensitivity by delivering gingipains to the liver,
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, Vol.1866, No.6, 165731, 2020.

(要約): Outer membrane vesicles (OMVs) are nanosized particles derived from the outer membrane of gram-negative bacteria. Oral bacterium Porphyromonas gingivalis (Pg) is known to be a major pathogen of periodontitis that contributes to the progression of periodontal disease by releasing OMVs. The effect of Pg OMVs on systemic diseases is still unknown. To verify whether Pg OMVs affect the progress of diabetes mellitus, we analyzed the cargo proteins of vesicles and evaluated their effect on hepatic glucose metabolism. Here, we show that Pg OMVs were equipped with Pg-derived proteases gingipains and translocated to the liver in mice. In these mice, the hepatic glycogen synthesis in response to insulin was decreased, and thus high blood glucose levels were maintained. Pg OMVs also attenuated the insulin-induced Akt/ glycogen synthase kinase-3 (GSK-3 signaling in a gingipain-dependent fashion in hepatic HepG2 cells. These results suggest that the delivery of gingipains mediated by Pg OMV elicits changes in glucose metabolisms in the liver and contributes to the progression of diabetes mellitus.
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbadis.2020.165731
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 32088316; ● Search Scopus @ Elsevier (PMID): 32088316; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbadis.2020.165731

(DOI: 10.1016/j.bbadis.2020.165731, PubMed: 32088316) Kohei Nonaka, Yukari Kajiura, Mika Bandou, Eijiro Sakamoto, Yuji Inagaki, JH Lew, Koji Naruishi, Takahisa Ikuta, Kaya Yoshida, Tesuo Kobayashi, Hiromasa Yoshie, Toshihiko Nagata and Jun-ichi Kido :
Advanced glycation end-products increase IL-6 and ICAM-1 expression via RAGE, MAPK and NF-kB pathways in human gingival fibroblasts,
Journal of Periodontal Research, Vol.53, No.3, 334-344, 2018.

(要約): Diabetes mellitus (DM) is a risk factor for periodontal diseases and may exacerbate the progression of the pathogenesis of periodontitis. Advanced glycation end-products (AGEs) cause DM complications relative to levels of glycemic control and larger amounts accumulate in the periodontal tissues of patients with periodontitis and DM. In the present study, we investigated the effects of AGEs on the expression of inflammation-related factors in human gingival fibroblasts (HGFs) to elucidate the impact of AGEs on DM-associated periodontitis. HGFs were cultured with or without AGEs. Cell viability was examined, and RNA and protein fractions were isolated from AGE-treated cells. The expression of interleukin (IL)-6, intercellular adhesion molecule-1 (ICAM-1), and the receptor for AGE (RAGE) was investigated using reverse transcription-polymerase chain reaction, quantitative real-time polymerase chain reaction and enzyme-linked immunosorbent assay, and reactive oxygen species activity was measured using a kit with 2',7'-dichlorofluorescin diacetate. Human monocytic cells (THP-1) labeled with a fluorescent reagent were co-cultured with HGFs treated with AGEs and IL-6 siRNA, and the adhesive activity of THP-1 cells to HGFs was assessed. The expression of IL-6 and ICAM-1 was examined when HGFs were pretreated with recombinant human IL-6, the siRNAs of RAGE and IL-6, and inhibitors of MAPK and NF-κB, and then cultured with and without AGEs. The phosphorylation of MAPK and NF-κB was assessed using western blotting. AGEs increased the mRNA and protein expressions of RAGE, IL-6, ICAM-1 and reactive oxygen species activity in HGFs, and promoted the adhesion of THP-1 cells to HGFs, but had no effect on cell viability until 72 hours. Recombinant human IL-6 increased ICAM-1 expression in HGFs, while the siRNAs of RAGE and IL-6 inhibited AGE-induced IL6 and ICAM1 mRNA expression, and IL-6 siRNA depressed AGE-induced THP-1 cell adhesion. AGEs increased the phosphorylation of p38 and ERK MAPKs, p65 NF-κB and IκBα, while inhibitors of p38, ERK MAPKs and NF-κB significantly decreased AGE-induced IL-6 and ICAM-1 expression. AGEs increase IL-6 and ICAM-1 expression via the RAGE, MAPK and NF-κB pathways in HGFs and may exacerbate the progression of the pathogenesis of periodontal diseases.
(キーワード): Antigens, Neoplasm / Diabetes Complications / Fibroblasts / Gingiva / Glycation End Products, Advanced / Humans / Intercellular Adhesion Molecule-1 / Interleukin-6 / MAP Kinase Signaling System / Mitogen-Activated Protein Kinase Kinases / Mitogen-Activated Protein Kinases / NF-kappa B / Periodontitis / Phosphorylation / Reactive Oxygen Species / THP-1 Cells
(徳島大学機関リポジトリ): ● Metadata: 113617
(出版サイトへのリンク): ● Publication site (DOI): 10.1111/jre.12518
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29193068; ● Summary page in Scopus @ Elsevier: 2-s2.0-85036593558

(徳島大学機関リポジトリ: 113617, DOI: 10.1111/jre.12518, PubMed: 29193068, Elsevier: Scopus) Kaya Yoshida, Jumpei Teramachi, Kenta Uchibe, Mika Ikegame, Lihong Qiu, Di Yang and Hirohiko Okamura :
Reduction of protein phosphatase 2A Ca promotes in vivo bone formation and adipocyte differentiation.,
Molecular and Cellular Endocrinology, Vol.470, 251-258, 2018.

(要約): Serine/threonine protein phosphatase 2A (PP2A) regulates diverse physiological processes such as cell cycle, growth, apoptosis, and signal transduction. Previously, we demonstrated that silencing of the α-isoform of PP2A catalytic subunit (PP2A Cα) in osteoblasts accelerated osteoblast differentiation, whereas its overexpression suppressed differentiation. In this study, we examined the role of PP2A Cα in in vivo bone formation by generating transgenic mice (PP2A-Tg), in which the dominant negative form of PP2A Cα was specifically expressed in osteoblasts. PP2A-Tg mice exhibited an increase in body weight, cortical bone mineral density, and cortical bone thickness. Interestingly, they also displayed higher amounts of adipose tissue in the bone marrow of tibiae. The co-culture study showed that PP2A Cα-knockdown osteoblasts stimulated adipocyte differentiation from undifferentiated mesenchymal cells via upregulation of the adipocyte marker genes, such as peroxisome proliferator-activated receptor γ (PPARγ) and CCAAT/enhancer binding protein α (C/EBPα). These results indicated that the reduction of PP2A Cα levels in osteoblasts promoted bone formation in vivo. Additionally, PP2A Cα in osteoblasts was also potentially involved in controlling adipocyte differentiation through a paracrine mechanism.
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.mce.2017.11.005
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 29128580; ● Summary page in Scopus @ Elsevier: 2-s2.0-85033794901

(DOI: 10.1016/j.mce.2017.11.005, PubMed: 29128580, Elsevier: Scopus) Yuka Hiroshima, Eijiro Sakamoto, Kaya Yoshida, Kaori Abe, Koji Naruishi, Takenori Yamamoto, Yasuo Shinohara, Jun-ichi Kido and Carolyn L Geczy :
Advanced glycation end-products and Porphyromonas gingivalis lipopolysaccharide increase calprotectin expression in human gingival epithelial cells.,
Journal of Cellular Biochemistry, Vol.119, No.2, 1591-1603, 2018.

(要約): Accumulation of advanced glycation end-products (AGEs) in periodontal tissues of patients with diabetes mellitus aggravates periodontitis, but the mechanisms are unknown. Calprotectin, a heterocomplex of S100A8 and S100A9 proteins, is a constitutive cytoplasmic component of healthy gingival epithelial cells. This study aimed at investigating the effects of AGE and Porphyromonas gingivalis lipopolysaccharide (PgLPS) on calprotectin expression in the human gingival epithelial cell line OBA-9. AGE and PgLPS increased the expression of S100A8 and S100A9 mRNAs, and AGE + PgLPS co-stimulation amplified their expression in OBA-9 cells. A higher concentration of calprotectin in cell lysates was also induced by stimulation with AGE and/or PgLPS. S100A8 was mainly translocated from the nucleus to the cytoplasm by AGE stimulation, while cytoplasmic localization of S100A9 was not altered following stimulation with AGE and/or PgLPS. Calprotectin was found in the cytoplasm of BSA-treated cells, but cytoplasmic and nuclear localization was observed following stimulation with AGE and/or PgLPS. AGE-induced S100A8, and S100A9 mRNA expression was partially suppressed by RAGE-specific siRNA. In contrast, PgLPS-induced S100A8 and S100A9 mRNA expression was strongly suppressed by TLR2-specific siRNA. Furthermore, the inhibition of p38, JNK MAPK, and NF-κB attenuated AGE- and PgLPS-induced S100A8 and S100A9 mRNA expression. Taken together, these results demonstrate that AGE acts in synergy with PgLPS to stimulate RAGE and TLR2 expression and activate p38, JNK MAPK, and NF-κB signaling pathways, resulting in increased activation of calprotectin (S100A8/S100A9) in human gingival epithelial cells. Our results suggest that calprotectin may be involved in the pathogenesis of diabetic periodontitis. This article is protected by copyright. All rights reserved.
(徳島大学機関リポジトリ): ● Metadata: 119200
(出版サイトへのリンク): ● Publication site (DOI): 10.1002/jcb.26319
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28771806; ● Search Scopus @ Elsevier (PMID): 28771806; ● Search Scopus @ Elsevier (DOI): 10.1002/jcb.26319

(徳島大学機関リポジトリ: 119200, DOI: 10.1002/jcb.26319, PubMed: 28771806) Kaya Yoshida, Hirohiko Okamura, Yuka Hiroshima, Kaori Abe, Jun-ichi Kido, Yasuo Shinohara and Kazumi Ozaki :
PKR induces the expression of NLRP3 by regulating the NF-κB pathway in Porphyromonas gingivalis-infected osteoblasts,
Experimental Cell Research, Vol.354, No.1, 57-64, 2017.

(要約): The double-stranded RNA-dependent kinase (PKR), which is activated by double stranded RNA, induces inflammation by regulating NF-κB signaling. The NLR family pyrin domain-containing 3 (NLRP3) inflammasome also modulates inflammation in response to infection. Porphyromonas gingivalis (P.gingivalis) is an oral bacterium which is implicated in the pathogenesis of periodontal diseases. We previously reported that PKR is a key modulator of bone metabolism and inflammation in the periodontal tissue. PKR was also reported to induce inflammation in response to microbes by regulating the NLRP3 inflammasome, suggesting that PKR could affect inflammation along with NLRP3 in periodontal diseases. In this study, we investigated the effects of PKR on NLRP3 expression and NF-κB activity in P. gingivalis infected osteoblasts. We first constructed a SNAP26b-tagged P.gingivalis (SNAP-P. g.) and traced its internalization into the cell. SNAP-P. g. increased the activity of PKR and NF-κB and also induced NLRP3 expression in osteoblasts. Inhibition of NF-κB attenuated SNAP-P. g.-induced NLRP3 expression. The knockdown of PKR using shRNA decreased both the activity of NF-κB and the expression of NLRP3 induced by SNAP-P.g.. We therefore concluded that in osteoblasts, P. gingivalis activated PKR, which in turn increased NLRP3 expression by activating NF-κB. Our results suggest that PKR modulates inflammation by regulating the expression of the NLRP3 inflammasome through the NF-κB pathway in periodontal diseases.
(キーワード): 3T3 Cells / Animals / Gene Expression Regulation / Humans / Inflammasomes / Inflammation / Mice / NF-kappa B / NLR Family, Pyrin Domain-Containing 3 Protein / Osteoblasts / Periodontal Pocket / Porphyromonas gingivalis / Receptors, G-Protein-Coupled / Signal Transduction / Transcription Factor RelA
(徳島大学機関リポジトリ): ● Metadata: 111349
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.yexcr.2017.03.028
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28341446; ● Search Scopus @ Elsevier (PMID): 28341446; ● Search Scopus @ Elsevier (DOI): 10.1016/j.yexcr.2017.03.028

(徳島大学機関リポジトリ: 111349, DOI: 10.1016/j.yexcr.2017.03.028, PubMed: 28341446) Hirohiko Okamura, Kaya Yoshida, Hiroyuki Morimoto, Jumpei Teramachi, Kazuhiko Ochiai, Tatsuji Haneji and Akihito Yamamoto :
Role of Protein Phosphatase 2A in Osteoblast Differentiation and Function.,
Journal of Clinical Medicine, Vol.6, No.3, 2017.

(要約): The reversible phosphorylation of proteins plays hugely important roles in a variety of cellular processes, such as differentiation, proliferation, and apoptosis. These processes are strictly controlled by protein kinases (phosphorylation) and phosphatases (de-phosphorylation). Here we provide a brief history of the study of protein phosphorylation, including a summary of different types of protein kinases and phosphatases. One of the most physiologically important serine/threonine phosphatases is PP2A. This review provides a description of the phenotypes of various PP2A transgenic mice and further focuses on the known functions of PP2A in bone formation, including its role in osteoblast differentiation and function. A reduction in PP2A promotes bone formation and osteoblast differentiation through the regulation of bone-related transcription factors such as Osterix. Interestingly, downregulation of PP2A also stimulates adipocyte differentiation from undifferentiated mesenchymal cells under the appropriate adipogenic differentiation conditions. In osteoblasts, PP2A is also involved in the ability to control osteoclastogenesis as well as in the proliferation and metastasis of osteosarcoma cells. Thus, PP2A is considered to be a comprehensive factor in controlling the differentiation and function of cells derived from mesenchymal cells such as osteoblasts and adipocytes.
(キーワード): 骨芽細胞 (osteoblast) / 蛋白質脱リン酸化 (protein dephosphorylation) / プロテインフォスファターゼ (protein phosphatase)
(徳島大学機関リポジトリ): ● Metadata: 117742
(出版サイトへのリンク): ● Publication site (DOI): 10.3390/jcm6030023
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 28241467; ● Search Scopus @ Elsevier (PMID): 28241467; ● Search Scopus @ Elsevier (DOI): 10.3390/jcm6030023

(徳島大学機関リポジトリ: 117742, DOI: 10.3390/jcm6030023, PubMed: 28241467) Takamura Haruna, Kaya Yoshida, Hirohiko Okamura, Natsumi Fujiwara and Kazumi Ozaki :
Porphyromonas gingivalis attenuates the insulin-induced phosphorylation and translocation of forkhead box protein O1 in human hepatocytes,
Archives of Oral Biology, Vol.69, 19-24, 2016.

(徳島大学機関リポジトリ): ● Metadata: 111993
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.archoralbio.2016.05.010
(文献検索サイトへのリンク): ● Summary page in Scopus @ Elsevier: 2-s2.0-84969142160

(徳島大学機関リポジトリ: 111993, DOI: 10.1016/j.archoralbio.2016.05.010, Elsevier: Scopus) Kaya Yoshida, Masami Yoshioka, Hirohiko Okamura, Moriyama Satomi, Kazuyoshi Kawazoe, Grenier Daniel and Daisuke Hinode :
Preventive effect of Daiokanzoto (TJ-84) on 5-fluorouracil-induced human gingival cell death through the inhibition of reactive oxygen species production,
PLoS ONE, Vol.9, No.11, e112689, 2014.

(要約): Daiokanzoto (TJ-84) is a traditional Japanese herbal medicine (Kampo formulation). While many Kampo formulations have been reported to regulate inflammation and immune responses in oral mucosa, there is no evidence to show that TJ-84 has beneficial effects on oral mucositis, a disease resulting from increased cell death induced by chemotherapeutic agents such as 5-fluorouracil (5-FU). In order to develop effective new therapeutic strategies for treating oral mucositis, we investigated (i) the mechanisms by which 5-FU induces the death of human gingival cells and (ii) the effects of TJ-84 on biological events induced by 5-FU. 5-FU-induced lactate dehydrogenase (LDH) release and pore formation in gingival cells (Sa3 cell line) resulted in cell death. Incubating the cells with 5-FU increased the expression of nucleotide-binding domain and leucine-rich repeat containing PYD-3 (NLRP3) and caspase-1. The cleavage of caspase-1 was observed in 5-FU-treated cells, which was followed by an increased secretion of interleukin (IL)-1β. The inhibition of the NLRP3 pathway slightly decreased the effects of 5-FU on cell viability and LDH release, suggesting that NLRP3 may be in part involved in 5-FU-induced cell death. TJ-84 decreased 5-FU-induced LDH release and cell death and also significantly inhibited the depolarization of mitochondria and the up-regulation of 5-FU-induced reactive oxygen species (ROS) and nitric oxide (NO) production. The transcriptional factor, nuclear factor-κB (NF-κB) was not involved in the 5-FU-induced cell death in Sa3 cells. In conclusion, we provide evidence suggesting that the increase of ROS production in mitochondria, rather than NLRP3 activation, was considered to be associated with the cell death induced by 5-FU. The results also suggested that TJ-84 may attenuate 5-FU-induced cell death through the inhibition of mitochondrial ROS production.
(出版サイトへのリンク): ● Publication site (DOI): 10.1371/journal.pone.0112689
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 25389767; ● Search Scopus @ Elsevier (PMID): 25389767; ● Search Scopus @ Elsevier (DOI): 10.1371/journal.pone.0112689

(DOI: 10.1371/journal.pone.0112689, PubMed: 25389767) Hirohiko Okamura, Di Yang, Kaya Yoshida, Jumpei Teramachi and Tatsuji Haneji :
Reduction of PP2A C stimulates adipogenesis by regulating the Wnt/GSK-3/-catenin pathway and PPAR expression,
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Vol.1843, No.11, 2376-2384, 2014.

(要約): Serine/threonine protein phosphatase 2A (PP2A) regulates several physiological processes such as the cell cycle, cell growth, apoptosis, and signal transduction. In this study, we examined the expression and role of PP2A Cα in adipocyte differentiation. PP2A Cα expression and PP2A activity decreased during adipocyte differentiation in C3H10T1/2 and 3T3-L1 cells and the expression of adipocyte marker genes such as PPARγ and adiponectin increased. To further clarify the role of PP2A Cα in adipocyte differentiation, we constructed PP2A knockdown cells by infecting C3H10T1/2 cells with a lentivirus expressing a shRNA specific for the PP2A Cα (shPP2A cells). Silencing of PP2A Cα in C3H10T1/2 cells dramatically stimulated adipocyte differentiation and lipid accumulation, which were accompanied by expression of adipocyte marker genes. Silencing of PP2A Cα suppressed Wnt10b expression and reduced the levels of the inactivated form of GSK-3β (phospho-GSK-3β), leading to the reduction of β-catenin levels in the nucleus and its transcriptional activity. Treatment with LiCl, a GSK-3β inhibitor, and inhibition of PPARγ expression suppressed the accelerated adipogenesis of shPP2A cells. Our data indicate that PP2A Cα plays an important role in the regulation of adipocyte differentiation by regulating the Wnt/GSK-3β/β-catenin pathway and PPARγ expression.
(キーワード): PP2A (PP2A) / プロテインフォスファターゼ (protein phosphatase) / 脂肪細胞 (adipocyte)
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbamcr.2014.06.008
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24949891; ● Summary page in Scopus @ Elsevier: 2-s2.0-84905178655

(DOI: 10.1016/j.bbamcr.2014.06.008, PubMed: 24949891, Elsevier: Scopus) Ishikawa Makoto, Kaya Yoshida, Hirohiko Okamura, Kazuhiko Ochiai, Takamura Haruna, Natsumi Fujiwara and Kazumi Ozaki :
Oral porphyromonas gingivalis translocates to the liver and regulates hepatic glycogen synthesis through the Akt/GSK-3b signaling pathway,
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, Vol.1832, No.12, 2035-2043, 2013.

(要約): Periodontal diseases are common chronic inflammatory disorders that result in the destruction of tissues around teeth. Many clinical studies suggest that periodontal diseases are risk factors for insulin resistance and diabetic mellitus development. However, the molecular mechanisms by which periodontal diseases regulate the progress of diabetes mellitus remain unknown. In this study, we investigated whether Porphyromonas gingivalis (P.g.), a major pathogen of periodontal diseases, present in the oral cavity, moves to the liver and affects hepatic glycogen synthesis. SNAP26b-tagged P.g. (SNAP-P.g.) was introduced into the oral cavity to induce periodontal disease in 4-week old female Balb/c mice. SNAP-P.g. was detected in the liver extracted from SNAP-P.g.-treated mice using nested PCR analysis. High blood glucose levels tended to promote SNAP-P.g. translocation from the oral cavity to the liver in mice. Periodic acid-Schiff staining suggested that hepatic glycogen synthesis decreased in SNAP-P.g.-treated mice. SNAP-P.g. was also internalized into the human hepatoma cell line HepG2, and this attenuated the phosphorylation of insulin receptor substrate (IRS)-1, Akt and glycogen synthase kinase-3β induced by insulin. Insulin-induced glycogen synthesis was suppressed by SNAP-P.g. in HepG2 cells. Our results suggest that P.g. translocation from the oral cavity to the liver may contribute to the progress of diabetes mellitus by influencing hepatic glycogenesis.
(キーワード): 歯周炎 (periodontal disease) / 糖尿病 (diabetes mellitus) / Porphyromonas gingivalis / Hepatic glycogenesis / SNAP26b
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbadis.2013.07.012
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23899607; ● Search Scopus @ Elsevier (PMID): 23899607; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbadis.2013.07.012

(DOI: 10.1016/j.bbadis.2013.07.012, PubMed: 23899607) Hirohiko Okamura, Kaya Yoshida, Di Yang and Tatsuji Haneji :
Protein phosphatase 2A Cα regulates osteoblast differentiation and the expressions of bone sialoprotein and osteocalcin via osterix transcription factor.,
Journal of Cellular Physiology, Vol.228, No.5, 1031-1037, 2013.

(要約): Serine/threonine protein phosphatase 2A (PP2A) participates in regulating many important physiological processes such as cell cycle, growth, apoptosis, and signal transduction. Osterix is a zinc-finger-containing transcription factor that is essential for osteoblast differentiation and regulation of many bone-related genes. We have recently reported that decrease in α-isoform of PP2A catalytic subunit (PP2A Cα) accelerates osteoblast differentiation through the expression of bone-related genes. In this study, we further examined the role of PP2A Cα in osteoblast differentiation by establishing the stable cell lines that overexpress PP2A Cα. Overexpression of PP2A Cα reduced alkaline phosphatase (ALP) activity. Osteoblast differentiation and mineralization were also decreased in PP2A Cα-overexpressing cells, with reduction of bone-related genes including osterix, bone sialoprotein (Bsp), and osteocalcin (OCN). Luciferase assay showed that the transcriptional activity of the Osterix promoter region was decreased in PP2A Cα-overexpressing cells. Introduction of ectopic Osterix rescued the expression of Bsp and OCN in PP2A Cα-overexpressing cells. These results indicate that PP2A Cα and its activity play a negative role in osteoblast differentiation and Osterix is a key factor responsible for regulating the expressions of Bsp and OCN during PP2A Cα-mediated osteoblast differentiation.
(キーワード): 骨芽細胞 (osteoblast) / プロテインフォスファターゼ (protein phosphatase)
(出版サイトへのリンク): ● Publication site (DOI): 10.1002/jcp.24250
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23042641; ● Search Scopus @ Elsevier (PMID): 23042641; ● Search Scopus @ Elsevier (DOI): 10.1002/jcp.24250

(DOI: 10.1002/jcp.24250, PubMed: 23042641) Hirohiko Okamura, Di Yang, Kaya Yoshida and Tatsuji Haneji :
Protein phosphatase 2A C is involved in osteoclastogenesis by regulating RANKL and OPG expression in osteoblasts.,
FEBS Letters, Vol.587, No.1, 48-53, 2013.

(要約): We examined whether alteration of PP2A Cα expression in osteoblasts is involved in osteoclast differentiation. Reduction of PP2A Cα in MC3T3-E1 cells (shPP2A) decreased receptor activator of nuclear factor κB ligand (RANKL) expression and increased osteoprotegerin (OPG) expression. The conditioned medium from shPP2A cells failed to induce NFATc1 as well as the expression of osteoclast marker genes cathepsin K and osteoclast-associated receptor (OSCAR) in bone marrow macrophage cells. Treatment of bone marrow macrophage cells with the conditioned medium from shPP2A cells impaired osteoclastogenesis. These results suggest that alteration of PP2A Cα expression in osteoblasts modulates the expressions of RANKL and OPG, which are involved in osteoclastogenesis via the NFATc1 transcription factor.
(キーワード): 骨芽細胞 (osteoblast) / プロテインフォスファターゼ (protein phosphatase) / 破骨細胞 (osteoclast)
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.febslet.2012.10.041
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23183242; ● Search Scopus @ Elsevier (PMID): 23183242; ● Search Scopus @ Elsevier (DOI): 10.1016/j.febslet.2012.10.041

(DOI: 10.1016/j.febslet.2012.10.041, PubMed: 23183242) Kaya Yoshida, Hirohiko Okamura, Kazuhiko Ochiai, Yumi Hoshimo, Tatsuji Haneji, Masami Yoshioka, Daisuke Hinode and Hideo Yoshida :
PKR plays a positive role in osteoblast differentiation by regulating GSK-3b activity through a b-catenin-independent pathway,
Molecular and Cellular Endocrinology, Vol.361, No.1-2, 99-105, 2012.

(要約): Double-stranded RNA-dependent protein kinase (PKR) is involved in various cellular functions. We previously reported that PKR regulates osteoblast differentiation, but the specific mechanisms by which this occurs remain unclear. In this study, we investigated the role of PKR in Glycogen synthase kinase 3 (GSK-3) regulation of osteoblast differentiation. Lithium chloride (LiCl), a GSK-3 inhibitor, increased GSK-3 phosphorylation in MC3T3-E1 and MG-63 cells. LiCl also inhibited Runx2 and expression of its regulated genes, causing inhibition of Alkaline phosphatase activity and mineralization. LiCl injection to the calvaria in mice suppressed bone formation. Further, GSK-3 phosphorylation was increased in osteoblasts, by Akt-independent mechanisms, in which PKR was constitutively inactivated. A PKR inhibitor, 2-aminopurine, also induced GSK-3 phosphorylation in MC3T3-E1 and MG-63 cells. Further, Runx2 and its regulated genes were inhibited in PKR-inactivated osteoblasts, and differentiation was suppressed through a -catenin-independent pathway. PKR positively regulates the differentiation of osteoblasts by mediating GSK-3 activity through a -catenin-independent pathway.
(キーワード): Animals / Cell Differentiation / Cell Line / Enzyme Activation / Glycogen Synthase Kinase 3 / Humans / Lithium Chloride / Mice / Models, Biological / Osteoblasts / Osteogenesis / Phosphorylation / Proto-Oncogene Proteins c-akt / Signal Transduction / Skull / beta Catenin / eIF-2 Kinase
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.mce.2012.03.019
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 22484461; ● Search Scopus @ Elsevier (PMID): 22484461; ● Search Scopus @ Elsevier (DOI): 10.1016/j.mce.2012.03.019

(DOI: 10.1016/j.mce.2012.03.019, PubMed: 22484461) Kaya Yoshida, Hirohiko Okamura, Yumi Hoshimo, Masayuki Shono, Masami Yoshioka, Daisuke Hinode and Hideo Yoshida :
Interaction between PKR and PACT mediated by LPS-inducible NF-kB in human gingival cells,
Journal of Cellular Biochemistry, Vol.113, 165-173, 2012.

(要約): The double-stranded RNA-dependent protein kinase (PKR) is a serine/threonine kinase expressed constitutively in mammalian cells. PKR is activated upon virus infection by double-stranded RNA (dsRNA), and plays a critical role in host antiviral defense mechanisms. PKR is also known to regulate various biological responses, including cell differentiation and apoptosis. However, whether PKR is involved in the progress of periodontitis is not clear. The present study explained the phosphorylation of PKR by LPS in the human gingival cell line, Sa3. Expression of genes encoding LPS receptors was detected in Sa3 cells and treatment of cells with 1 µg/mL LPS for 6 h caused PKR phosphorylation. LPS elevated the expression of the protein activator of PKR (PACT) mRNA and protein, followed by the enhanced association between PACT and PKR within 3 h. In addition, LPS treatment induced the translocation of NF-κB to the nucleus after 30 min, and inhibition of NF-κB decreased the PACT-PKR interaction induced by LPS. The level of pro-inflammatory cytokine mRNA, including interleukin-6 (IL-6) and tumor necrosis factor alpha (TNFα), appeared within 45 min and reached at the maximal levels by 90 min after the addition of LPS. This induction of pro-inflammatory cytokines was not affected by RNAi-mediated silencing of PKR and a pharmacological inhibitor of PKR, whereas the inhibition of NF-κB decreased it. These results indicated that LPS induces PKR phosphorylation and the PACT-PKR association in Sa3 cells. Our results also suggest that NF-κB is involved in the PACT-PKR interaction and the production of pro-inflammatory cytokines in periodontitis.
(キーワード): Apoptosis / Biological Transport / Cell Line / Gingiva / Humans / Interleukin-6 / Lipopolysaccharides / NF-kappa B / Periodontitis / Phosphorylation / RNA Interference / RNA, Double-Stranded / RNA, Small Interfering / RNA-Binding Proteins / Signal Transduction / Tumor Necrosis Factor-alpha / eIF-2 Kinase
(出版サイトへのリンク): ● Publication site (DOI): 10.1002/jcb.23340
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21882225; ● Search Scopus @ Elsevier (PMID): 21882225; ● Search Scopus @ Elsevier (DOI): 10.1002/jcb.23340

(DOI: 10.1002/jcb.23340, PubMed: 21882225) Hirohiko Okamura, Kaya Yoshida, Kazuhiko Ochiai and Tatsuji Haneji :
Reduction of protein phosphatase 2A Cα enhances bone formation and osteoblast differentiation through the expression of bone-specific transcription factor Osterix.,
Bone, Vol.49, No.3, 368-375, 2011.

(要約): The serine/threonine protein phosphatase 2A (PP2A) participates in regulating many important physiological processes such as control of cell cycle, growth, and division. On the other hand, Osterix is a zinc-finger-containing transcription factor that is essential for the differentiation of osteoblasts and regulation of many bone-related genes. Here we examined the effect of okadaic acid (OA), a specific inhibitor of PP2A, on bone formation in vivo and the molecular mechanism regulated by PP2A Cα in osteoblast differentiation. Administration of 1nM OA to the calvarial region in mice increased bone mineral density, as shown by μCT, while histomorphological analysis showed an increase in mineral apposition and bone thickness in the same region. In addition, treatment with 1nM OA stimulated osteoblast differentiation and the expression of Osterix, bone sialoprotein (Bsp), and osteocalcin (OCN) in mouse osteoblastic MC3T3-E1 cells. Moreover, the expression and phosphatase activity of PP2A Cα was decreased in the initial step of osteoblast differentiation, which was in parallel with an increase in Osterix expression. To further clarify the role of PP2A Cα in osteoblast differentiation, we constructed PP2A knock-down cells by infecting MC3T3-E1 cells with a lentivirus expressing shRNA specific for the PP2A Cα. Accordingly, the silencing of PP2A Cα in MC3T3-E1 cells dramatically increased osteoblast differentiation and mineralization, which were accompanied with expressions of Osterix, Bsp, and OCN. Our data indicate that PP2A Cα plays an important role in the regulation of bone formation and osteoblast differentiation through the bone-related genes.
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bone.2011.06.004
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21683816; ● Search Scopus @ Elsevier (PMID): 21683816; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bone.2011.06.004

(DOI: 10.1016/j.bone.2011.06.004, PubMed: 21683816) Heni Susilowati, Hirohiko Okamura, Katsuhiko Hirota, Masayuki Shono, Kaya Yoshida, Keiji Murakami, Atsushi Tabata, Hideaki Nagamune, Tatsuji Haneji and Yoichiro Miyake :
Intermedilysin induces EGR-1 expression through calcineurin/NFAT pathway in human cholangiocellular carcinoma cells.,
Biochemical and Biophysical Research Communications, Vol.404, No.1, 57-61, 2011.

(要約): (Intermedilysin (ILY) is a cholesterol-dependent cytolysin produced by Streptococcus intermedius, which is associated with human brain and liver abscesses. Although intrahepatic bile duct cells play a valuable role in the pathogenesis of liver abscess, the molecular mechanism of ILY-treated intrahepatic bile duct cells remains unknown. In this study, we report that ILY induced a nuclear accumulation of intracellular calcium ([Ca(2+)]i) in human cholangiocellular cells HuCCT1. We also demonstrate that 10 ng/ml ILY induced NFAT1 dephosphorylation and its nuclear translocation in HuCCT1 cells. In contrast to the result that ILY induced NF-B translocation in human hepatic HepG2 cells, ILY did not affect NF-B localization in HuCCT1 cells. Dephosphorylation and nuclear translocation of NFAT1 caused by ILY were prevented by [Ca(2+)]i calcium chelator, BAPTA/AM, and calcineurin inhibitors, cyclosporine A and tacrolimus. ILY induced early growth response-1 (EGR-1) expression and it was inhibited by the pre-treatment with cyclosporine A, indicating that the calcineurin/NFAT pathway was involved in EGR-1 expression in response to ILY. ILY-induced calcineurin/NFAT1 activation and sequential EGR-1 expression might be related to the pathogenesis of S. intermedius in human bile duct cells.)
(キーワード): Bacteriocins / Bile Ducts, Intrahepatic / Calcineurin / カルシウム (calcium) / Cell Line, Tumor / Cell Nucleus / Early Growth Response Protein 1 / Humans / NFATC Transcription Factors
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbrc.2010.11.057
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21094139; ● Summary page in Scopus @ Elsevier: 2-s2.0-78650872240

(DOI: 10.1016/j.bbrc.2010.11.057, PubMed: 21094139, Elsevier: Scopus) Yuji Inagaki, Kaya Yoshida, Hirofumi Ohba, Hiroyuki Seto, Jun-ichi Kido, Tatsuji Haneji and Toshihiko Nagata :
High glucose levels increase osteopontin production and pathologic calcification in rat dental pulp tissues.,
Journal of Endodontics, Vol.36, No.6, 1014-1020, 2010.

(要約): INTRODUCTION: Pulp stones are frequently formed as a pathologic calcification product in dental pulp tissues, but the pathogenesis is poorly understood. We previously found that osteopontin (OPN) was produced by dental pulp cells, and its expression was associated with formation of the pulp stone matrix. It was reported that amorphous calcification appeared in the dental pulp of diabetic patients. The aim of this study was to determine the relationship between OPN expression and pathologic calcification in rat diabetic pulp. METHODS: The effect of glucose on OPN production and alkaline phosphatase activity in cultured rat dental pulp cells (RPC-C2A) was investigated, and then dental pulp calcification and OPN expression in diabetic rats were determined and compared with those in healthy rats by histologic and immunohistochemical analyses. RESULTS: In RPC-C2A cells, biochemical analysis showed that a high concentration of glucose (50 mmol/L) increased OPN protein production and alkaline phosphatase activity 1.3-fold and 1.5-fold, respectively. Histologic observations showed more calcified particles in dental pulp tissues in diabetic than in nondiabetic rats. Moreover, a thickened layer of predentin was formed in the radicular pulp of diabetic rats. OPN was more strongly stained around the calcified particles and in the odontoblast zone under the thickened predentin in diabetic rats. CONCLUSIONS: OPN might be a key molecule involved in the increase of pathologic pulp calcifications, which are frequently observed in diabetic patients.
(キーワード): Alkaline Phosphatase / Animals / Blood Glucose / Body Weight / Cell Culture Techniques / Cell Line / Dental Pulp / Dental Pulp Calcification / Dentin / Diabetes Mellitus, Type 2 / グルコース (glucose) / Hemoglobin A, Glycosylated / Male / Odontoblasts / オステオポンティン (osteopontin) / Rats / Rats, Inbred OLETF / Rats, Long-Evans / Time Factors / Tooth Root
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.joen.2010.03.018
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20478457; ● Summary page in Scopus @ Elsevier: 2-s2.0-77955303422

(DOI: 10.1016/j.joen.2010.03.018, PubMed: 20478457, Elsevier: Scopus) Hirohiko Okamura, Kaya Yoshida and Tatsuji Haneji :
Negative regulation of TIMP1 is mediated by transcription factor TWIST1,
International Journal of Oncology, Vol.35, No.1, 181-186, 2009.

(要約): TWIST1 is involved in tumor invasion and metastasis by promoting epithelial-to-mesenchymal transition. However, the molecular target of TWIST1 involving this mechanism is poorly understood. To identify the TWIST1-regulated genes, we established the Saos-2 cells stably expressing TWIST1 gene by transfecting TWIST1 cDNA into the cells and performed a differential display approach by using annealing control primers. Here, we report that one of the genes that were down-regulated in TWIST1 expressing cells is predicted to be TIMP1. TIMP1 has been reported as the naturally occurring specific inhibitor of matrix metalloproteinases (MMPs). Overexpression of TWIST1 gene suppressed the expression of TIMP1 mRNA but had no effect on TIMP2 and MMP-2 expression, as determined by semi-quantitative RT-PCR. We showed that TWIST1 was up-regulated in SCCBHY cells, which have a strong capacity of invasion into mandibular bone compared with SCCHN cells. Our present results suggest that TWIST1 is involved in tumor invasion by regulating the expression of TIMP1.
(キーワード): Base Sequence / Bone Neoplasms / Carcinoma, Squamous Cell / Cell Line, Tumor / Down-Regulation / Gene Expression Profiling / Gene Expression Regulation, Neoplastic / Humans / Molecular Sequence Data / Mouth Neoplasms / Neoplasm Invasiveness / Nuclear Proteins / Osteosarcoma / Reverse Transcriptase Polymerase Chain Reaction / Sequence Analysis, DNA / Tissue Inhibitor of Metalloproteinase-1 / Transcription, Genetic / Transfection / Twist Transcription Factor
(出版サイトへのリンク): ● Publication site (DOI): 10.3892/ijo_00000327
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19513566; ● Search Scopus @ Elsevier (PMID): 19513566; ● Search Scopus @ Elsevier (DOI): 10.3892/ijo_00000327

(DOI: 10.3892/ijo_00000327, PubMed: 19513566) Kaya Yoshida, Hirohiko Okamura, Bruna Rabelo Amorim, Daisuke Hinode, Hideo Yoshida and Tatsuji Haneji :
PKR-mediated degradation of STAT1 regulates osteoblast differentiation,
Experimental Cell Research, Vol.315, No.12, 2105-2114, 2009.

(要約): The double-stranded RNA-dependent protein kinase (PKR) plays a critical role in various biological responses including antiviral defense, cell differentiation, apoptosis, and tumorigenesis. In this study, we investigated whether PKR could affect the post-translational modifications of STAT1 protein and whether these modifications regulate osteoblast differentiation. We demonstrated that PKR was necessary for the ubiquitination of STAT1 protein. The expressions of bone-related genes such as type I collagen, integrin binding sialoprotein, osteopontin, and osterix were suppressed in osteoblasts lacking PKR activity. In contrast, the expressions of interleukin-6 and matrix metalloproteinases 8 and 13 increased in PKR-mutated osteoblasts. The expression and degradation of STAT1 protein were regulated by PKR in a SLIM-dependent pathway. Inhibition of SLIM by RNA interference resulted in the decreased activity of Runx2 in osteoblasts. Stimulation of interleukin-6 expression and suppression of alkaline phosphatase activity were regulated through by SLIM-dependent pathway. However, expressions of bone-related genes and MMPs were regulated by SLIM-independent pathway. Our present results suggest that the aberrant accumulation of STAT1 protein induced by loss of PKR regulate osteoblast differentiation through both SLIM/STAT1-dependent and -independent pathways.
(キーワード): Adaptor Proteins, Signal Transducing / Alkaline Phosphatase / Animals / Antigens, Differentiation / Cell Differentiation / Cell Line / Interleukin-6 / LIM Domain Proteins / Metalloproteases / Mice / Osteoblasts / RNA, Messenger / STAT1 Transcription Factor / Ubiquitin-Protein Ligases / Ubiquitination / eIF-2 Kinase
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.yexcr.2009.02.003
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19230833; ● Search Scopus @ Elsevier (PMID): 19230833; ● Search Scopus @ Elsevier (DOI): 10.1016/j.yexcr.2009.02.003

(DOI: 10.1016/j.yexcr.2009.02.003, PubMed: 19230833) 伊賀弘起, 日野出大輔, 中野雅德, 吉田秀夫, 尾崎和美, 羽田勝, 吉岡昌美, 吉田賀弥, 竹内祐子, 星野由美, 松本尚子, 永田俊彦 :
徳島大学パイロット事業支援プログラム「歯科医療系学生の口腔保健・福祉体験実習による健康長寿支援」,
大学教育研究ジャーナル, Vol.6, 108-114, 2009年.

(キーワード): 口腔保健福祉 / コウクウホケンフクシ / 健康長寿支援 / ケンコウチョウジュシエン / ホスピタリティマインド / ホスピタリティマインド / oral health and welfare / oral health and welfare / health support program / health support program / hospitality mind / hospitality mind
(徳島大学機関リポジトリ): ● Metadata: 82696
(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1050282812440496128

(徳島大学機関リポジトリ: 82696, CiNii: 1050282812440496128) Hirohiko Okamura, Bruna Rabelo Amorim, Jie Wang, Kaya Yoshida and Tatsuji Haneji :
Calcineurin regulates phosphorylation satus of transcriptionfactor osterix,
Biochemical and Biophysical Research Communications, Vol.379, No.2, 440-444, 2009.

(要約): Osterix is an osteoblast-specific transcriptional factor that is essential for osteoblast differentiation and bone formation. Calcineurin regulates bone formation through modulating osteoblast differentiation. However, post-translational modification of osterix such as phosphorylation and interactions between osterix and calcineurin remains unclear. In the present study, we demonstrated that calcineurin interacted with osterix determined by immunoprecipitation assay and Western analysis. Immunocytochemical study also revealed that osterix and calcineurin were co-localized in nucleus. Deletion of calcineurin binding motif on osterix molecule disrupted osterix-calcineurin interaction. Phosphorylation status of osterix was augmented by treatment with phosphatase inhibitors, FK506 and calyculin A. In contrast, treatment of recombinant calcineurin reduced phosphorylation status of osterix. Our present study suggests that calcineurin has an important role in the function of osterix through its modification of phosphorylation.
(キーワード): osterix / phosphorylation / calcineurin
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbrc.2008.12.094
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19114031; ● Search Scopus @ Elsevier (PMID): 19114031; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrc.2008.12.094

(DOI: 10.1016/j.bbrc.2008.12.094, PubMed: 19114031) Hirohiko Okamura, Kaya Yoshida, Bruna Rabelo Amorim and Tatsuji Haneji :
Histone H1.2 is translocated to mitochondria and associates with Bak in bleomycin-induced apoptotic cells,
Journal of Cellular Biochemistry, Vol.103, No.5, 1488-1496, 2008.

(要約): Bleomycin induces single- and double-stranded breaks in DNA, with consequent mitochondrial membrane aberrations that lead to the apoptotic cell death. It is poorly understood how DNA damage-inducing apoptotic signals are transmitted to mitochondria, from which apoptotic factors are released into the cytoplasm. Here, we investigated the localization of histone H1.2 in the bleomycin-treated human squamous carcinoma SCCTF cells. The presence of DNA double-strand breaks in the bleomycin-treated cells was examined by Western analysis using antibody against phosphorylated histone H2AX (gamma-H2AX). Incubation of SCCTF cells for 48 h with 10 microM bleomycin induced apoptosis, as determined by cleavage of lamin B1 to 28 kDa fragment and DNA ladder formation. The mitochondrial permeabilization causing apoptotic feature was also detected with MitoCapture in the bleomycin-treated cells. Histone H1.2 was translocated from the nucleus to the mitochondria after treatment with bleomycin and co-localized with Bak in mitochondria. Our present results suggest that histone H1.2 plays an important role in transmitting apoptotic signals from the nucleus to the mitochondria following double-stranded breaks of DNA by bleomycin.
(キーワード): Antibiotics, Antineoplastic / Apoptosis / Bleomycin / Cell Line, Tumor / Cell Membrane Permeability / DNA Breaks, Double-Stranded / DNA Breaks, Single-Stranded / DNA Fragmentation / Histones / Humans / Laminin / Mitochondria / Mitochondrial Membranes / Protein Transport / Signal Transduction / bcl-2 Homologous Antagonist-Killer Protein
(出版サイトへのリンク): ● Publication site (DOI): 10.1002/jcb.21537
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17879944; ● Search Scopus @ Elsevier (PMID): 17879944; ● Search Scopus @ Elsevier (DOI): 10.1002/jcb.21537

(DOI: 10.1002/jcb.21537, PubMed: 17879944) Kazumi Akita, Hirohiko Okamura, Kaya Yoshida, Hiroyuki Morimoto, Hiroaki Ogawa-Iyehara and Tatsuji Haneji :
Cobalt chloride induces apoptosis and zinc chloride suppresses cobalt-induced apoptosis by bcl-2 expression in human submandibular gland HSG cells,
International Journal of Oncology, Vol.31, No.4, 923-929, 2007.

(要約): To determine the effects of cobalt chloride on human submandibular gland cells, HSG cells were exposed to various concentrations of cobalt chloride. Cobalt chloride induced cytotoxicity and cell death in HSG cells as determined by phase-contrast microscopy and WST-1 cell viability assay. By using the Hoechst 33342 staining, marked nuclear condensation and fragmentation of chromatin were observed in cobalt chloride-treated cells. Cobalt chloride induced DNA ladder formation in HSG cells in both dose- and time-dependent manner with maximal effect at a concentration of 0.5 mM and 48 h, respectively. Cobalt chloride inhibited the expression of both Bcl-2 protein and mRNA in dose- and time-dependent manner. Zinc chloride recovered the cobalt-suppressed Bcl-2 expression and protected against cobalt-induced apoptosis in HSG cells. Our results show that the pathway of the apoptosis in HSG cells is regulated by cobalt chloride and zinc chloride. Our results also indicate that cobalt-induced apoptotic steps in HSG cells are related to the production of Bcl-2 protein.
(キーワード): Antimutagenic Agents / アポトーシス (apoptosis) / Blotting, Western / Cell Nucleus / Cell Survival / Cells, Cultured / Chlorides / Cobalt / Humans / Mouthwashes / Proto-Oncogene Proteins c-bcl-2 / RNA, Messenger / Reverse Transcriptase Polymerase Chain Reaction / Salivary Ducts / Submandibular Gland / Zinc Compounds
(出版サイトへのリンク): ● Publication site (DOI): 10.3892/ijo.31.4.923
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17786326; ● Summary page in Scopus @ Elsevier: 2-s2.0-35848933016

(DOI: 10.3892/ijo.31.4.923, PubMed: 17786326, Elsevier: Scopus) Hirohiko Okamura, Kaya Yoshida, Eiko Sasaki, Lihong Qiu, Bruna Rabelo Amorim, Hiroyuki Morimoto and Tatsuji Haneji :
Expression of PTEN and Akt phosphorylation in Lippopolysacccharide-treated NIH3T3 cells,
Cell Biology International, Vol.31, No.2, 119-125, 2007.

(要約): PTEN is a tumor suppressor gene encoding a phosphatase, and it negatively regulates cell survival mediated by the phosphoinositol 3-kinase (PI3-Kinase)-Akt pathway. To elucidate PTEN expression and its effect on the PI3-kinase-Akt pathway in fibroblasts and macrophages, we investigated the expression of PTEN and the phosphorylation status of Akt in NIH3T3 and RAW264.7 cells treated with LPS. Phosphorylation of Akt was induced by LPS treatment in a dose-dependent manner in RAW264.7 cells, but not in NIH3T3 cells. LPS induced the expression of PTEN in a dose and time-dependent manner in NIH3T3 cells (0-1 microg/ml, 0-6h). However, LPS did not stimulate PTEN expression in RAW264.7 cells. These data indicate the existence of diverse mechanisms for PTEN expression and Akt activation in fibroblasts and macrophages. RNA interference using double-stranded RNA specific for the PTEN gene reduced both mRNA and protein levels of PTEN in NIH3T3 cells treated or not with LPS. The phosphorylation status of Akt in NIH3T3 cells stimulated with LPS did not change when the PTEN expression had been inhibited by RNA interference. The present results suggest that the up-regulation of PTEN expression by LPS is not involved in the activation of Akt in NIH3T3 cells. PTEN expression might be involved in the diverse inflammatory responses to LPS in fibroblasts and macrophages.
(キーワード): Animals / Fibroblasts / Gene Expression Regulation, Enzymologic / Insulin / Lipopolysaccharides / Macrophages / Mice / NIH 3T3 Cells / PTEN Phosphohydrolase / Phosphorylation / Proto-Oncogene Proteins c-akt / RNA, Small Interfering / Signal Transduction
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.cellbi.2006.09.014
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17081778; ● Search Scopus @ Elsevier (PMID): 17081778; ● Search Scopus @ Elsevier (DOI): 10.1016/j.cellbi.2006.09.014

(DOI: 10.1016/j.cellbi.2006.09.014, PubMed: 17081778) Hiroaki Tanaka, Kaya Yoshida, Hirohiko Okamura, Hiroyuki Morimoto, Toshihiko Nagata and Tatsuji Haneji :
Calyculin A induces apoptosis and stimulates phosphorylation of p65NF-κB in human osteoblastic osteosarcoma MG63 cells,
International Journal of Oncology, Vol.31, No.2, 389-396, 2007.

(要約): Previously, we reported that okadaic acid, a specific inhibitor of serine/threonine protein phosphatases, induced apoptosis in human osteoblastic cells. However, it is not clear whether calyculin A, another inhibitor of protein phosphatases, would induce apoptosis in human osteoblastic cells and if so, which mechanisms are involved and whether the phosphorylation status of NF-kappaB could be affected by the treatment with calyculin A. In this report, we demonstrate that calyculin A induced apoptosis in MG63 cells, as judged by WST-8 assay, nuclear fragmentation, and DNA ladder formation. Expression of PTEN, FasL, and FasR mRNA was stimulated by calyculin A treatment in MG63 cells. Calyculin A also enhanced the phosphorylation level of NF-kappaB, as judged from the results of Western blot analysis and an in vitro dephosphorylation assay. Western blot analysis with anti-phospho-p65NF-kappaB antibody disclosed that the NF-kappaB was phosphorylated on serine 536 in cytosol and translocated into nucleus with calyculin A-treatment. The phosphorylation status of p65NF-kappaB was further confirmed by using the phosphorylation site-mutated p65NF-kappaB gene transfected into HEK293 cells. Unlike TNF-alpha, calyculin A treatment did not degraded IkappaBalpha within 10 min, while it degraded IkappaBalpha at 2-h treatment. Our findings indicate that calyculin A elicit phosphorylation of NF-kappaB on serine 536 in MG63 cells, resulting in the translocation of phospho-NF-kappaB to the nucleus, thereby promoting transcriptional activity of NF-kappaB-related genes.
(キーワード): Apoptosis / Binding Sites / Bone Neoplasms / Cell Line, Tumor / Cell Survival / Enzyme Inhibitors / Humans / Mutation / Osteoblasts / Osteosarcoma / Oxazoles / Phosphorylation / Serine / Transcription Factor RelA / Transcription, Genetic
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17611696; ● Search Scopus @ Elsevier (PMID): 17611696

(PubMed: 17611696) Hiroyuki Morimoto, Akiko Ozaki, Hirohiko Okamura, Kaya Yoshida, Bruna Rabelo Amorim, Hiroaki Tanaka, Seiichiro Kitamura and Tatsuji Haneji :
Differntial expression of protein phosphatase type 1 isotypes and nucleolin during cell cycle arrest,
Cell Biochemistry and Function, Vol.25, No.4, 369-375, 2007.

(要約): In the present study, we examined the expression and cytolocalization of protein phosphatase type 1 (PP1) isoforms and nucleolin in human osteoblastic cell line MG63 cells at two boundaries in the cell cycle. We treated MG63 cells with hydroxyurea and nocodazole to arrest the cells at the G(1)/S and G(2)/M boundaries, respectively. As judged from the results of Western blot analysis, PP1 isoforms were expressed differently at each boundary of the cell cycle. Nucleolin was also shown to have a different expression pattern at each boundary. In the hydroxyurea-treated cells, nucleolus-like bodies were bigger in size and decreased in number compared with those in asynchronized cells. However, the subcellular localization of PP1s and nucleolin was not changed. Anti-nucleolin antibody interacted with 110-kDa and 95-kDa proteins present in asynchronized cells and in the cells treated with hydroxyurea. Treatment of the cells with nocodazole decreased the level of the 95-kDa form of nucleolin. In the nocodazole-treated cells, it was impossible to distinguish the distribution of each protein. The phosphorylation status of nucleolin in the cell cycle arrested samples was examined by 2D-IEF-PAGE followed by Western blot analysis. In the case of asynchronized cells or hydroxyurea-treated ones, nucleolin was located at a basic isoelectric point (dephosphorylated status); whereas in the G(2)/M arrest cells, the isoelectric point of nucleolin shifted to an acidic status, indicating that nucleolin was phosphorylated. The present results indicate that PP1 and nucleolin were differently expressed at G(1)/S and G(2)/M boundaries of the cell cycle and acted in a different fashion during cell-cycle progression.
(キーワード): Cell Cycle / Cells, Cultured / Cyclin B / Cyclin B1 / Cyclin D / Cyclins / Electrophoresis, Gel, Two-Dimensional / Humans / Hydroxyurea / Isoenzymes / Nocodazole / Phosphoprotein Phosphatases / Phosphoproteins / Protein Phosphatase 1 / Protein Phosphatase 2 / RNA-Binding Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1002/cbf.1300
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16329155; ● Search Scopus @ Elsevier (PMID): 16329155; ● Search Scopus @ Elsevier (DOI): 10.1002/cbf.1300

(DOI: 10.1002/cbf.1300, PubMed: 16329155) Lihong Qiu, Kaya Yoshida, Bruna Rabelo Amorim, Hirohiko Okamura and Tatsuji Haneji :
Calyculin A stimulates the expression of TNF-a mRNA via phosphorylation of Akt in mouse osteoblastic MC3T3-E1 cells,
Molecular and Cellular Endocrinology, Vol.271, No.1-2, 38-44, 2007.

(要約): Intracellular phosphatase activity has been recognized to play a central role in signal transduction. In the present study, we investigated the effects of calyculin A, an inhibitor of protein phosphatases, on the expression of TNF-alpha mRNA and the possible signaling pathways in mouse osteoblastic MC3T3-E1 cells. The result of semiquantitative RT-PCR showed that calyculin A increased the expression of TNF-alpha mRNA in MC3T3-E1 cells. Pre-treatment of LY294002 and Wortmannin, inhibitors of PI3K, inhibited the calyculin A-stimulated TNF-alpha mRNA expression. Western blot result disclosed that calyculin A increased the phosphorylation status of Akt at Ser473. However, U0126 and SB203580, specific inhibitor of MEK1/2 and p38MAPK, respectively, had no effect on calyculin A-stimulated expression of TNF-alpha mRNA. BAY11-7085 and CAPE, inhibitors of NF-kappaB activity, did not alter the calyculin A-stimulated TNF-alpha mRNA expression. Indirect immunofluorescent study confirmed that NF-kappaB was not translocated to the nucleus by calyculin A treatment. Our present results suggest that inhibition of phosphatase activity by calyculin A stimulate the phosphorylation of Akt at Ser473 by PI3K/Akt signaling pathway, resulting in the expression TNF-alpha mRNA.
(キーワード): 3T3 Cells / Animals / Enzyme Inhibitors / Mice / Mitogen-Activated Protein Kinases / NF-kappa B / Oxazoles / Phosphatidylinositol 3-Kinases / Proto-Oncogene Proteins c-akt / RNA, Messenger / Signal Transduction / Tumor Necrosis Factor-alpha
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.mce.2007.03.005
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17482757; ● Search Scopus @ Elsevier (PMID): 17482757; ● Search Scopus @ Elsevier (DOI): 10.1016/j.mce.2007.03.005

(DOI: 10.1016/j.mce.2007.03.005, PubMed: 17482757) Bruna Rabelo Amorim, Hirohiko Okamura, Kaya Yoshida, Lihong Qiu, Hiroyuki Morimoto and Tatsuji Haneji :
The transcriptional factor Osterix directly interacts with RNA helicase A,
Biochemical and Biophysical Research Communications, Vol.355, No.2, 347-351, 2007.

(要約): Osterix is an osteoblast-specific transcriptional factor, required for bone formation and osteoblast differentiation. Here, we identified new Osterix interacting factors by using matrix-assisted laser desorption ionization time-of-flight mass spectrometry. Among the candidates, RNA helicase A was identified to interact with Osterix. To determine the interaction of Osterix with RNA helicase A, immunoprecipitation assay was performed. Western analysis confirmed the association between Osterix and RNA helicase A. Immunocytochemical analysis also showed that Osterix and RNA helicase A were co-localized in HEK 293 cells. Our data suggest that RNA helicase A might be a component of Osterix regulation.
(キーワード): Amino Acid Sequence / Cell Line / Humans / Immunoprecipitation / Molecular Sequence Data / Protein Binding / RNA Helicases / Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Transcription Factors
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.bbrc.2007.01.150
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17303075; ● Search Scopus @ Elsevier (PMID): 17303075; ● Search Scopus @ Elsevier (DOI): 10.1016/j.bbrc.2007.01.150

(DOI: 10.1016/j.bbrc.2007.01.150, PubMed: 17303075) Kaya Yoshida, Hiroyuki Shinohara, (名) Suryono, Tatsuji Haneji and Toshihiko Nagata :
Arachidonic acid inhibits osteoblast differentiation through cytosolic phospholipase A2-dependent pathway.,
Oral Diseases, Vol.13, No.1, 32-39, 2007.

(要約): Arachidonic acid, a precursor of prostaglandins (PGs), is released by phospholipase A2 (PLA2) and plays an important role in biological reactions. We examined the roles of arachidonic acid on the pathway of PG synthesis and osteoblast differentiation by using clone MC3T3-E1 cells. The effect of arachidonic acid was evaluated by the measurement of alkaline phosphatase activity, cells shape, production of arachidonic acid and the expression of cyclooxygenase (COX). Arachidonic acid dose dependently decreased alkaline phosphatase activity and increased PGE2 production in MC3T3-E1 cells. The cell shape changed from polygonal to fibroblastic following treatment with arachidonic acid. These effects were recovered by the treatment of NS-398 and indomethacin. Arachidonic acid increased the expression of COX-2 mRNA and the PGE2 production. The exogenous arachidonic acid induced the release of cellular arachidonic acid in MC3T3-E1 cells. Moreover, methylarachidonyl fluorophosphonate suppressed the arachidonic acid release and the expression of COX-2 mRNA. The present results indicate that exogenous arachidonic acid stimulated the activity of PLA2, leading to the new release of membranous arachidonic acid. The amplified arachidonic acid enhanced PGE2 production by COX-2, which inhibits the differentiation of MC3T3-E1 cells. Our results provide a new insight into the molecular mechanisms by which exogenous arachidonic acid plays a role as a paracrine/autocrine amplifier of PGE2 biosynthesis by coupling with PLA2 and COX-2.
(キーワード): 3T3 Cells / Alkaline Phosphatase / Animals / Arachidonic Acid / Arachidonic Acids / 細胞分化 (cell differentiation) / Cell Shape / Clone Cells / Cyclooxygenase 2 / Cyclooxygenase 2 Inhibitors / Cyclooxygenase Inhibitors / Cytosol / Dinoprostone / Enzyme Inhibitors / Fibroblasts / Indomethacin / Mice / Nitrobenzenes / Osteoblasts / Phospholipases A / Phospholipases A2 / Phosphonic Acids / Prostaglandin-Endoperoxide Synthases / Prostaglandins / RNA, Messenger / Sulfonamides
(出版サイトへのリンク): ● Publication site (DOI): 10.1111/j.1601-0825.2006.01239.x
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17241427; ● Search Scopus @ Elsevier (PMID): 17241427; ● Search Scopus @ Elsevier (DOI): 10.1111/j.1601-0825.2006.01239.x

(DOI: 10.1111/j.1601-0825.2006.01239.x, PubMed: 17241427) Akiko Ozaki, Hiroyuki Morimoto, Hiroaki Tanaka, Hirohiko Okamura, Kaya Yoshida, Bruna Rabelo Amorim and Tatsuji Haneji :
Okadaic acid induces phosphorylation of p65NF-κB on serine 536 adn activates NF-κB transcriptional activity in human osteoblastic MG63 cells,
Journal of Cellular Biochemistry, Vol.99, No.5, 1275-1284, 2006.

(要約): Nuclear factor-kappa B (NF-kappaB) is an essential transcription factor in the control of expression of genes involved in cell growth, differentiation, inflammation, and neoplastic transformation. Previously, we reported that okadaic acid (OA), which is a specific inhibitor of serine/threonine protein phosphatases, induced apoptosis in cells of human osteosarcoma cell line MG63. However, to date, it is not clear whether the phosphorylation status of NF-kappaB could be affected by the treatment with OA. In this report, we demonstrate that treatment of MG63 cells with OA enhanced the phosphorylation level of NF-kappaB, as judged from the results of Western blot analysis and a lambda protein phosphatase dephosphorylation assay. The phosphorylation level of NF-kappaB was enhanced in both time- and dose-dependent manners. In the cells treated with 100 nM OA for 3 h, consequential translocation of NF-kappaB from the cytosol to the nucleus occurred. Western blotting experiments with an anti-phospho-p65NF-kappaB antibody disclosed that the NF-kappaB was phosphorylated on serine 536. Furthermore, OA stimulated the transcriptional activity of NF-kappaB in MG63 cells, as judged from the results of a luciferase assay. Our findings indicate that OA elicit phosphorylation of NF-kappaB on serine 536 in MG63 cells, resulting in the translocation of phospho-NF-kappaB to the nucleus, thereby promoting transcriptional activity of genes.
(キーワード): Cell Line / Enzyme Inhibitors / Humans / Okadaic Acid / Osteoblasts / Phosphorylation / Promoter Regions, Genetic / Serine / Transcription Factor RelA / Transcription, Genetic
(出版サイトへのリンク): ● Publication site (DOI): 10.1002/jcb.20873
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16795036; ● Search Scopus @ Elsevier (PMID): 16795036; ● Search Scopus @ Elsevier (DOI): 10.1002/jcb.20873

(DOI: 10.1002/jcb.20873, PubMed: 16795036) Kaya Yoshida, Hirohiko Okamura, Bruna Rabelo Amorim, Akiko Ozaki, Hiroaki Tanaka, Hiroyuki Morimoto and Tatsuji Haneji :
Double-stranded RNA-dependent protein kinase is required for bone calcification in MC3T3-E1 cells in vitro,
Experimental Cell Research, Vol.311, No.1, 117-125, 2005.

(要約): In this study, we demonstrated that double-stranded RNA-dependent protein kinase (PKR) is required for the calcification of osteoblasts via the signal transducers and activators of transcription 1alpha (STAT1alpha) signaling in vitro. A dominant-negative mutant PKR cDNA, in which the amino acid lysine at 296 was replaced with arginine and which does not have catalytic activity, was transfected into mouse osteoblastic MC3T3-E1 cells; thereby, we established cells that stably expressed the PKR mutant gene (PKR-K/R). Phosphorylation of PKR was not stimulated by polyinosic-polycytidylic acid in the mutant cells. The PKR-K/R mutant cells exhibited up-regulated cell growth and had low alkaline phosphatase (ALP) activity. The PKR-K/R mutant cells were not able to form bone nodules in vitro. In the PKR-K/R mutant cells, runt-related gene 2 (Runx2)-mediated transcription decreased compared with the levels in the control cells. The expression of STAT1alpha protein increased and the protein was translocated to the nucleus in the PKR-K/R mutant cells. When the expression of STAT1alpha protein in PKR mutant cells was suppressed using RNAi, the activity of Runx2-mediated transcription recovered to the control level. Our results indicate that PKR is a stimulator of Runx2 transcription and is a negative modulator of STAT1alpha expression. Our findings also suggest that PKR plays important roles in the differentiation and calcification of osteoblasts by modulating STAT1alpha and/or Runx2 expression.
(キーワード): Alkaline Phosphatase / Animals / Bone and Bones / Calcification, Physiologic / Cell Differentiation / Cell Nucleus / Core Binding Factor Alpha 1 Subunit / Genes, Dominant / Interferon-Stimulated Gene Factor 3 / Mice / Osteoblasts / Phosphorylation / Protein Transport / RNA, Double-Stranded / RNA, Small Interfering / Signal Transduction / Trans-Activators / Transcription, Genetic / eIF-2 Kinase
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.yexcr.2005.09.006
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16216244; ● Search Scopus @ Elsevier (PMID): 16216244; ● Search Scopus @ Elsevier (DOI): 10.1016/j.yexcr.2005.09.006

(DOI: 10.1016/j.yexcr.2005.09.006, PubMed: 16216244) Hiroyuki Morimoto, Akiko Ozaki, Hirohiko Okamura, Kaya Yoshida, Seiichiro Kitamura and Tatsuji Haneji :
Okadaic acid induces tyrosine phosphorylation of IkBa that mediated by PKR pathway in human osteoblastic MG63 cells,
Molecular and Cellular Biochemistry, Vol.276, No.1-2, 211-217, 2005.

(要約): Treatment of human osteosarcoma cell line MG 63 cells with okadaic acid stimulated phosphorylation of IkappaBalpha, as judged from the results of Western blot analysis and a lambda protein phosphatase dephosphorylation assay. The stimulated phosphorylation of IkappaBalpha was both time- and dose-dependent. The phosphorylation sites of IkappaBalpha were taken to be tyrosine residues because the anti-phospho-tyrosine antibody bound to the samples immunoprecipitated with the anti-IkappaBalpha antibody. In the cells treated with 100 nM okadaic acid consequential translocation of NF-kappaB p65 from the cytosol to the nucleus occurred. Double-stranded RNA-dependent protein kinase (PKR) is a player in the cellular antiviral response and is involved in transcriptional stimulation through activation of NF-kappaB. We investigated the functional relationship between PKR and IkappaBalpha phosphorylation by constructing MG 63 PKR K/R cells that produced a catalytically inactive mutant PKR. NF-kappaB p65 was detected in the nucleus of these cells, even in the unstimulated cells. Although IkappaBalpha was degraded phosphorylation of eIF-2 alpha, a substrate of PKR, did not occur in the mutant cells treated with okadaic acid. Our results suggest that okadaic acid-induced tyrosine phosphorylation of IkappaBalpha was mediated by PKR kinase activity, thus indicating the involvement of this kinase in the control mechanism governing the activation of NF-kappaB.
(キーワード): Cell Line, Tumor / Humans / I-kappa B Proteins / Okadaic Acid / Osteoblasts / Osteosarcoma / Phosphorylation / Phosphotyrosine / eIF-2 Kinase
(出版サイトへのリンク): ● Publication site (DOI): 10.1007/s11010-005-4440-y
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16132703; ● Search Scopus @ Elsevier (PMID): 16132703; ● Search Scopus @ Elsevier (DOI): 10.1007/s11010-005-4440-y

(DOI: 10.1007/s11010-005-4440-y, PubMed: 16132703) Hirohiko Okamura, Kaya Yoshida, Hiroyuki Morimoto and Tatsuji Haneji :
PTEN expression by Egr-1 transcription factor in calyculin A-induced apoptotic cells,
Journal of Cellular Biochemistry, Vol.94, No.1, 117-125, 2005.

(要約): PTEN is a tumor suppressor gene encoding a phosphatase that negatively regulates cell survival mediated by the PI3-kinase-Akt pathway. The gene for transcription factor EGR-1 is an early response gene essential for cellular growth, proliferation, and differentiation. Protein phosphatase inhibitors including calyculin A and okadaic acid are potent inducers of apoptosis in several cell lines; however, the molecular mechanisms underlying their action are unknown. The purpose of this study was to examine the expression of PTEN and EGR-1 and the phosphorylation status of EGR-1 and Akt in calyculin A-treated human squamous carcinoma cells (SCCTF). Phosphorylation of EGR-1 and upregulation of PTEN expression were observed to occur in SCCTF cells treated with calyculin A in time- and dose-dependent fashions. The level of phosphorylated Akt decreased as the expression of PTEN protein increased in the calyculin A-treated SCCTF cells. Calyculin A-stimulated expression of EGR-1 and PTEN might be p53 independent, because the expression of them was also detected in p53-null Saos-2 cells. RNA interference using double-stranded RNA specific for the EGR-1 gene inhibited not only EGR-1 expression but also PTEN expression in SCCTF cells treated or not with calyculin A. Calyculin A induced nuclear fragmentation and chromatin condensation in SCCTF cells. The present results suggest that the level of PTEN expression and the phosphorylation status of Akt were associated with apoptosis induced by calyculin A. These observations also support the view that EGR-1 regulates PTEN expression in the initial steps of the apoptotic pathway.
(キーワード): Apoptosis / Base Sequence / Cell Line, Tumor / DNA Primers / DNA-Binding Proteins / Down-Regulation / Early Growth Response Protein 1 / Humans / Immediate-Early Proteins / Oxazoles / PTEN Phosphohydrolase / Phosphoric Monoester Hydrolases / Phosphorylation / Transcription Factors / Tumor Suppressor Proteins
(出版サイトへのリンク): ● Publication site (DOI): 10.1002/jcb.20283
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15517593; ● Search Scopus @ Elsevier (PMID): 15517593; ● Search Scopus @ Elsevier (DOI): 10.1002/jcb.20283

(DOI: 10.1002/jcb.20283, PubMed: 15517593) Hiroyuki Morimoto, Hirohiko Okamura, Kaya Yoshida, Seiichiro Kitamura and Tatsuji Haneji :
Okadaic acid induces apoptosis through double-stranded RNA-dependent protein kinase/eukaryotic initiation factor-2a pathway in human osteoblastic MG63 cells,
The Journal of Biochemistry, Vol.136, No.4, 433-438, 2004.

(要約): Double-stranded RNA-dependent protein kinase (PKR) is a participant in the cellular antiviral response and phosphorylates the alpha-subunit of eukaryotic translation initiation factor 2alpha (eIF-2alpha) to block protein synthesis. Treatment of human osteosarcoma cell line MG63 cells with a serine and threonine protein phosphatase inhibitor, okadaic acid, at the concentration of 100 nM, but not at 20 nM, induced apoptosis. To investigate the functional relationship between phosphatases and apoptosis, we examined the phosphorylation levels of PKR and eIF-2alpha by Western blot analysis. During treatment of cells with it at the higher concentration (100 nM), okadaic acid increased the level of phosphorylated PKR in MG63 cells, this kinase phosphorylating eIF-2alpha. However, at the lower concentration (20 nM), okadaic acid did not affect the level of phosphorylated PKR. In the cells treated with 100 nM okadaic acid, activation of NF-kappaB also occurred. Even though inhibition of translation occurred simultaneously in MG63 cells, the expression of pro-apoptotic proteins Fas and Bax was not affected by 100 nM okadaic acid in these cells. We concluded that the inhibition of translation decreased anti-apoptotic protein expression, thus resulting in apoptosis. Our results also suggest that the inhibition of the protein phosphatase activity by okadaic acid induced apoptosis in MG63 cells through PKR and eIF-2alpha.
(キーワード): Apoptosis / Blotting, Western / Cell Line, Tumor / DNA / Dose-Response Relationship, Drug / Electrophoresis, Agar Gel / Electrophoresis, Polyacrylamide Gel / Eukaryotic Initiation Factor-2 / Humans / Microscopy, Phase-Contrast / NF-kappa B / Okadaic Acid / Osteoblasts / Phosphorylation / Protein Biosynthesis / Pyrazoles / Pyrimidines / Time Factors / eIF-2 Kinase
(出版サイトへのリンク): ● Publication site (DOI): 10.1093/jb/mvh144
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15625311; ● Search Scopus @ Elsevier (PMID): 15625311; ● Search Scopus @ Elsevier (DOI): 10.1093/jb/mvh144

(DOI: 10.1093/jb/mvh144, PubMed: 15625311) Hirohiko Okamura, Kaya Yoshida, Eiko Sasaki, Hiroyuki Morimoto and Tatsuji Haneji :
Transcription factor NF-Y regulates mdr1 expression through binding to inverted CCAAT sequence in drug-resistant human squamous carcinoma cells,
International Journal of Oncology, Vol.25, No.4, 1031-1037, 2004.

(要約): In this study, the expression and transcriptional regulation of the multidrug resistance-1 (MDR1) gene in multidrug-resistant SCCTF cells and -sensitive SCCKN cells derived from human squamous carcinoma were investigated. RT-PCR revealed that mdr1 mRNA was highly expressed in SCCTF cells while it was under the limit of detection in SCCKN cells. With an electrophoretic mobility shift assay using the mdr1 promoter region, a DNA-protein complex was detected strongly in SCCTF cells, but weakly in SCCKN cells. Incubation of the DNA-protein complex with an anti-NF-Y antibody caused a supershift in the migration to a position near the origin of the gel. Chromatin immunoprecipitation assay with an anti-NF-Y antibody showed that NF-Y binds to mdr1 promoter in SCCTF cells. The mdr1 promoter region including its NF-Y binding sequence was cloned into the luciferase reporter plasmid pGL3-basic vector, and this vector was used to transfect SCCTF and SCCKN cells. The luciferase assay showed that the inverted CCAAT sequence in the mdr1 promoter region is involved in the positive regulation of mdr1 promoter activity. NF-YA protein was expressed at higher levels in SCCTF cells than that in SCCKN cells. Hoechst dye staining also showed that MDR1 protein acts more effectively as an efflux pump in SCCTF cells than that in SCCKN cells.
(キーワード): Base Sequence / CCAAT-Binding Factor / Carcinoma, Squamous Cell / Cell Line, Tumor / DNA-Binding Proteins / Drug Resistance, Neoplasm / Gene Expression Regulation, Neoplastic / Genes, MDR / Humans / Molecular Sequence Data / Promoter Regions, Genetic
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15375553; ● Search Scopus @ Elsevier (PMID): 15375553

(PubMed: 15375553) Hiroyuki Morimoto, Hirohiko Okamura, Kaya Yoshida, Seiichiro Kitamura and Tatsuji Haneji :
Double-stranded RNA mediates selective gene silencing of protein phosphatase type 1 delta isoform in HEK-293 cells,
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol.19, No.4, 327-331, 2004.

(要約): The reversible phosphorylation of proteins mediates cellular signals in eukaryotic cells. RNA interference inhibits the expression of genes and proteins in a sequence-specific manner and provides a tool to study the functions of target molecules. The effect of RNA interference on protein phosphatase isoforms in HEK-293 cells was examined. Protein phosphatase 1 delta (PP1delta) sequence-specific double-stranded RNA (dsRNA) inhibited mRNA and protein expression of the PP1delta. This RNA interference did not affect the expression of lphaand gamma1 isoforms of PP1. Transfection of antisense RNA specific for PP1delta also suppressed the expression of PP1delta. It was further demonstrated by an in vitro RNA cleavage assay that extracts of HEK-293 cells catalyzed the processing of dsRNA. This cell line had much stronger mRNA expression of Dicer, an RNase III-like enzyme, than did human osteoblastic MG63 cells. The present results show that RNA interference is a useful tool to distinguish between PP1 isoforms.
(キーワード): protein phosphatases / isoform / double-stranded RNA / RNAi / HEK-293 cells / HUMAN OSTEOBLASTIC CELLS / OKADAIC ACID / RETINOBLASTOMA PROTEIN / CATALYTIC SUBUNIT / INDUCE APOPTOSIS / CARCINOMA-CELLS / MAMMALIAN-CELLS / FAS LIGAND / INTERFERENCE / EXPRESSION
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15558948; ● Search Scopus @ Elsevier (PMID): 15558948

(PubMed: 15558948) Michi Fujita, Kaho Goto, Kaya Yoshida, Hirohiko Okamura, Hiroyuki Morimoto, Shinji Kito, Jinichi Fukuda and Tatsuji Haneji :
Okadaic acid stimulates expression of Fas receptor and Fas ligand by activation of nuclear factor kappa-B in human oral squamous carcinoma cells,
Oral Oncology, Vol.40, No.2, 199-206, 2004.

(要約): In the present study, we used western blot and RT-PCR analysis to examine the expression of proteins and mRNAs of Fas receptor and Fas ligand in human oral squamous carcinoma SCC-25 cells treated with okadaic acid. Treatment with okadaic acid enhanced the expression of proteins and mRNAs of both Fas receptor and Fas ligand in SCC-25 cells. The amount of IkappaB-alpha in whole cell lysates decreased, while the level of NF-kappaB in nucleus increased, in the okadaic acid-treated cells. Okadaic acid-treatment also alters the cellular localization of NF-kappaB, from cytoplasm to nuclei. To investigate the activation of NF-kappaB in okadaic acid-treated SCC-25 cells, we performed electrophoretic mobility gel shift assay using nuclear extracts and the consensus oligonucleotide for NF-kappaB DNA binding site. The binding of nuclear proteins to the oligonucleotide of NF-kappaB increased when the cells had been treated with 20 nM okadaic acid for 4 h. We transfected the cells with pFLF1, which has the promoter region of Fas receptor gene containing NF-kappaB binding site. A luciferase reporter gene assay demonstrated that the activity in the cells transfected with pFLF1 and treated with 20 nM okadaic acid increased in a time-dependent manner and that the activity was more than three-fold over that in the control cells. Our results suggest that NF-kappaB activated at early stages in the okadaic acid-treated SCC-25 cells stimulated the promoter activity of Fas receptor in the cells leading to the apoptotic death of these cells.
(キーワード): Antigens, CD95 / Carcinoma, Squamous Cell / Enzyme Inhibitors / Fas Ligand Protein / Gene Expression Regulation, Neoplastic / Humans / I-kappa B Proteins / Ligands / Membrane Glycoproteins / NF-kappa B / Neoplasm Proteins / Okadaic Acid / Promoter Regions, Genetic / Reverse Transcriptase Polymerase Chain Reaction / Tongue Neoplasms / Transfection / Tumor Cells, Cultured
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/S1368-8375(03)00152-0
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 14693245; ● Search Scopus @ Elsevier (PMID): 14693245; ● Search Scopus @ Elsevier (DOI): 10.1016/S1368-8375(03)00152-0

(DOI: 10.1016/S1368-8375(03)00152-0, PubMed: 14693245) Eiko Sasaki, Yoshifumi Okamoto, Kaya Yoshida, Hirohiko Okamura, Katsuhide Shimizu, Fumio Nasu, Hiroyuki Morimoto and Tatsuji Haneji :
Transblot and cytochemical identification of avidin-interacting proteins in mitochondoria of cultured cells,
Histochemistry and Cell Biology, Vol.120, No.4, 327-333, 2003.

(要約): Cell lysates prepared from 3T3-L1 cells were analyzed by western blotting using the avidin-biotin complex system and anti-Bax antibody. The antibody interacted with bands of proteins with estimated molecular weights of 120, 74, 72, and 25 kDa. However, only the 25-kDa band was detected with the anti-Bax antibody when the direct immunoblotting method was used. Peroxidase-conjugated avidin interacted with the 120-, 74-, and 72-kDa bands. This interaction was not limited to 3T3-L1 cells, because peroxidase-avidin also interacted with these three proteins in MC3T3-E1, YROS, Saos-2, MG63, SCCKN, and SCCTF cells although the staining intensity was different in each cell type. Avidin-peroxidase also interacted with these three proteins in the mitochondria-containing fractions prepared from 3T3-L1 cells. FITC-streptavidin was also localized in mitochondria in the cultured cells. The localization of avidin/streptavidin-interacting proteins in mitochondria was confirmed by using double staining with FITC-streptavidin and Mito-tracker.
(キーワード): 3T3-L1 Cells / Animals / Blotting, Western / Cells, Cultured / Electrophoresis, Polyacrylamide Gel / Indicators and Reagents / Mice / Mitochondria / Mitochondrial Proteins / Proto-Oncogene Proteins / Proto-Oncogene Proteins c-bcl-2 / Streptavidin / bcl-2-Associated X Protein
(出版サイトへのリンク): ● Publication site (DOI): 10.1007/s00418-003-0572-x
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 14574588; ● Search Scopus @ Elsevier (PMID): 14574588; ● Search Scopus @ Elsevier (DOI): 10.1007/s00418-003-0572-x

(DOI: 10.1007/s00418-003-0572-x, PubMed: 14574588) Shinji Kito, Katsuhide Shimizu, Hirohiko Okamura, Kaya Yoshida, Michi Fujita, Hiroyuki Morimoto, Yasuhiro Morimoto, Takeshi Ohba and Tatsuji Haneji :
Cleavage of nucleolin and argyrophilic nucleolar organizer region associated proteins in,
Biochemical and Biophysical Research Communications, Vol.300, No.4, 950-956, 2003.

(要約): To investigate the behavior of nuclear proteins in apoptotic cells, we examined the changes in nucleolin and proteins of the nucleolar organizing region during apoptosis in human osteoblastic cell lines, Saos-2 and MG63. Apoptosis was induced by treatment of these cells with okadaic acid. Proteins prepared from apoptotic cells were subjected to Western blot analysis and a modified Western blot method using silver nitrate. The anti-nucleolin antibody recognized the 110-kDa band and the staining intensity of this band decreased in the proteins prepared from the okadaic acid-treated apoptotic cells. The additional band of an 80-kDa was also detected in the proteins prepared from the apoptotic cells. Two major silver nitrate-stained bands, 110-kDa and 37-kDa, were detected among the proteins obtained from control cells. Like the Western blot analysis, the intensity of the 110-kDa silver nitrate-staining band decreased; an 80-kDa band appeared and its staining intensity increased in the lysate from the okadaic acid-treated cells. The signal intensity of the 37-kDa protein did not change in the sample from the apoptotic cells. In a cell-free apoptotic system, the 80-kDa protein was also detected and the amount of the 110-kDa protein decreased in the extract of Saos-2 cell nuclei incubated with apoptotic cytosol. The change in nucleolin in Saos-2 cells induced to undergo apoptosis was examined by an immunocytochemical procedure using the anti-nucleolin antibody and Hoechst 33342. Nucleolin was visible as dots in nucleoli in the control cells; however, it was not detected in the cells undergoing apoptosis. The dual-exposure view of Hoechst 33342 and anti-nucleolin staining cells confirmed that nucleolin had disappeared from the apoptotic nuclei of Saos-2.
(キーワード): Apoptosis / Blotting, Western / Cell Fractionation / Cell Line / Cell Nucleolus / Cell Nucleus / Cell-Free System / DNA Fragmentation / Enzyme Inhibitors / Fluorescent Dyes / Humans / Immunohistochemistry / Nuclear Proteins / Nucleolus Organizer Region / Okadaic Acid / Osteoblasts / Phosphoproteins / RNA-Binding Proteins / Silver Nitrate
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/S0006-291X(02)02942-X
(文献検索サイトへのリンク): ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12559966; ● Search Scopus @ Elsevier (PMID): 12559966; ● Search Scopus @ Elsevier (DOI): 10.1016/S0006-291X(02)02942-X

(DOI: 10.1016/S0006-291X(02)02942-X, PubMed: 12559966) Kaya Yoshida, Hirohiko Okamura, Hiroyuki Morimoto, Toshihiko Nagata and Tatsuji Haneji :
Okadaic acid stimulates the expression of receptor activator of nuclear factor-kappa B ligand RANKL in mouse osteoblastic cells,
Biomedical Research (India), Vol.14, No.2, 126-132, 2003.

(文献検索サイトへのリンク): ● CiNii @ 国立情報学研究所 (CRID): 1573950399828180096; ● Summary page in Scopus @ Elsevier: 2-s2.0-0344099417

(CiNii: 1573950399828180096, Elsevier: Scopus) 吉田賀弥 :
アラキドン酸による骨芽細胞の分化抑制作用およびその機構解明に関する研究,
四国歯学会, Vol.16, No.1, 141-151, 2003年.

MISC

研究者総覧に該当データはありませんでした。

総説・解説

Hirohiko Okamura, Katsuhiko Hirota, Kaya Yoshida, Weng Yao, He Yuhan, Shiotsu Noriko, Ikegame Mika, Fukuhara Yoko-Uchida, Tanai Airi and Guo Jiajie :
Outer membrane vesicles of Porphyromonas gingivalis: Novel communication tool and strategy,
Japanese Dental Science Review, Vol.57, 138-146, Aug. 2021.

(徳島大学機関リポジトリ): ● Metadata: 116930
(出版サイトへのリンク): ● Publication site (DOI): 10.1016/j.jdsr.2021.07.003
(文献検索サイトへのリンク): ● Summary page in Scopus @ Elsevier: 2-s2.0-85113357654

(徳島大学機関リポジトリ: 116930, DOI: 10.1016/j.jdsr.2021.07.003, Elsevier: Scopus) Kaya Yoshida, Kayo Yoshida, Mariko Seyama, Kazumi Ozaki and Hirohiko Okamura :
Extracellular Vesicles in Periodontal Medicine: The Candidates Linking Oral Health to General Health,
Journal of Oral Health and Biosciences, Vol.33, No.1, 15-23, Jun. 2020.

(徳島大学機関リポジトリ): ● Metadata: 114869
(出版サイトへのリンク): ● Publication site (DOI): 10.20738/johb.33.1_15
(文献検索サイトへのリンク): ● Search Scopus @ Elsevier (DOI): 10.20738/johb.33.1_15

(徳島大学機関リポジトリ: 114869, DOI: 10.20738/johb.33.1_15) 吉田賀弥 :
歯周病と糖尿病の深い関係∼歯周病はどのように糖尿病を悪化させるか?∼,
いのち輝く, Vol.93, 28-29, 2020年1月. 吉田賀弥 :
旬の研究紹介歯周病と糖尿病の関連性を証明する,
医歯薬学研究部だより, No.8, 4, 2018年10月. 吉田賀弥 :
骨芽細胞の分化におけるPKRの役割について,
四国歯学会雑誌, Vol.20, No.2, 223-227, 2008年1月.

(徳島大学機関リポジトリ): ● Metadata: 109766

(徳島大学機関リポジトリ: 109766) Kaya Yoshida :
The role of double-stranded RNA-dependent protein kinase in osteoblasts,
Journal of Oral Biosciences, Vol.49, No.3, 155-162, Aug. 2007.

(出版サイトへのリンク): ● Publication site (DOI): 10.1016/S1349-0079(07)80027-2
(文献検索サイトへのリンク): ● Summary page in Scopus @ Elsevier: 2-s2.0-85010143374

(DOI: 10.1016/S1349-0079(07)80027-2, Elsevier: Scopus)

講演・発表

Kaya Yoshida :
Periodontal disease-derived Extracellular vesicles: Potential as regulator of systemic diseases,
The 3rd International Conference on Bioinformatics, Biotechnology, and Biomedical Engineering, Yogyakarta, Oct. 2020. Kaya Yoshida, Mariko Seyama, Natsumi Fujiwara, Hirohiko Okamura and Kazumi Ozaki :
The effects of outer membrane vesicles delived from Porphyromonas gingivalis on hepatic glucose metabolisms.,
International Society for ExtracellularVesicles 2019 Annual Meeting, Kyoto, Apr. 2019. Yuka Hiroshima, Eijiro Sakamoto, Kaori Abe, Kaya Yoshida, Koji Naruishi, Toshihiko Nagata, Yasuo Shinohara, Geczy Carolyn and Jun-ichi Kido :
Advanced Glycation End-Products Increase Calprotectin in Human Gingival Epithelial Cells,
The 95th General Session & Exhibition of the International Association for Dental Research (IADR), San Francisco, Mar. 2017. Kaya Yoshida, Haruna Takamura, Hirohiko Okamura, Natsumi Fujiwara and Kazumi Ozaki :
Oral porphyromonas gingivalis translocates to liver and regulates hepatic glycogen metabolisms by attenuating insulin signaling,
10 th Asian Pacific Society of Periodontology Meeting, Nara, Japan, Sep. 2013. Susilowati Heni, Hirohiko Okamura, Katsuhiko Hirota, Kaya Yoshida, Atsushi Tabata, Hideaki Nagamune, Tatsuji Haneji and Yoichiro Miyake :
Nuclear Translocation of NF-kB induced by Streptococcus intermedius intermedilysin,
International Conference of Indonesian Society for Microbiology: Recent advances of Microbiology in Health, Agriculture, Bioindustry, Surabayai, Nov. 2009. Tatsuji Haneji, Hirohiko Okamura and Kaya Yoshida :
Bleomycin-induced apoptosis and Histone H1.2,
The 9th China-Japan Joint Seminar on Histochemistry and Cytochemistry, Nanning, China, Nov. 2009. Susilowati Heni, Hirohiko Okamura, Katsuhiko Hirota, Kaya Yoshida, Keiji Murakami, Atsushi Tabata, Hideaki Nagamune, Tatsuji Haneji and Yoichiro Miyake :
The molecular mechanism for Streptococcus intermedius intermedilysin-induced cell death inhuman cholangiocellular carcinoma cells,
International Joint Symposium Frontier in Biomedical Sciences: From Genes to Applications, Yogyakarta, Nov. 2008. Bruna Rabelo Amorim, Hirohiko Okamura, Kaya Yoshida and Tatsuji Haneji :
The bone transcriptional factor Osterix interacts with RNA helicase A,
The 3rd International Symposium on ''Oral Sciences to Improve the Quality of Life'', Tokushima, Japan, Sep. 2008. Bruna Rabelo Amorim, Hirohiko Okamura, Kaya Yoshida, Jie Wang, Lihong Qiu and Tatsuji Haneji :
The transcriptional factor Osterix directly interacts with RNA helicase A,
12th International Congress on Oral Cancer, Shanghai, China, May 2008. Susilowati Heni, Hirohiko Okamura, Katsuhiko Hirota, Kaya Yoshida, Keiji Murakami, Hideaki Nagamune, Tatsuji Haneji and Yoichiro Miyake :
NFAT1 activation in intermedilysin-induced human cholangiocellular carcinoma cell HuCCT1,
The 2nd International Symposium on "The Future Direction of Oral Sciences in the 21st Century", Tokushima, Dec. 2007. Hiroaki Tanaka, Hirohiko Okamura, Kaya Yoshida, Toshihiko Nagata and Tatsuji Haneji :
Phosphorylation of p65NF-kB and degradation of IkB in Calyculin-A-induced apoptotic cells,
The 2nd international symposium on and workshop ''The Future Direction of Oral Sciences in the 21st century'' -Oral Sciences for Our Healthy Life-, Tokushima, Japan, Dec. 2007. Bruna Rabelo Amorim, Hirohiko Okamura, Kaya Yoshida and Tatsuji Haneji :
Osterix directly interacts with RNA helicase A,
The 2nd international symposium on and workshop ''The Future Direction of Oral Sciences in the 21st century'' -Oral Sciences for Our Healthy Life-, Tokushima, Japan, Dec. 2007. Hiroaki Tanaka, Kaya Yoshida, Hirohiko Okamura, Toshihiko Nagata and Tatsuji Haneji :
Phosphorylation of NF-kB in calyculin A-induced apoptotic cells,
21st International Association for Dental Research - South East Asia Division, Bali, Indonesia, Sep. 2007. Heni Susilowati, Katsuhiko Hirota, Hirohiko Okamura, Kaya Yoshida, Keiji Murakami, Atsushi Tabata, Hideaki Nagamune, Tatsuji Haneji and Yoichiro Miyake :
Intermedilysin induces cell death in HepG2 cells,
21st International Association for Dental Research - South East Asia Division, Bali, Indonesia, Sep. 2007. Bruna Rabelo Amorim, Hirohiko Okamura, Kaya Yoshida and Tatsuji Haneji :
About the protein interacting with transcriptional factor Osterix,
The 1st international symposium and workshop ''The Future Direction of Oral Sciences in the 21st century'', Awajishima, Mar. 2007. Hiroaki Tanaka, Hirohiko Okamura, Kaya Yoshida, Toshihiko Nagata and Tatsuji Haneji :
Calyculin A induces apoptosis and phosphorylation of p65NF-kB,
The 1st international symposium and workshop ''The Future Direction of Oral Sciences in the 21st century'', Awajishima, Mar. 2007. Heni Susilowati, Katsuhiko Hirota, Hirohiko Okamura, Kaya Yoshida, Keiji Murakami, Atsushi Tabata, Hideaki Nagamune, Tatsuji Haneji and Yoichiro Miyake :
The mechanisms of Intermedilysin to induce cell death on HepG2 and HuCCT1 cell lines,
The 1st international symposium and workshop ''The Future Direction of Oral Sciences in the 21st century'', Awajishima, Mar. 2007. Kaya Yoshida, Lihong Qiu, Bruna Rabelo Amorim, Hirohiko Okamura and Tatsuji Haneji :
Double-stranded RNA-dependent protein kinase is required for bone calcification in MC3T3-E1 cells in vitro,
The 7th Chinese Congress on Oral Pathology, Shenyang, China, Oct. 2006. Lihong Qiu, Kaya Yoshida, Hirohiko Okamura and Tatsuji Haneji :
Calyculin A stimulates TNF-a expression and transcriptional activity via phosphorylation of Akt in MC3T3-E1 cells,
The 7th Chinese Congress on Oral Pathology, Shenyang, China, Oct. 2006. Hirohiko Okamura, Kaya Yoshida, Lihong Qiu, Bruna Rabelo Amorim and Tatsuji Haneji :
Translocation of histone H1.2 from nucleus to mitochondoria in bleomycin-induced apoptotic cells,
The 7th Chinese Congress on Oral Pathology, Shenyang, China, Oct. 2006. Tatsuji Haneji, Kaya Yoshida, Hirohiko Okamura and Lihong Qiu :
Cleavage of nucleolin and argyrophilic nuclear organizer region associated proteins in apoptosis-induced cells,
The 7th Chinese Congress on Oral Pathology, Shenyang, China, Oct. 2006. Yuji Inagaki, Hirofumi Ohba, Hiroyuki Seto, Masumi Horibe, Kaya Yoshida, Tatsuji Haneji and Toshihiko Nagata :
Dental Pulp Calcification and Osteopontin Expression in Diabetic Rats,
International Association for Dental Research, Brisbane, Australia, Jun. 2006. Hiroyuki Morimoto, Hirohiko Okamura, Kaya Yoshida, Kikuji Yamashita, Seiichiro Kitamura and Tatsuji Haneji :
Protein phosphatase regulates apoptosis through PKR/EIF-2Éø pathway in human osteoblastic cells.,
16 th Internatinal Congress of the IFAA., Kyoto, Japan., Aug. 2004. Hiroyuki Morimoto, Hirohiko Okamura, Kaya Yoshida, Seiichiro Kitamura and Tatsuji Haneji :
Protein phosphatase regulates apoptosisi through PKR/EIF-2 pathway in human osteoblastic cells.,
Kyoto,Japan, Aug. 2004. Hirohiko Okamura, Kaya Yoshida, Hiroyuki Morimoto, Fumio Nasu and Tatsuji Haneji :
PTEN expression by EGR-1 tanscriptional factor in calyculin A-induced apoptotic cells,
The 16th International Congress of the IFAA, Kyoto, Aug. 2004. Kaya Yoshida, Hirohiko Okamura, Hiroyuki Morimoto and Tatsuji Haneji :
Potent requirement of functional double-stranded RNA-dependent protein kinase (PKR) for the activation of NF-kB by lipopolysaccaride in MC3T3-E1 cells,
The 16th International Congress of the IFAA, Kyoto, Aug. 2004. Hiroyuki Morimoto, Hirohiko Okamura, Kaya Yoshida, Kikuji Yamashita, Seiichiro Kitamura and Tatsuji Haneji :
Protein phosphatase reglates apoptosis through PKR/eIF-2 a family in human osteoblastic cells,
The 16th International Congress of the IFAA, Kyoto, Aug. 2004. Kaya Yoshida, Hiroyuki Shinohara, (名) Suryono, Tatsuji Haneji and Toshihiko Nagata :
Inhibition of osteoblastic differentiation by arachidonic acid treatment through increase of prostaglandin E2 in MC3T3-E1 cells,
The 1st Joint Meeting of the International Bone and Mineral Society, Osaka, Jun. 2003. 吉田賀弥 :
歯周病菌由来の細胞外小胞と全身疾患,
第66回歯科基礎医学会学術大会・アップデートシンポジウム5「細胞外小胞」, 2024年11月. 吉田賀弥, 廣島佑香, 髙井彩有, 生田あゆ, 吉田佳世, 尾崎和美 :
歯周病菌外膜小胞が血管透過性を亢進する機構,
第11回日本細胞外小胞学会学術集会, 2024年10月. 芽形真奈, 吉田賀弥, 高井彩有, 瀬山真莉子, 生田あゆ, 尾崎和美 :
Porphyromonas gingivalisのOuter membrane vesiclesが血管透過性に与える影響,
第67回春季日本歯周病学会学術大会, 2024年5月. 高井彩有, 吉田賀弥, 生田あゆ, 瀬山真莉子, 芽形真奈, 尾崎和美 :
Porphyromonas gingivalis由来OMVsによるアストロサイトのNLRP3インフラマソーム活性化機構,
第67回春季日本歯周病学会学術大会, 2024年5月. 高井彩有, 吉田賀弥, 濱江柚実, 宮倉よしの, 生田あゆ, 瀬山真莉子, 芽形真奈, 吉田佳世, 尾崎和美 :
要介護高齢者の認知機能と口腔機能の関係,
第 268 回徳島医学会学術集会(令和5年度冬期), 2024年3月. Jin Shengjian, 常松貴明, 堀口大吾, 毛利安宏, 卲文華, 三好圭子, 水澤典子, Hagita Hiroko, 猿棒元陽, 吉田佳世, 吉田賀弥, 藤原奈津美, 尾崎和美, 石丸直澄, 工藤保誠 :
頭頸部扁平上皮癌(HNSCC)の進行における脱ユビキチン化酵素 OTUB1 の役割,
第82回日本癌学会学術集会, 2023年9月. 吉田佳世, 吉田賀弥, 瀬山真莉子, 芽形真奈, 藤原奈津美, 水澤典子, 毛利安宏, 工藤保誠, 尾崎和美 :
歯周病原菌由来細胞外小胞を介した肺炎発症メカニズムの解明,
第66回春季日本歯周病学会学術大会, 2023年5月. 瀬山真莉子, 藤原奈津美, 高井彩有, 芽形真奈, 吉田佳世, 吉田賀弥, 尾崎和美 :
認知・口腔機能管理のためのWebシステムの可用性に関する研究,
第66回春季日本歯周病学会学術大会, 2023年5月. 木戸理恵, 廣島佑香, 木戸淳一, 吉田賀弥, 生田貴久, 湯本浩通 :
人工合成したSecretory leukocyte protease inhibitorの抗菌活性とリポソーム封入,
第66回春季日本歯周病学会学術大会, 2023年5月. 瀬山真莉子, 藤原奈津美, 高井彩有, 芽形真奈, 吉田佳世, 吉田賀弥, 尾崎和美 :
認知機能評価Webシステムの有用性に関する研究,
第20回日本口腔ケア学会/第3回国際口腔ケア総会・学術大会, 2023年4月. Jin Shengjian, Takaaki Tsunematsu, Taigo Horiguchi, Yasuhiro Mouri, Wenhua Shao, Keiko Miyoshi, Noriko Mizusawa, Hiroko Hagita, YOSHIDA Kayo, Kaya Yoshida, Natsumi Fujiwara, Kazumi Ozaki, Naozumi Ishimaru and Yasusei Kudo :
The role of Deubiquitinating enzyme, OTUB1 in head and neck squamous cell carcinoma (HNSCC) progression,
第61回四国歯学会, Mar. 2023. 吉田賀弥 :
歯科衛生士養成課程における解剖教育,
第128回日本解剖学会総会・全国学術集会,指定シンポジウム SB7, 2023年3月. 吉田佳世, 吉田賀弥, 瀬山真莉子, 尾崎和美 :
歯周病原菌の外膜小胞がもたらすアルツハイマー型認知症発症機構の解明,
第64回歯科基礎医学会学術大会プログラム・抄録集, 263, 2022年9月. 木戸淳一, 廣島佑香, 木戸理恵, 吉田賀弥, 稲垣裕司, 成石浩司, 湯本浩通 :
人工合成したβ-defensin 2によるPorphyromonas gingivalisの付着抑制およびリポソーム封入と口腔上皮細胞への送達,
四国歯学会第60回例会, 2022年6月. 木戸淳一, 廣島佑香, 木戸理恵, 吉田賀弥, 稲垣裕司, 成石浩司, 湯本浩通 :
人工合成したbeta-defensin 2によるPorphyromonas gingivalisの付着抑制およびリポソーム封入と口腔上皮細胞への送達,
第65回春季日本歯周病学会学術大会, 2022年6月. 木戸淳一, 廣島佑香, 木戸理恵, 吉田賀弥, 稲垣裕司, 成石浩司, 湯本浩通 :
リポソームに封入したリポカリン2の口腔上皮細胞への送達,
第64回春季日本歯周病学会学術大会, 2021年5月. 吉田佳世, 吉田賀弥, 瀬山真莉子, 尾崎和美 :
歯周病原菌感染マクロファージの細胞外小胞が肺に線維化を誘導する可能性の検証,
第62回秋季日本歯周病学会学術大会, 2020年10月. 吉田賀弥, 岡村裕彦 :
歯周病原菌-マクロファージ間コミュニケーションに起因する全身疾患発症機構,
第62回日本歯科基礎医学会学術大会・アップデートシンポジウム05, 2020年9月21日(鹿児島市), 2020年9月. 廣島佑香, 木戸淳一, 木戸理恵, 吉田賀弥, 稲垣裕司, 成石浩司, 湯本浩通 :
オーラルケアへの応用に関連するリポソームのデリバリー法の検討,
第63回春季日本歯周病学会学術大会, 2020年5月. 廣島佑香, 木戸淳一, 木戸理恵, 吉田賀弥, 稲垣裕司, 成石浩司, 湯本浩通 :
オーラルケアへの応用を目指した抗菌ペプチド合成とリポソーム封入,
第62回秋季日本歯周病学会学術大会, 2019年10月. 吉田賀弥, 吉田佳世, 尾崎和美, 岡村裕彦 :
Porphyromonas gingivalis感染マクロファージの細胞外小胞が多臓器に及ぼす影響,
第6回日本細胞外小胞学会, 2019年10月. 吉田賀弥 :
歯周病原菌感染マクロファージが放出する膜小胞の臓器移行とその障害性について,
四国歯学会第38回総会, 2019年9月. 吉田賀弥, 吉田佳世, 藤原奈津美, 尾崎和美, 岡村裕彦 :
感染マクロファージの膜小胞は歯周病関連疾患発症に関与するか?,
第38回分子病理学研究会淡路島シンポジウム, 2019年7月. 木戸理恵, 廣島佑香, 生田貴久, 吉田賀弥, 稲垣裕司, 成石浩司, 尾崎和美, 木戸淳一, 湯本浩通 :
最終糖化産物はヒト口腔上皮細胞のリポカリン2発現を増加する,
第62回春季日本歯周病学会学術大会, 2019年5月. 吉田賀弥, 瀬山真莉子, 藤原奈津美, 尾崎和美 :
Porphyromonas gingivalis感染したマクロファージが由来の膜小胞が肝臓糖代謝に及ぼす影響,
第61回秋季日本歯周病学会学術大会 2018年10月26日(大阪市), Vol.60, 115, 2018年10月. 吉田賀弥, 藤原奈津美, 尾崎和美, 内部健太, 池亀美華, 岡村裕彦 :
Porphyromonas gingivalis感染したマクロファージが産生する膜小胞が肝臓糖代謝に及ぼす影響,
第60回日本歯科基礎医学会学術大会 2018年9月5-7日(九州大学病院キャンパス百年講堂, 福岡市), 2018年9月. 藤原奈津美, 村上圭史, 吉田賀弥, 工藤保誠, 弘田克彦, 尾崎和美, 藤猪英樹, 湯本浩通 :
MPCポリマーコーティングによる義歯用レジンのカンジダ付着(撥菌)効果,
第60回日本歯科基礎医学会学術大会 2018年9月5-7日(九州大学病院キャンパス百年講堂, 福岡市), 2018年9月. Kaya Yoshida, Natsumi Fujiwara, Kazumi Ozaki, 内部健太, 池亀美華 and Hirohiko Okamura :
Extracellular vesicles from Porphyromonas gingivalis-infected macrophages include histone proteins and translocate to the liver,
第10回日本RNAi研究会・第5回日本細胞外小胞学会 (グランドプリンスホテル広島・広島市), Aug. 2018.

(キーワード): 骨芽細胞 (osteoblast)

瀬山真莉子, 吉田賀弥, 藤原奈津美, 尾崎和美 :
Porphyromonas gingivalisの分泌小胞は肝臓の糖代謝に影響を与える,
第61回日本歯周病学会学術大会, Vol.60, 128, 2018年6月. 木目隆大, 内部健太, 池亀美華, 吉田賀弥, 岡村裕彦 :
ヒストン脱メチル化酵素Jmjd3は転写調節因子Runx2とOsterixを介して骨芽細胞分化を制御する,
第123回日本解剖学会総会・全国学術集会, 2018年3月. 岡村裕彦, 吉田賀弥, 内部健太, 池亀美華 :
骨芽細胞の分化におけるプロテインホスファターゼPP2A Caの役割とその標的因子,
第59回歯科基礎医学会学術大会, 2017年9月. 廣島佑香, 木戸淳一, 坂本英次郎, 阿部佳織, 吉田賀弥, 永田俊彦, 篠原康雄 :
最終糖化産物はヒト歯肉上皮細胞におけるS100A8およびS100A9発現を上昇する,
第59回秋季日本歯周病学会学術大会, 2016年10月. 吉田賀弥, 岡村裕彦 :
PKRは骨芽細胞においてPorphylomonas gingivalisが誘導するNLRP3発現をNF-kB経路を介して制御する,
第58回歯科基礎医学会学術大会, 2016年8月24-26日, 札幌コンベンションセンター(札幌市), 2016年8月. 廣島佑香, 木戸淳一, 吉田賀弥, 阿部佳織, 篠原康雄, 永田俊彦 :
低酸素環境はヒト口腔上皮細胞におけるS100A8発現を抑制する,
第59回春季日本歯周病学会学術大会, 2016年5月. 吉田賀弥, 藤原奈津美, 廣島佑香, 阿部佳織, 木戸淳一, 尾崎和美 :
Porphyromonas gingivalisはSOCS3やIRS-1を制御して肝臓におけるインスリンシグナルを抑制する,
第59回春季日本歯周病学会学術大会, 2016年5月. 中江弘美, 薮内さつき, 藤原奈津美, 柳沢志津子, 吉岡昌美, 吉田賀弥, 竹内祐子, 渡辺朱理, 土井登紀子, 松山美和, 伊賀弘起, 尾崎和美, 日野出大輔, 中野雅德, 白山靖彦 :
健口体操ポスターを活用した口腔機能向上の取り組み,
第13回日本口腔ケア学会総会・学術大会, 2016年4月. Kaya Yoshida, Hirohiko Okamura and Kazumi Ozaki :
PKRやインフラマソームがP. gingivalisを感染させた骨芽細胞において骨吸収に関連する因子の発現に与える影響,
第57回歯科基礎医学会学術大会, Sep. 2015. 薮内さつき, 中江弘美, 日野出大輔, 竹内祐子, 伊賀弘起, 尾崎和美, 白山靖彦, 松山美和, 柳沢志津子, 吉岡昌美, 吉田賀弥, 藤原奈津美, 渡辺朱理, 土井登紀子, 中野雅德, 河野文昭, 吉本勝彦 :
地域育成型歯学教育プログラムの評価(第2報)地域福祉体験学習における教育効果の変化,
平成26年度FD推進プログラム大学教育カンファレンスin徳島, 62-63, 2014年12月. 吉田賀弥, 吉岡昌美, 岡村裕彦, 日野出大輔 :
大黄甘草湯は活性酸素やインフラマソームを介して5-fluorouracilが誘導する細胞死を改善させる,
第56回歯科基礎医学会学術大会・総会, 2014年9月. 石川真琴, 吉田賀弥, 藤原奈津美, 細川義隆, 細川育子, 尾崎和美 :
歯周病原性細菌Porphyromonas gingivalis感染が肝臓糖代謝に及ぼす影響,
日本歯科保存学雑誌, 155, 2012年11月. 尾崎和美, 那賀川明美, 中野雅德, 白山靖彦, 松山美和, 日野出大輔, 羽田勝, 吉岡昌美, 中道敦子, 吉田賀弥, 竹内祐子, 星野由美, 藤原奈津美, 中江弘美, 薮内さつき, 伊賀弘起, 河野文昭, 市川哲雄 :
社会福祉施設での訪問口腔ケアを支援する包括ケア型地域ICTシステムについて,
第22回日本歯科医学会総会プログラム・事前抄録集, 163, 2012年11月. 吉田賀弥, 岡村裕彦 :
ヒト歯肉においてLPSはNF-kB経路依存的にPACTとPKRの結合を促進する,
第53回歯科基礎医学会学術大会, 2011年10月. 吉田賀弥, 岡村裕彦, 星野由美, 吉岡昌美, 日野出大輔 :
GSK-3bを介したPKRの骨芽細胞分化調節機構について,
第29回日本骨代謝学会学術集会, 2011年7月. 薮内さつき, 中江弘美, 日野出大輔, 竹内祐子, 伊賀弘起, 中野雅德, 吉田秀夫, 羽田勝, 尾崎和美, 吉岡昌美, 吉田賀弥, 中道敦子, 星野由美, 藤原奈津美, 河野文昭, 吉本勝彦 :
徳島大学教育GP「高齢社会を担う地域育成型歯学教育」授業アンケートから考察される教育効果,
平成22年度全学FD大学教育カンファレンス in 徳島, 2011年1月. 羽地達次, 寺町順平, 岡村裕彦, 吉田賀弥, 森本景之 :
PKR変異型骨芽細胞株における蛋白質脱リン酸化酵素阻害剤によるアポトーシス誘導とIkBの発現,
第51回歯科基礎医学会総会, 2009年9月. 羽地達次, 田中宏明, 岡村裕彦, 吉田賀弥, 森本景之 :
カリクリンAによるMG63細胞のアポトーシス誘導，I-kBの分解，NF-kBのリン酸化,
日本Cell Death学会第18回学術集会, 2009年8月. 日野出大輔, 竹内祐子, 伊賀弘起, 中野雅德, 吉田秀夫, 羽田勝, 尾崎和美, 吉岡昌美, 吉田賀弥, 星野由美, 松本尚子, 河野文昭, 吉本勝彦 :
高齢社会を担う地域育成型歯学教育 -初年次教育における達成課題-,
平成20年度全学FD 徳島大学教育カンファレンス, 2009年1月. 吉田賀弥, 岡村裕彦, 羽地達次 :
ブレオマイシン誘導アポトーシス細胞におけるヒストンH1.2とBakの細胞内局在,
第49回日本組織細胞化学会総会・学術集会, 2008年10月. 吉田賀弥, 岡村裕彦, 羽地達次 :
骨芽細胞の分化における蛋白質リン酸化と脱リン酸化,
第49回日本組織細胞化学会総会・学術集会, 2008年10月. 弘田克彦, 岡村裕彦, 吉田賀弥, 羽地達次, 三宅洋一郎 :
Streptococcus intermediusが誘導するヒト胆管上皮細胞死の分子機構の解明,
第50回歯科基礎医学会学術大会, 2008年9月. 岡村裕彦, 吉田賀弥, Bruna Rabelo Amorim, 羽地達次 :
転写因子TWISTの標的因子の探索と扁平上皮癌細胞における発現,
第50回歯科基礎医学会総会, 2008年9月. 吉田賀弥, 岡村裕彦, 羽地達次 :
PKR によるSTAT1 の発現調節機構の解明,
第50回歯科基礎医学会総会, 2008年9月. 岡村裕彦, 吉田賀弥, Bruna Rabelo Amorim :
転写因子TWISTの標的因子の探索と扁平上皮癌細胞における発現,
第50回歯科基礎医学会総会, 2008年9月. 弘田克彦, Heni Susilowati, 岡村裕彦, 吉田賀弥, 田端厚之, 鹿山鎭男, 湯本浩通, 羽地達次, 長宗秀明, 小野恒子, 三宅洋一郎 :
Intermedilysinにより誘導されるカルシウム振動と胆管上皮細胞死,
第17回Lancefielfレンサ球菌研究会 2008, 2008年7月. 星野由美, 尾崎和美, 松本尚子, 吉田賀弥, 吉岡昌美, 竹内祐子, 吉田秀夫, 日野出大輔, 中野雅德, 伊賀弘起, 羽田勝 :
歯科衛生士教育の4年生教育に関するニーズ,
第2回日本衛生士教育学術大会, 2007年11月. 岡村裕彦, 吉田賀弥, アモリンハベロブルーナ, 羽地達次 :
ブレオマイシン誘導アポトーシスとヒストンH1.2の細胞内局在変化,
日本解剖学会第62回中国，四国地方会, 2007年10月. 田中宏明, 吉田賀弥, 岡村裕彦, 吉澤尚樹, 羽地達次 :
蛋白質脱リン酸化酵素阻害剤カリクリンAによるアポトーシス誘導とNF-kBのリン酸化,
日本解剖学会第62回中国，四国地方会, 2007年10月. 弘田克彦, 岡村裕彦, 吉田賀弥, 羽地達次, 三宅洋一郎 :
Intermedilysin が誘導する非アポトーシス型細胞死の分子機構の解明,
第49 回歯科基礎医学会総会, 2007年8月. 田中宏明, 岡村裕彦, 吉田賀弥, 永田俊彦, 羽地達次 :
カリクリンA 誘導アポトーシス細胞によおけるIkB の分解とNF-kB のリン酸化,
第49 回歯科基礎医学会総会, 2007年8月. Bruna Rabelo Amorim, Hirohiko Okamura, Kaya Yoshida and Tatsuji Haneji :
The transcriptional factor Osterix directly interacts with RNA helicase A in HEK 293 cells,
The 49th Annual Meeting of Japanese Association for Oral Biology, Aug. 2007. 吉田賀弥, 岡村裕彦, 羽地達次 :
PKR がSTAT1の発現や機能に及ぼす影響について,
第49回歯科基礎医学会総会, 2007年8月. 岡村裕彦, 吉田賀弥, 羽地達次 :
GeneFishing法による転写因子TWISTの標的遺伝子探索,
第49回歯科基礎医学会総会, 2007年8月. 岡村裕彦, 吉田賀弥, 羽地達次 :
骨芽細胞におけるプロテインフォスファターゼの発現と機能,
第49回歯科基礎医学会総会 -サテライトシンポジウムー, 2007年8月. 田中宏明, 吉田賀弥, 岡村裕彦, 羽地達次 :
カリクリンAによるMG63細胞のアポトーシスとNF-kBのリン酸化,
第26回分子病理研究会 -湘南シンホシウムー, 2007年6月. 田中宏明, 岡村裕彦, 吉田賀弥, 羽地達次 :
蛋白質脱リン酸化酵素阻害剤カリクリンAによるアポトーシス誘導とNF-kBのリン酸化,
第112回日本解剖学会総会, 2007年3月. 森本景之, 西野朋子, 佐藤永洋, 岡村裕彦, 吉田賀弥, 羽地達次, 土肥良秋 :
蛋白質脱リン酸化酵素阻害剤によるアポトーシス誘導機序の解明,
日本顕微鏡学会第48回九州地方会, 2006年12月. 田中宏明, 岡村裕彦, 吉田賀弥, 尾崎明子, Bruna Rabelo Amorim, 羽地達次 :
蛋白質脱リン酸化酵素阻害剤カリクリンAとオカダ酸によるNF-kBのリン酸化,
日本解剖学会第61回中国，四国地方会, 2006年11月. Bruna Rabelo Amorim, Hirohiko Okamura, Kaya Yoshida and Tatsuji Haneji :
PKR mediates osterix expression in IGF-1 treated MC3T3-E1 cells,
日本解剖学会第61回中国，四国地方会, Nov. 2006. 森本景之, 西野朋子, 土肥良秋, 岡村裕彦, 吉田賀弥, 羽地達次 :
軟骨細胞の分化過程におけるPKRとSTATの発現,
日本解剖学会第62回九州地方会, 2006年10月. 弘田克彦, 岡村裕彦, 吉田賀弥, 羽地達次, 三宅洋一郎 :
IntermedilysinによるHucCT1細胞核抗原の異所性表出,
第48回歯科基礎医学会学術大会, 2006年9月. 弘田克彦, 岡村裕彦, 吉田賀弥, 羽地達次, 三宅洋一郎 :
Intermedilysin によるHuCCT1 細胞核抗原の異所性表出,
第48回歯科基礎医学会総会, 2006年9月. 岡村裕彦, 吉田賀弥, アモリンハベロブルーナ, 森本景之, 羽地達次 :
ブレオマイシン誘導アポトーシス細胞におけるヒストンH1.2とBak,
第48回歯科基礎医学会総会, 2006年9月. 吉田賀弥, 岡村裕彦, アモリンハベロブルーナ, 森本景之, 羽地達次 :
PKR変異型骨芽細胞株におけるRunx2の発現について,
第48回歯科基礎医学会総会, 2006年9月. 森本景之, 西野朋子, 土肥良秋, 岡村裕彦, 吉田賀弥, 羽地達次 :
軟骨細胞分化ににおけるPKRの役割,
第48回歯科基礎医学会総会, 2006年9月. 森本景之, 尾崎明子, 岡村裕彦, 吉田賀弥, 羽地達次, 西野朋子, 土肥良秋 :
蛋白質脱リン酸化酵素阻害剤カリクリンAとオカダ酸によるNF-kBのリン酸化,
第38回日本臨床分子形態学会総会, 2006年9月. 稲垣裕司, 大場博史, 瀬戸浩行, 堀部ますみ, 吉田賀弥, 永田俊彦 :
2型糖尿病モデルラットにおける歯髄内石灰化物形成とオステオポンチンの関与,
第124回春季日本歯科保存学会学術大会, 2006年5月. 吉田賀弥, Bruna Rabelo Amorim, 尾崎明子, 岡村裕彦, 田中宏明, 森本景之, 羽地達次 :
骨芽細胞の分化と石灰化におけるPKRの役割について,
日本解剖学会第60回中国，四国地方会, 2005年10月. 吉田賀弥, Bruna Rabelo Amorim, 尾崎明子, 岡村裕彦, 田中宏明, 森本景之, 羽地達次 :
PKRが骨の石灰化に及ぼす影響,
第47回歯科基礎医学会総会, 2005年9月. 森本景之, 尾崎明子, 岡村裕彦, 吉田賀弥, Bruna Rabelo Amorim, 山下菊治, 北村清一郎, 羽地達次 :
蛋白質脱リン酸化酵素阻害剤によるXIAPの発現とアポトーシス,
第47回歯科基礎医学会総会, 2005年9月. 尾崎明子, 森本景之, 田中宏明, 岡村裕彦, 吉田賀弥, Bruna Rabelo Amorim, 羽地達次 :
オカダ酸によるNF-kBのリン酸化とリン酸化部位の同定,
第47回歯科基礎医学会総会, 2005年9月. 岡村裕彦, 吉田賀弥, 森本景之, 尾崎明子, 田中宏明, Bruna Rabelo Amorim, 那須史男, 羽地達次 :
ブレオマイシン誘導アポトーシスとH1.2,
第47回歯科基礎医学会総会, 2005年9月. 田中宏明, 岡村裕彦, 弘田克彦, 尾崎明子, Bruna Rabelo Amorim, 吉田賀弥, 長宗秀明, 三宅洋一郎, 永田俊彦, 羽地達次 :
Streptococcus Intermedius由来毒素intermedilysin処理細胞におけるPTEN, Akt, 及びPDK-1の発現,
第47回歯科基礎医学会総会, 2005年9月. 森本景之, 尾崎明子, 岡村裕彦, 吉田賀弥, 山下菊治, 北村清一郎, 羽地達次 :
蛋白質脱リン酸化酵素1型アイソフォーム特異的RNAiとヒトDicer遺伝子変異体の同定．,
第110回日本解剖学会総会・全国学術集会., 2005年3月. 岡村裕彦, 吉田賀弥, 森本景之, 尾崎明子, 田中宏明, 羽地達次 :
LPS刺激によるPTENの発現とAktのリン酸化,
第110回日本解剖学会総会, 2005年3月. 森本景之, 尾崎明子, 岡村裕彦, 吉田賀弥, 山下菊治, 北村清一郎, 羽地達次 :
蛋白質脱リン酸化酵素1型アイソフォーム特異的RNAiとヒトDicer遺伝子変異体の同定,
第110回日本解剖学会総会, 2005年3月. 吉田賀弥, Bruna Rabelo Amorim, 尾崎明子, 岡村裕彦, 森本景之, 羽地達次 :
骨芽細胞分化におけるPKRの役割について,
第110回日本解剖学会総会, 2005年3月. 尾崎明子, 森本景之, 田中宏明, 岡村裕彦, 吉田賀弥, Bruna Rabelo Amorim, 羽地達次 :
オカダ酸処理細胞における NF-kB のリン酸化,
第110回日本解剖学会総会, 2005年3月. 田中宏明, 岡村裕彦, 尾崎明子, 吉田賀弥, 森本景之, 羽地達次 :
カリクリンA誘導アポトーシス細胞におけるPTENとAktの発現,
第110回日本解剖学会総会, 2005年3月. 尾崎明子, 森本景之, 田中宏明, 岡村裕彦, 吉田賀弥, 羽地達次 :
オカダ酸処理細胞におけるNF-kBのリン酸化,
第59回日本解剖学会中国，四国地方会, 2004年11月. 森本景之, 尾崎明子, 岡村裕彦, 吉田賀弥, 山下菊治, 北村清一郎, 羽地達次 :
蛋白脱リン酸化酵素剤によるIkB/NF-kBの調節,
第46回歯科基礎医学会学術大会ならびに総会, 2004年9月. 吉田賀弥, 岡村裕彦, 尾崎明子, 森本景之, 羽地達次 :
骨芽細胞の分化におけるPKRの役割について,
第46回歯科基礎医学会総会, 2004年9月. 岡村裕彦, 吉田賀弥, 森本景之, 田中宏明, 羽地達次 :
LPS処理線維芽細胞におけるPTENの発現とAktのリン酸化,
第46回歯科基礎医学会総会, 2004年9月. 森本景之, 尾崎明子, 岡村裕彦, 吉田賀弥, 山下菊治, 北村清一郎, 羽地達次 :
蛋白質脱リン酸化酵素阻害によるIkB/NF-kBの調節,
第46回歯科基礎医学総会, 2004年9月. 森本景之, 岡村裕彦, 吉田賀弥, 山下菊治, 北村清一郎, 羽地達次 :
蛋白質脱リン酸化酵素阻害によるアポトーシス誘導機構,
第45回歯科基礎医学会総会, 2003年9月. 吉田賀弥, 永田俊彦, 羽地達次 :
アラキドン酸がプロスタグランジンE2合成経路に与える影響について,
第45回歯科基礎医学会総会, 2003年9月. 岡村裕彦, 森本景之, 吉田賀弥, 清水克英, 羽地達次 :
カリクリンA処理扁平上皮癌細胞におけるEgr-1およびPTENの発現,
第45回歯科基礎医学会総会, 2003年9月. 森本景之, 岡村裕彦, 吉田賀弥, 北村清一郎, 羽地達次 :
フォスファターゼ阻害によるアポトーシス誘導,
第1回日本プロテインフォスファターゼ研究会学術集会, 2003年7月. 岡村裕彦, 森本景之, 吉田賀弥, 羽地達次 :
上皮癌細胞での転写因子NF-YによるMDR1の発現調節,
第20回分子病理研究会, 2003年7月. 東智子, 張剛太, 鈴木敬三, 吉田賀弥, 堀部ますみ, 中村輝夫, 二宮雅美, 大石慶二, 木戸淳一, 永田俊彦 :
糖尿病性腎症患者の歯周病罹患に関する疫学的研究,
日本歯周病学会会誌, 2003年4月.

(キーワード): 糖尿病性腎症 / 人工透析 / CPITN

岡村裕彦, 吉田賀弥, 森本景之, 永田俊彦, 北村清一郎, 羽地達次 :
薬剤感受性の異なる口腔扁平上皮癌細胞におけるMDR1の発現と転写調節,
第44回歯科基礎医学会総会, 2002年10月. 吉田賀弥, 岡村裕彦, 永田俊彦, 羽地達次 :
マウス骨芽細胞様細胞MC3T3-E1においてオカダ酸はRANKLの発現を促進する,
第44回歯科基礎医学会総会, 2002年10月.

研究会・報告書: 藤原奈津美, 邵文華, 吉田賀弥, 新垣理恵子, 尾崎和美, 石丸直澄, 工藤保誠 :
Fusobacterium nucleatumが与える口腔癌細胞への影響,
第38回分子病理学研究会淡路島シンポジウム(兵庫県) 2019年7月19-20日, 2019年7月. 吉田賀弥, 瀬山真莉子, 藤原奈津美, 尾崎和美, 内部健太, 池亀美華, 岡村裕彦 :
歯周病が糖尿病を重症化する機序について,
2018 Bioscience retreat in Awaji, 2018年11月. 藤原奈津美, 鶴熊美樹, 吉田賀弥, 村上圭史, 尾崎和美, 藤猪英樹, 湯本浩通 :
MPCポリマーコーティングによる義歯用レジンのカンジダ付着抑制効果,
2018 Bioscience retreat in Awaji, 2018年11月. 瀬山真莉子, 吉田賀弥, 藤原奈津美, 尾崎和美 :
Porphyromonas gingivalisの分泌小胞が肝臓インスリンシグナルに及ぼす影響について,
2017 Bioscience Retreat in Tosa, 2017年12月. 吉田賀弥, 瀬山真莉子, 藤原奈津美, 尾崎和美, 内部健太, 池亀美華, 岡村裕彦 :
Porphyromonas gingivalis感染したマクロファージはインスリンシグナル抑制因子を含むエクソソームを産生する,
2017 Bioscience Retreat in Tosa, 2017年12月. 吉田賀弥 :
歯肉においてPKRがリン酸化する機構:歯周病との関連性は?,
第22回HBS月例交流セミナー, 2011年7月. 稲垣裕司, 吉田賀弥, 大場博史, 中島由紀子, 瀬戸浩行, 木戸淳一, 羽地達次, 永田俊彦 :
高血糖は歯髄組織におけるオステオポンチン産生と病的石灰化を促進する,
第1回骨バイオサイエンス研究会 (岡山), 2010年6月. 吉田賀弥 :
PKRと骨代謝,
電気学会光・量子デバイス研究会, 2008年5月.

特許: 研究者総覧に該当データはありませんでした。
作品: 研究者総覧に該当データはありませんでした。
補助金・競争的資金: 歯周病菌膜小胞のDNAとミクログリアに着目した認知症発症機構の解明 (研究課題/領域番号: 23K09505 )
Fusobacterium nucleatum感染による口腔癌病態の解明 (研究課題/領域番号: 22K10342 )
母子健康に理想的な口腔環境を探る～歯周病原菌の小胞による胎盤組織への障害性～ (研究課題/領域番号: 21K19644 )
医・歯・看護の医療連携を飛躍させる「歯周病関連疾患の一括予測リキッドバイオシー」 (研究課題/領域番号: 20K21714 )
歯周病原菌が放出する小胞の組織障害性と病態評価への応用 (研究課題/領域番号: 19H04051 )
人工細胞を用いたオーラルケアシステムの基礎研究 (研究課題/領域番号: 17H04418 )
PKRが骨代謝を制御し糖尿病関連歯周炎を重症化する分子機構の解明 (研究課題/領域番号: 16K11506 )
最終糖化産物AGEsによる糖尿病関連歯周炎の重症化機序の解明と診断システムの構築 (研究課題/領域番号: 15H05054 )
プロテインホスファターゼＰＰ２Ａによる骨形成と間葉系細胞分化機構の解明 (研究課題/領域番号: 26462786 )
ＰＫＲはインフラマソームを介して歯周病の進行を制御するか？ (研究課題/領域番号: 25462918 )
漢方薬を応用した口腔保健管理による入院患者への医療支援の確立 (研究課題/領域番号: 24390471 )
プロテインホスファターゼＰＰ２Ａによる新たな骨芽細胞分化機構の解明 (研究課題/領域番号: 23592703 )
PKRによるSTAT1のユビキチン化を介した骨石灰化調節機構の解明 (研究課題/領域番号: 21791791 )
専門的口腔ケアによる自己免疫疾患の抑制 (研究課題/領域番号: 20390536 )
PKRによる骨石灰化調節機構の解明 (研究課題/領域番号: 19791346 )
PKR-骨石灰化における新たな調節因子- (研究課題/領域番号: 17791304 )
研究者番号（60363157）による検索

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2024年11月21日更新

専門分野・研究分野: 口腔解剖学 (Oral Anatomy)
口腔組織学 (Oral Histology)
細胞生物学 (Cell Biology)
骨代謝学
所属学会・所属協会: 歯科基礎医学会
日本歯周病学会
四国歯学会
社団法人日本解剖学会
日本細胞外小胞学会
委員歴・役員歴: 社団法人日本解剖学会 (医療専門職教育委員 [2021年4月])
受賞: 2006年9月, 歯科基礎医学会賞 (歯科基礎医学会)
2006年12月, 第十二回高田充歯科基礎医学奨励賞
活動: 学生委員会委員 (2014年4月〜2016年3月)

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2024年11月16日更新

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Jグローバル最終確認日: 2024/11/16 01:29
氏名（漢字）: 吉田賀弥
氏名（フリガナ）: ヨシダカヤ
氏名（英字）: Yoshida Kaya
所属機関: 徳島大学准教授

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researchmap最終確認日: 2024/11/17 02:54
氏名（漢字）: 吉田賀弥
氏名（フリガナ）: ヨシダカヤ
氏名（英字）: Yoshida Kaya
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登録日時: 2018/8/18 11:01
更新日時: 2024/8/27 11:09
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所属ID: 0344000000
所属: 徳島大学
部署: 医歯薬学研究部口腔保健教育学分野
職名: 准教授
学位: 博士（歯学）
学位授与機関: 徳島大学
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研究者番号: 60363157

所属（現在）: 2024/4/1 : 徳島大学, 大学院医歯薬学研究部(歯学域), 准教授

所属（過去の研究課題 情報に基づく）*注記: 2019/4/1 – 2023/4/1 : 徳島大学, 大学院医歯薬学研究部(歯学域), 准教授
2018/4/1 : 徳島大学, 大学院医歯薬学研究部(歯学域), 講師
2016/4/1 – 2017/4/1 : 徳島大学, 大学院医歯薬学研究部(歯学系), 講師
2015/4/1 : 徳島大学, 大学院医歯薬学研究部, 講師
2011/4/1 – 2014/4/1 : 徳島大学, ヘルスバイオサイエンス研究部, 講師
2013/4/1 : 徳島大学, 大学院ヘルスバイオサイエンス研究部, 講師
2012/4/1 : 徳島大学, 大学院・ヘルスバイオサイエンス研究部, 講師
2010/4/1 : 徳島大学, 大学院・ヘルスバイオサイエンス研究部, 講師
2009/4/1 : 徳島大, ヘルスバイオサイエンス研究部, 講師
2008/4/1 : 徳島大学, 大学院・ヘルスバイオサイエンス研究部, 講師
2007/4/1 : 徳島大学, 歯学部, 講師
2006/4/1 : 徳島大学, 大学院・ヘルスバイオサイエンス研究部, 助手
2005/4/1 : 徳島大学, 大学院ヘルスバイオサイエンス研究部, 助手

審査区分/研究分野

研究代表者

生物系 / 医歯薬学 / 歯学 / 形態系基礎歯科学
生物系 / 医歯薬学 / 歯学 / 病態科学系歯学・歯科放射線学
中区分58:社会医学、看護学およびその関連分野
小区分57080:社会系歯学関連

研究代表者以外

生物系 / 医歯薬学 / 歯学 / 社会系歯学
生物系 / 医歯薬学 / 歯学 / 形態系基礎歯科学
生物系 / 医歯薬学 / 歯学 / 歯周治療系歯学
小区分59040:栄養学および健康科学関連
中区分58:社会医学、看護学およびその関連分野
小区分57080:社会系歯学関連

キーワード

研究代表者

骨芽細胞 / 石灰化 / PKR / 転写因子 / STAT1 / 口腔解剖学(含組織学・発生学) / STAT 1 / ユビキチン / STATI / インフラマソーム / 歯周病 / NLRP3 / NF-kappaB / priming / 破骨細胞活性化 / ＰＫＲリン酸化 / 炎症性サイトカイン / 骨代謝調節因子 / 糖尿病 / ＰＫＲ / ＡＧＥｓ / 高血糖 / 破骨細胞分化 / AGEs / 歯周病マウス / PKR活性化 / AGEs合成 / 骨芽細胞分化 / 最終糖化産物 / 骨代謝 / リキッドバイオプシー / 歯周病関連疾患 / マクロファージ / exosome / 細胞外小胞 / micro RNA / 医療連携 / 予測診断 / 歯周病原菌 / 歯周病菌 / アルツハイマー型認知症

研究代表者以外

専門的口腔ケア / 自己免疫疾患 / 歯周病原細菌 / 熱ショック蛋白質 / リウマチ患者 / 唾液IgA / PKR / 專門的口腔ケア / 頬粘膜乾燥 / 舌苔 / 口腔内不潔物 / 自己抗体 / 口腔衛生学 / 骨芽細胞 / 骨形成 / 骨代謝 / プロテインホスファターゼ / PP2A / Osterix / 破骨細胞 / 骨分化 / 転写因子 / 漢方薬 / 抗がん剤 / 口腔粘膜炎 / 食道がん / 口腔保健管理 / 大黄甘草湯 / 病原性 / P. gingivalis / F. nucleatum / 食道がん化学療法 / 細胞死 / 抗癌剤 / がん / 造血幹細胞移植 / 嚥下補助食品 / 脂肪細胞 / 間葉系細胞 / 骨肉腫 / 蛋白質脱リン酸化 / 骨 / 糖尿病関連歯周炎 / AGE / 歯肉線維芽細胞 / マクロファージ / 糖尿病性関連歯周炎 / 歯周病 / 糖尿病 / オーラルケア / 抗菌ペプチド / 無細胞蛋白質合成 / リポソーム / ドラッグデリバリーシステム / 人工細胞 / 細菌付着抑制 / 無細胞蛋白合成 / 細胞外分泌小胞 / 肝臓 / 歯周病原菌 / Outer membrane vesicles / 遠隔臓器 / 細胞障害性 / 全身性疾患 / 肺 / 糖代謝 / 胎盤 / 胎児 / 細胞外小胞 / 血管新生 / VEGFR1 / 発育 / Fusobacterium nucleatum / 口腔癌

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2021年11月18日

歯周病の原因菌であるフゾバクテリウムが口腔がんの進展を促進する

工藤保誠藤原奈津美石丸直澄尾崎和美湯本浩通吉田賀弥

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シームレスな光イノベーションを創出する次世代光技術

安井武史矢野隆章久世直也藤方潤一山本健詞南川丈夫古部昭広吉田賀弥江本顕雄時実悠岸川博紀長谷栄治加藤遼

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吉田賀弥