研究者を探す
長谷川 敬展
徳島大学
2024年11月13日更新
- 職名
- 講師
- 電話
- 088-633-7324
- 電子メール
- thase@dent.tokushima-u.ac.jp
- 学歴
- 2001/3: 静岡大学 理学部 生物地球環境科学科 卒業
2003/3: 静岡大学大学院理工学研究科 生物地球環境科学専攻 修了
2006/3: 静岡大学大学院理工学研究科 環境科学専攻博士課程 修了 - 学位
- 博士(理学) (静岡大学) (2006年3月)
- 職歴・経歴
- 2003/4: 日本学術振興会 特別研究員(DC1)
2006/4: 群馬大学大学院医学系研究科 技術職員(生体構造解析学分野)
- 専門分野・研究分野
- 分子細胞生物学 (Molecular and Cellular Biology)
2024年11月13日更新
- 専門分野・研究分野
- 分子細胞生物学 (Molecular and Cellular Biology)
- 担当経験のある授業科目
- (基礎系)国家試験・CBT対策講義 (学部)
加齢歯科学 (学部)
口腔保健衛生学基礎実習 (学部)
口腔分子生理学 (大学院)
口腔分子生理学演習 (大学院)
口腔生理学 (学部)
基礎生物学DⅡ (共通教育)
基礎生物学実験D (共通教育)
基礎生理学 (学部)
実践口腔科学コアセミナー (大学院)
生理学 (学部)
生理学・口腔生理学実習 (学部)
生理学・生化学・病理学・薬理学 (学部)
生理学実習 (学部)
統合生理・口腔生理学 (学部)
総合歯科学一 (学部)
高齢者歯科学実験実習 (大学院) - 指導経験
- 3人 (博士)
2024年11月13日更新
- 専門分野・研究分野
- 分子細胞生物学 (Molecular and Cellular Biology)
- 研究テーマ
- 唾液腺における水・イオン輸送機構 (唾液腺 (salivary gland), アクアポリン (aquaporin))
- 著書
- 研究者総覧に該当データはありませんでした。
- 論文
- Shintaroh Kusunoki, Takako Fukuda, Saori Maeda, Chenjuan Yao, Takahiro Hasegawa, Tetsuya Akamatsu and Hiroshi Yoshimura :
Relationships between feeding behaviors and emotions: An electroencephalogram (EEG) frequency analysis study,
The Journal of Physiological Sciences, Vol.73, No.1, 2, 2023.- (要約)
- Feeding behaviors may be easily affected by emotions, both being based on brain activity; however, the relationships between them have not been explicitly defined. In this study, we investigated how emotional environments modulate subjective feelings, brain activity, and feeding behaviors. Electroencephalogram (EEG) recordings were obtained from healthy participants in conditions of virtual comfortable space (CS) and uncomfortable space (UCS) while eating chocolate, and the times required for eating it were measured. We found that the more participants tended to feel comfortable under the CS, the more it took time to eat in the UCS. However, the EEG emergence patterns in the two virtual spaces varied across the individuals. Upon focusing on the theta and low-beta bands, the strength of the mental condition and eating times were found to be guided by these frequency bands. The results determined that the theta and low-beta bands are likely important and relevant waves for feeding behaviors under emotional circumstances, following alterations in mental conditions.
- (キーワード)
- 摂食行動 / 情動 / 脳波 (electroencephalogram) / 高速フーリエ変換 / 仮想空間
- (徳島大学機関リポジトリ)
- ● Metadata: 118602
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1186/s12576-022-00858-w
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 36869303
- ● Search Scopus @ Elsevier (PMID): 36869303
- ● Search Scopus @ Elsevier (DOI): 10.1186/s12576-022-00858-w
(徳島大学機関リポジトリ: 118602, DOI: 10.1186/s12576-022-00858-w, PubMed: 36869303) Xiaoke Wang, Piaoyu Zhu, Shenya Xu, Yuting Liu, Yang Jin, Shali Yu, Haiyan Wei, Jinlong Li, Qinglin Zhang, Takahiro Hasegawa, Chenjuan Yao, Hiroshi Yoshimura, Qiyun Wu and Xinyuan Zhao :
Antimony, a novel nerve poison, triggers neuronal autophagic death via reactive oxygen species-mediated inhibition of the protein kinase B/mammalian target of rapamycin pathway.,
The International Journal of Biochemistry & Cell Biology, Vol.114, 105561, 2019.- (要約)
- Antimony (Sb), a naturally occurring metal present in air and drinking water, has been found in the human brain, and there is evidence of its toxic effects on neurobehavioral perturbations, suggesting that Sb is a potential nerve poison. Here, we provide the first study on the molecular mechanism underlying Sb-associated neurotoxicity. Mice exposed to antimony potassium tartrate hydrate showed significantly increased neuronal apoptosis. In vitro, Sb triggered apoptosis in PC12 cells in a dose-dependent manner. Mechanically, Sb triggered autophagy as indicated by increased expression of microtubule-associated protein 1 light chain 3-II (LC3-II) and accumulation of green fluorescent protein-tagged LC3 dots. Moreover, Sb enhanced autophagic flux and sequestosome 1 (p62) degradation. Subsequent analyses showed that Sb treatment decreased phosphorylation of protein kinase B (Akt) as well as the mammalian target of rapamycin (mTOR), while an Akt activator protected PC12 cells from autophagy. Moreover, the antioxidant N-acetylcysteine attenuated Sb-induced Akt/mTOR inhibition and decreased autophagy and apoptosis, with autophagy inhibition also playing a cytoprotective role. In vivo, mice treated with Sb showed higher expression of LC3-II and p62 in the brain, consistent with the in vitro results. In summary, Sb induced autophagic cell death through reactive oxygen species-mediated inhibition of the Akt/mTOR pathway.
- (キーワード)
- Animals / Antimony / Autophagic Cell Death / Mice / Nerve Agents / Neurons / PC12 Cells / Proto-Oncogene Proteins c-akt / Rats / Reactive Oxygen Species / TOR Serine-Threonine Kinases
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1016/j.biocel.2019.105561
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 31228582
- ● Search Scopus @ Elsevier (PMID): 31228582
- ● Search Scopus @ Elsevier (DOI): 10.1016/j.biocel.2019.105561
(DOI: 10.1016/j.biocel.2019.105561, PubMed: 31228582) Hiroshi Yoshimura, Sugai Tokio, Kato Nobuo, Tominaga Takashi, Tominaga Yoko, Takahiro Hasegawa, Chenjuan Yao and Tetsuya Akamatsu :
Interplay between non-NMDA and NMDA receptor activation during oscillatory wave propagation: Analyses of caffeine-induced oscillations in the visual cortex of rats,
Neural Networks, Vol.79, 141-149, 2016.- (要約)
- Generation and propagation of oscillatory activities in cortical networks are important features of the brain. However, many issues related to oscillatory phenomena are unclear. We previously reported neocortical oscillation following caffeine treatment of rat brain slices. Input to the primary visual cortex (Oc1) generates N-methyl-d-aspartate (NMDA) receptor-dependent oscillations, and we proposed that the oscillatory signals originate in the secondary visual cortex (Oc2). Because non-NMDA and NMDA receptors cooperate in synaptic transmission, non-NMDA receptors may also play an important role in oscillatory activities. Here we investigated how non-NMDA receptor activities contribute to NMDA receptor-dependent oscillations by using optical recording methods. After induction of stable oscillations with caffeine application, blockade of NMDA receptors abolished the late stable oscillatory phase, but elicited 'hidden' non-NMDA receptor-dependent oscillation during the early depolarizing phase. An interesting finding is that the origin of the non-NMDA receptor-dependent oscillation moved from the Oc1, during the early phase, toward the origin of the NMDA receptor-dependent oscillation that is fixed in the Oc2. In addition, the frequency of the non-NMDA receptor-dependent oscillation was higher than that of the NMDA receptor-dependent oscillation. Thus, in one course of spatiotemporal oscillatory activities, the relative balance in receptor activities between non-NMDA and NMDA receptors gradually changes, and this may be due to the different kinetics of the two receptor types. These results suggest that interplay between the two receptor types in the areas of Oc1 and Oc2 may play an important role in oscillatory signal communication.
- (キーワード)
- neural oscillation / non-NMDA receptor / NMDA受容体 (NMDA-receptors) / caffeine / ラット (rat)
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1016/j.neunet.2016.03.012
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 27136667
- ● Search Scopus @ Elsevier (PMID): 27136667
- ● Search Scopus @ Elsevier (DOI): 10.1016/j.neunet.2016.03.012
(DOI: 10.1016/j.neunet.2016.03.012, PubMed: 27136667) Hiroshi Yoshimura, 川邊 真道, 須貝 外喜夫, 加藤 伸郎, Takahiro Hasegawa, Chenjuan Yao and Tetsuya Akamatsu :
Influences of oral impairment on neural oscilltion and wave propagation in the neocortex of rats,
Neuroscience Research Suppl, Vol.Suppl, 2015. Gang Chen, Chenjuan Yao, Takahiro Hasegawa, Tetsuya Akamatsu, Hiroshi Yoshimura and Kazuo Hosoi :
Effects of isoproterenol on aquaporin 5 levels in the parotid gland of mice in vivo.,
American Journal of Physiology, Endocrinology and Metabolism, Vol.306, No.1, E100-E108, 2014.- (要約)
- In the membrane fraction of mouse parotid gland (PG), the protein level of aquaporin 5 (AQP5), a member of the water channel family, was increased by injection (ip) of isoproterenol (IPR), a β-adrenergic agonist, at 1 h, and stayed at high levels until 6 h; this change occurred simultaneously as amylase secretion. The AQP5 level then decreased and returned toward the original level at 12-48 h. After IPR injection, the AQP5 mRNA gradually increased and reached a maximum at 24 h. The facts suggest a rapid appearance of AQP5 at plasma membrane by IPR and subsequent degradation/metabolism by activation of proteolytic systems. Pretreatment of animals with two calpain inhibitors, N-Ac-Leu-Leu-methininal (ALLM) and calpeptin, as well as a protein synthesis inhibitor, cycloheximide (CHX), significantly suppressed the IPR-induced AQP5 degradation in the PG membrane fraction; such suppression was not observed by two proteasome inhibitors, MG132 and lactacystin, or the lysosome denaturant chloroquine, although most of these inhibitors increased AQP5 protein levels in unstimulated mice. The AQP5 protein was also degraded by μ-calpain in vitro. Furthermore, we demonstrated that μ-calpain was colocalized with AQP5 in the acinar cells by immunohistochemistry, and its activity in the PG was increased at 6 h after IPR injection. These results suggest that the calpain system was responsible for IPR-induced AQP5 degradation in the parotid gland and that such a system was coupled to the secretory-restoration cycle of amylase in the PG.
- (キーワード)
- アクアポリン5 / 耳下腺 / イソプロテレノール
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1152/ajpendo.00317.2013
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 24192288
- ● Summary page in Scopus @ Elsevier: 2-s2.0-84891527146
(DOI: 10.1152/ajpendo.00317.2013, PubMed: 24192288, Elsevier: Scopus) Hiroshi Yoshimura, Tokio Sugai, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Nobuo Kato :
Age-dependent emergence of caffeine-assisted voltage oscillations in the endopiriform nucleus of rats.,
Neuroscience Research, Vol.76, No.1-2, 16-21, 2013.- (要約)
- The gustatory insular cortex (IC) is connected with not only the somatosensory cortex, but also the endopiriform nucleus (EPN). We have previously revealed that low-frequency electrical stimulation to the IC can elicit membrane potential oscillations at a frequency of 8-10 Hz in the somatosensory cortex of rat brain slices under bath-application of caffeine. Using the same procedure, we investigated whether the EPN has the ability to generate oscillations, and whether such oscillations emerge age-dependently. Electrical stimulations were delivered to the IC, and field potentials were recorded from the EPN. In the case of slices made from mature rats, stable field potential oscillations at 8-10 Hz were induced in the EPN after repetitive stimulations. Optical recordings revealed that signals traveled from the IC to the EPN by way of the claustrum. Generation of oscillations was N-methyl-d-aspartate (NMDA) receptor activity-dependent, since oscillatory phases disappeared following application of NMDA receptor antagonist. In slices from immature rats, however, oscillations were not induced. IC stimulation can thus age-dependently elicit membrane potential oscillations in the EPN, and the EPN oscillations were NMDA receptor activity-dependent. These findings suggest that developmental changes in properties of the EPN might contribute to development of information integration, including gustatory information.
- (キーワード)
- 加齢 (aging) / Animals / Caffeine / Central Nervous System Stimulants / Cerebral Cortex / Electric Stimulation / Membrane Potentials / Organ Culture Techniques / Rats / Rats, Wistar
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1016/j.neures.2013.02.010
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 23517711
- ● Summary page in Scopus @ Elsevier: 2-s2.0-84884702568
(DOI: 10.1016/j.neures.2013.02.010, PubMed: 23517711, Elsevier: Scopus) Nunuk Purwanti, Mileva Ratko Karabasil, Shinsuke Matsuo, Gang Chen, Javkhlan Purevjav, Ahmad Azlina, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi :
Induction of Sca-1 via activation of STAT3 system in the duct cells of the mouse submandibular gland by ligation of the main excretory duct,
American Journal of Physiology, Gastrointestinal and Liver Physiology, Vol.301, No.5, G814-G824, 2011.- (要約)
- To examine the very initial step that takes place immediately after tissue injury and is linked to tissue regeneration, we employed the submandibular gland (SMG), which was injured by ligation of its main excretory duct (MED). Ligation of the MED of the SMG in mice induced the expression of Sca-1, a protein marker of hematopoietic stem cells. In the normal gland, a low level of Sca-1 was expressed, which was localized predominantly in the excretory duct cells. At 1 day after ligation, Sca-1 expression increased prominently in almost all of cells in the duct system, but not in the acinar cells. The level of Sca-1 mRNA had begun to increase at 6 h after ligation and continuously rose thereafter until it reached a plateau, which occurred ∼12 h after ligation. STAT3 phosphorylated at its tyrosine-705 (p-STAT3) in the ligated gland increased immediately after ligation, and it was localized in the nuclei of all duct cells. The results of an EMSA revealed the specific binding of a nuclear extract to the sequence of the γ-interferon activation site (GAS) present in the Sca-1 promoter and confirmed that such binding increased after ligation. Thus the present study suggests that STAT3, having been phosphorylated following MED ligation, was transferred to the nucleus, where it bound to the GAS element in the promoter of Sca-1 gene, resulting in promotion of Sca-1 gene expression. Actual prevention of STAT3 phosphorylation reduced the ligation-induced Sca-1 elevation.
- (キーワード)
- Animals / Antigens, Ly / Ligation / Membrane Proteins / Mice / Phosphorylation / Promoter Regions, Genetic / STAT3 Transcription Factor / Salivary Ducts / Submandibular Gland
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1152/ajpgi.00408.2010
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21868636
- ● Search Scopus @ Elsevier (PMID): 21868636
- ● Search Scopus @ Elsevier (DOI): 10.1152/ajpgi.00408.2010
(DOI: 10.1152/ajpgi.00408.2010, PubMed: 21868636) Purevjav Javkhlan, Yuka Hiroshima, Ahmad Azlina, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Jun-ichi Kido, Toshihiko Nagata and Kazuo Hosoi :
Lipopolysaccharide-mediated induction of calprotectin in the submandibular and parotid glands of mice,
Inflammation, Vol.34, No.6, 668-680, 2011.- (要約)
- S100A8 and S100A9 constitute a heterodimeric protein, calprotectin. The mRNAs of S100A8 and S100A9, being expressed at minimal levels in the submandibular and parotid glands (SMG and PG, respectively) of C3H/HeN mice, were induced strongly and transiently by lipopolysaccharide (LPS). Among the mRNAs of members of the S100 protein family examined, those of S100A8 and S100A9 were specifically induced by LPS in the salivary glands. The induction was assumed to be mediated via toll-like receptor 4 (TLR4), since their elevation was limited in C3H/HeJ mice, a TLR4-mutant strain. These proteins became expressed in the granular convoluted tubular cells and striated duct cells in the SMG, and in both acinar and duct cells in the PG (all in the cytoplasm). The salivary calprotectin level was not increased by LPS treatment, implying that elevated calprotectin was not secreted into the saliva and that they may function in microcellular environment of the salivary gland.
- (キーワード)
- Animals / Calgranulin A / Calgranulin B / Leukocyte L1 Antigen Complex / Lipopolysaccharides / Mice / Parotid Gland / RNA, Messenger / Salivary Glands / Submandibular Gland / Transcriptional Activation
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1007/s10753-010-9277-1
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21125321
- ● Search Scopus @ Elsevier (PMID): 21125321
- ● Search Scopus @ Elsevier (DOI): 10.1007/s10753-010-9277-1
(DOI: 10.1007/s10753-010-9277-1, PubMed: 21125321) Takahiro Hasegawa, Ahmad Azlina, Javkhlan Purevjav, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi :
Novel phosphorylation of aquaporin-5 at its threonine 259 through cAMP signaling,
American Journal of Physiology, Cell Physiology, Vol.301, No.3, C667-C678, 2011.- (要約)
- Aquaporin-5 (AQP5), a water channel, plays key roles in salivary secretion. The novel phosphorylation of AQP5 was investigated by using human salivary gland (HSG) cells and mouse salivary glands. In the HSG cells stably transfected with a wild-type mouse AQP5 construct, a protein band immunoreactive with antibody against phosphorylated PKA substrate was detected in the AQP5 immunoprecipitated sample, and its intensity was enhanced by short-term treatment of the cells with 8-bromo-cAMP, forskolin, or phorbol 12-myristate 13-acetate, but not by that with A23187 calcium ionophore. Such enhancement was inhibited in the presence of H-89, a PKA inhibitor. An AQP5 mutant (AQP5-T259A) expressed by transfection of HSG cells was not recognized by anti-phosphorylated PKA substrate antibody, even when the cells were stimulated with the protein kinase activators. Immunoblotting and immunofluorescence studies using a specific antibody detecting AQP5 phosphorylated at its Thr259 demonstrated that AQP5 was rapidly and transiently phosphorylated at the apical membrane of acinar cells in the submandibular and parotid glands after administration of isoproterenol, but not pilocarpine. Furthermore, both AQP5 and AQP5-T259A were constitutively localized at the plasma membrane in HSG cells under the resting and forskolin-stimulated conditions. These results suggest that AQP5 is phosphorylated at its Thr259 by PKA through cAMP, but not Ca(2+), signaling pathways, and that this phosphorylation does not contribute to AQP5 trafficking in the salivary gland cells.
- (キーワード)
- Amino Acid Substitution / Animals / Antibodies / Antibody Specificity / Aquaporin 5 / Calcimycin / Cell Line, Tumor / Cell Membrane / Cyclic AMP / Cyclic AMP-Dependent Protein Kinases / Detergents / Forskolin / Humans / Isoproterenol / Isoquinolines / Male / Mice / Mice, Inbred ICR / Parotid Gland / Phosphorylation / Pilocarpine / Protein Kinase Inhibitors / Protein Transport / Salivary Glands / Signal Transduction / Submandibular Gland / Sulfonamides / Tetradecanoylphorbol Acetate / Threonine / Transfection
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1152/ajpcell.00058.2011
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21633078
- ● Search Scopus @ Elsevier (PMID): 21633078
- ● Search Scopus @ Elsevier (DOI): 10.1152/ajpcell.00058.2011
(DOI: 10.1152/ajpcell.00058.2011, PubMed: 21633078) Nunuk Purwanti, Daisuke Tsuji, Ahmad Azlina, Mileva Ratko Karabasil, Purevjav Javkhlan, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Kouji Itou and Kazuo Hosoi :
Induction of Sca-1 in the duct cells of the mouse submandibular gland by obstruction of the main excretory duct,
Journal of Oral Pathology & Medicine, Vol.40, No.8, 651-658, 2011.- (要約)
- The effect of ligation of the main excretory duct (MED) of the mouse submandibular gland (SMG) on the expression of Sca-1, a stem cell antigen, was examined by Western blotting and immunohistochemistry. By Western blotting, the expression of Sca-1 with a molecular weight of 18 kDa was identified in the normal gland. At 1 day post-ligation, the expression level of Sca-1 was strongly increased in the experimental gland and weakly in the contralateral gland, and such expression in both glands decreased at 6 days. By immunohistochemistry, Sca-1 was detected weakly in the apical membrane of excretory duct (ED) cells of the SMG under the normal condition. By duct ligation, Sca-1 became expressed strongly in most cells of the two major duct systems, i.e., the striated duct (SD) and granular convoluted tubules (GCT), but was not detected in the acinar (Ac) cells. By fluorescence-activated cell sorter (FACS) analysis, the number of side population (SP) cells in this gland was found to be increased by ligation. These results imply that Sca-1-positive cells may have a role in the duct cell proliferation in the regeneration step elicited by MED ligation-induced injury.
- (キーワード)
- Animals / Antigens, Ly / Cell Count / Cell Proliferation / Ligation / Male / Membrane Proteins / Mice / Mice, Inbred C57BL / Regeneration / Salivary Ducts / Salivation / Side-Population Cells / Submandibular Gland
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1111/j.1600-0714.2011.01011.x
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21884259
- ● Search Scopus @ Elsevier (PMID): 21884259
- ● Search Scopus @ Elsevier (DOI): 10.1111/j.1600-0714.2011.01011.x
(DOI: 10.1111/j.1600-0714.2011.01011.x, PubMed: 21884259) Mileva Ratko Karabasil, Takahiro Hasegawa, Ahmad Azlina, Nunuk Purwanti, Chenjuan Yao, Tetsuya Akamatsu, Shigemasa Tomioka and Kazuo Hosoi :
Effects of naturally occurring G103D point mutation of AQP5 on its water permeability, trafficking, and cellular localization in the submandibular gland of rats,
Biology of the Cell, Vol.103, No.2, 69-86, 2011.- (要約)
- AQPs (aquaporins) are water channel proteins that are expressed in almost all living things. In mammalians, 13 members of AQPs (AQP0-12) have been identified so far. AQP5 is known to be expressed mostly in the exocrine cells, including the salivary gland acinar cells. A naturally occurring point mutation (G308A, Gly103 > Asp103) was earlier found in the rat AQP5 gene [Murdiastuti, Purwanti, Karabasil, Li, Yao, Akamatsu, Kanamori and Hosoi (2006) Am. J. Physiol. 291, G1081-G1088]; in this mutant, the rate of initial saliva secretion under stimulated and unstimulated conditions is less than that for the wt (wild-type) animals. Here the mutant molecule was characterized in detail. Using the Xenopus oocyte system, we demonstrated the mutant AQP5 to have water permeability almost the same as that of the wt molecule. Mutant and wt AQP5s, tagged with GFP (green fluorescent protein; GFP-AQP5s) and expressed in polarized MDCK-II (Madin-Darby canine kidney II) cells, first appeared in the vesicular structure(s) in the cytoplasm, and were translocated to the upper plasma membrane or apical membrane during cultivation, with the mutant GFP-AQP5 being translocated less efficiently. Thapsigargin and H-89 both induced translocation in vitro of either molecule, whereas colchicine inhibited this activity; the fraction of cells showing apical localization of mutant GFP-AQP5 was less than that showing that of the wt molecule under any of the experimental conditions used. In the mutant SMG (submandibular gland) tissue, localization of AQP5 in the apical membrane of acinar cells was extremely reduced. Vesicular structures positive for AQP5 and present in the cytoplasm of the acinar cells were co-localized with LAMP2 (lysosome-associated membrane protein 2) or cathepsin D in the mutant gland, whereas such co-localizations were very rare in the wt gland, suggesting that the mutant molecules largely entered lysosomes for degradation. Replacement of highly conserved hydrophobic Gly103 with strongly hydrophilic Asp103 in rat AQP5, though it did not affect water permeability, may possibly have resulted in less efficient membrane trafficking and increased lysosomal degradation, leading to its lower expression in the apical membrane of the acinar cells in the SMG.
- (キーワード)
- Amino Acid Sequence / Animals / Aquaporin 5 / Cell Line / Cell Membrane / Dogs / Molecular Sequence Data / Mutation, Missense / Permeability / Point Mutation / Protein Transport / Rats / Sequence Alignment / Submandibular Gland / Water / Xenopus
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1042/BC20100086
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 21138418
- ● Search Scopus @ Elsevier (PMID): 21138418
- ● Search Scopus @ Elsevier (DOI): 10.1042/BC20100086
(DOI: 10.1042/BC20100086, PubMed: 21138418) Ahmad Azlina, Purevjav Javkhlan, Yuka Hiroshima, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi :
Roles of lysosomal proteolytic systems in AQP5 degradation in the submandibular gland of rats following chorda tympani parasympathetic denervation,
American Journal of Physiology, Gastrointestinal and Liver Physiology, Vol.299, No.5, G1106-G1117, 2010.- (要約)
- Chorda tympani denervation (CTD) of rats was earlier shown to result in loss of submandibular gland (SMG) weight (at only 1 wk) and in continued reduction in aquaporin 5 (AQP5) protein expression (until 4 wk), without affecting its mRNA synthesis (Li X, Azlina A, Karabasil MR, Purwanti N, Hasegawa T, Yao C, Akamatsu T, Hosoi K. Am J Physiol Gastrointest Liver Physiol 295: G112-G123, 2008). The present study indicated that despite elevation of bax, a proapoptosis protein, by CTD, the operation also increased the level of bcl-2, an antiapoptosis protein, in the SMG. Terminal deoxynucleotidyl transferase dUTP nick-end labeling (TUNEL assay) showed no increase in the number of apoptotic cells in the SMG. CTD, however, induced strongly and transiently (at 1-3 days) the protein expression of LC3B-II, a marker protein of autophagosomes, suggesting that the reduction in the gland weight was due to onset of autophagy by CTD. Upon CTD, Lamp2, a lysosomal marker, gradually increased in amount, reaching a peak at the 14th day. Immunohistochemical analysis revealed an increase in the number of lysosome-like structures positive for both AQP5 and Lamp2 in the acinar cells of the SMG after CTD; similar changes were observed also for AQP5 and LC3Bs. These data suggest that AQP5 in the SMG entered autophagosomes and/or lysosomes for degradation upon CTD. In vitro AQP5-degrading activity was found in the SMG extracts, and such activity was shown to be increased by CTD. Inhibitor experiments implied cathepsins B and L to be candidate enzymes for this degradation under normal and CTD conditions, respectively.
- (キーワード)
- Animals / Apoptosis / Aquaporin 5 / Blotting, Western / Chorda Tympani Nerve / Immunohistochemistry / In Situ Nick-End Labeling / Lysosomal-Associated Membrane Protein 2 / Lysosomes / Male / Parasympathectomy / Proto-Oncogene Proteins c-bcl-2 / Rats / Rats, Sprague-Dawley / Submandibular Gland
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1152/ajpgi.00194.2010
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20689061
- ● Search Scopus @ Elsevier (PMID): 20689061
- ● Search Scopus @ Elsevier (DOI): 10.1152/ajpgi.00194.2010
(DOI: 10.1152/ajpgi.00194.2010, PubMed: 20689061) Chenjuan Yao, Nunuk Purwanti, Mileva Ratko Karabasil, Ahmad Azlina, Javkhlan Purevjav, Takahiro Hasegawa, Tetsuya Akamatsu, Toru Hosoi, Koichiro Ozawa and Kazuo Hosoi :
Potential down-regulation of salivary gland AQP5 by LPS via cross-coupling of NF-κB and p-c-Jun/c-Fos,
The American Journal of Pathology, Vol.177, No.2, 724-734, 2010.- (要約)
- The mRNA and protein levels of aquaporin (AQP)5 in the parotid gland were found to be potentially decreased by lipopolysaccharide (LPS) in vivo in C3H/HeN mice, but only weakly in C3H/HeJ, a TLR4 mutant mouse strain. In the LPS-injected mice, pilocarpine-stimulated saliva production was reduced by more than 50%. In a tissue culture system, the LPS-induced decrease in the AQP5 mRNA level was blocked completely by pyrrolidine dithiocarbamate, MG132, tyrphostin AG126, SP600125, and partially by SB203580, which are inhibitors for IkappaB kinase, 26S proteasome, ERK1/2, JNK, and p38 MAPK, respectively. In contrast, the expression of AQP1 mRNA was down-regulated by LPS and such down-regulation was blocked only by SP600125. The transcription factors NF-kappaB (p65 subunit), p-c-Jun, and c-Fos were increased by LPS given in vivo, whereas the protein-binding activities of the parotid gland extract toward the sequences for NF-kappaB but not AP-1-responsive elements present at the promoter region of the AQP5 gene were increased by LPS injection. Co-immunoprecipitation by using antibody columns suggested the physical association of the three transcription factors. These results suggest that LPS-induced potential down-regulation of expression of AQP5 mRNA in the parotid gland is mediated via a complex(es) of these two classes of transcription factors, NF-kappaB and p-c-Jun/c-Fos.
- (キーワード)
- Animals / Aquaporin 1 / Aquaporin 5 / Cells, Cultured / Enzyme Inhibitors / Humans / JNK Mitogen-Activated Protein Kinases / Lipopolysaccharides / Male / Mice / Mice, Inbred C3H / Mice, Inbred C57BL / NF-kappa B / Nitrates / Nitrites / Proto-Oncogene Proteins c-fos / Salivary Glands
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.2353/ajpath.2010.090282
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20522648
- ● Search Scopus @ Elsevier (PMID): 20522648
- ● Search Scopus @ Elsevier (DOI): 10.2353/ajpath.2010.090282
(DOI: 10.2353/ajpath.2010.090282, PubMed: 20522648) Y Ogushi, D Kitagawa, Takahiro Hasegawa, M Suzuki and S Tanaka :
Correlation between aquaporin and water permeability in response to vasotocin, hydrin and {beta}-adrenergic effectors in the ventral pelvic skin of the tree frog Hyla japonica.,
The Journal of Experimental Biology, Vol.213, No.2, 288-294, 2010.- (要約)
- The ventral pelvic skin of the tree frog Hyla japonica expresses two kinds of arginine vasotocin (AVT)-stimulated aquaporins (AQP-h2 and AQP-h3), which affect the capacity of the frog's skin to absorb water. As such, it can be used as a model system for analyzing the molecular mechanisms of water permeability. We investigated AQP dynamics and water permeability in the pelvic skin of H. japonica following challenge with AVT, hydrins (intermediate peptides of pro-AVT) and beta-adrenergic effectors. In the in vivo experiment, both AQP-h2 and AQP-h3 proteins were translocated to the apical plasma membrane in the principal cells of the first-reacting cell (FRC) layer in the pelvic skin following challenge with AVT, hydrin 1 and hydrin 2, thereby increasing the water permeability of the pelvic skin. The beta-adrenergic receptor agonist isoproterenol (IP) and its anatagonist propranolol (PP) in combination with AVT or hydrins were used as challenge in the in vitro experiment. IP increased water permeability whereas PP inhibited it, and both events were well correlated with the translocation of the AQPs to the apical membrane. In the PP+AVT-treated skins, labels for AQP-h2 and AQP-h3 were differentially visible among the principal cells; the apical plasma membrane of some cells was labeled while others were not, indicating that the response of PP or AVT is different from cell to cell. These results provide morphological evidence that the principal cells of the FRC layers may have two kinds of receptors: a V2 receptor and beta-adrenergic receptor.
- (キーワード)
- Adrenergic beta-Agonists / Adrenergic beta-Antagonists / Animals / Anura / Aquaporins / Isoproterenol / Male / Permeability / Propranolol / Skin / Time Factors / Vasotocin / Water
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1242/jeb.036871
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20038663
- ● Search Scopus @ Elsevier (PMID): 20038663
- ● Search Scopus @ Elsevier (DOI): 10.1242/jeb.036871
(DOI: 10.1242/jeb.036871, PubMed: 20038663) Yuji Ogushi, Gen Akabane, Takahiro Hasegawa, Hiroshi Mochida, Manabu Matsuda, Masakazu Suzuki and Shigeyasu Tanaka :
Water adaptation strategy in anuran amphibians: molecular diversity of aquaporin.,
Endocrinology, Vol.151, No.1, 165-173, 2009.- (要約)
- Most adult anuran amphibians except for the aquatic species absorb water across the ventral pelvic skin and reabsorb it from urine in the urinary bladder. Many terrestrial and arboreal species use a region in the posterior or pelvic region of the ventral skin that is specialized for rapid rehydration from shallow water sources or moist substrates. Periods of terrestrial activity can be prolonged by reabsorption of dilute urine from the urinary bladder. Aquaporin (AQP), a water channel protein, plays a fundamental role in these water absorption/reabsorption processes, which are regulated by antidiuretic hormone. Characterization of AQPs from various anurans revealed that the unique water homeostasis is basically mediated by two types of anuran-specific AQPs, i.e. ventral pelvic skin and urinary bladder type, respectively. The bladder-type AQP is further expressed in the pelvic skin of terrestrial and arboreal species, together with the pelvic skin-type AQP. In contrast, the pelvic skin-type AQP (AQP-x3) of the aquatic Xenopus has lost the ability of efficient protein production. The extra C-terminal tail in AQP-x3 consisting of 33 nucleotides within the coding region appears to participate in the posttranscriptional regulation of AQP-x3 gene expression by attenuating protein expression. The positive transcriptional regulation of bladder-type AQP in the pelvic skin and negative posttranscriptional regulation of pelvic skin-type AQP provide flexibility in the water regulation mechanisms, which might have contributed to the evolutionary adaptation of anurans to a wide variety of water environments.
- (キーワード)
- Adaptation, Biological / Amino Acid Sequence / Animals / Anura / Aquaporins / Ecosystem / Female / Gene Expression Regulation / Genetic Variation / Male / Molecular Sequence Data / Sequence Homology, Amino Acid / Species Specificity / Urinary Bladder / Water / Water-Electrolyte Balance
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1210/en.2009-0841
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19854867
- ● Search Scopus @ Elsevier (PMID): 19854867
- ● Search Scopus @ Elsevier (DOI): 10.1210/en.2009-0841
(DOI: 10.1210/en.2009-0841, PubMed: 19854867) Mileva Ratko Karabasil, Takahiro Hasegawa, Ahmad Azlina, Nunuk Purwanti, Javkhlan Purevjav, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi :
Trafficking of GFP-AQP5 chimeric proteins conferred with unphosphorylated amino acids at their PKA-target motif (152SRRTS) in MDCK-II cells,
The Journal of Medical Investigation : JMI, Vol.56, No.1, 2, 55-63, 2009.- (要約)
- Three constructs having mutated PKA-target motif at (152)SRRTS of AQP5, an exocrine type water channel, were prepared and fused to C-terminus of green fluorescence protein cDNA to examine the effects of blocking of phosphorylation at (152)SRRTS (a consensus PKA-target motif of AQP5) on translocation or trafficking of the chimeric proteins expressed in the Madin-Darby canine kidney-II (MDCK-II) cells. H-89 treatment increased translocation of wild-type GFP-AQP5 to the apical membrane. All 3 mutant molecules translocated 1.5 to 2 times more than the control wild-type GFP-AQP5. Colchicine but not cytochalasin B inhibited the translocation of wild-type GFP-AQP5. Present results suggest dephosphorylation of this consensus sequence increase GFP-AQP5 translocation, and that microtubules but not microfilaments are involved in this event.
- (キーワード)
- Amino Acid Motifs / Amino Acids / Animals / Aquaporin 5 / Cell Line / Cell Membrane / Chimera / Colchicine / Cyclic AMP-Dependent Protein Kinases / Cytochalasin B / Dogs / Green Fluorescent Proteins / Isoquinolines / Kidney / Phosphorylation / Protein Transport / Sulfonamides
- (徳島大学機関リポジトリ)
- ● Metadata: 111308
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.2152/jmi.56.55
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19262015
- ● Search Scopus @ Elsevier (PMID): 19262015
- ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.55
(徳島大学機関リポジトリ: 111308, DOI: 10.2152/jmi.56.55, PubMed: 19262015) Tetsuya Akamatsu, Ahmad Azlina, Nunuk Purwanti, Mileva Ratko Karabasil, Takahiro Hasegawa, Chenjuan Yao and Kazuo Hosoi :
Inhibition and transcriptional silencing of a subtilisin-like proprotein convertase, PACE4/SPC4, reduces the branching morphogenesis of and AQP5 expression in rat embryonic submandibular gland,
Developmental Biology, Vol.325, No.2, 434-443, 2009.- (要約)
- The submandibular gland (SMG) develops through the epithelial-mesenchymal interaction mediated by many growth/differentiation factors including activin and BMPs, which are synthesized as inactive precursors and activated by subtilisin-like proprotein convertases (SPC) following cleavage at their R-X-K/R-R site. Here, we found that Dec-RVKR-CMK, a potent inhibitor of SPC, inhibited the branching morphogenesis of the rat embryonic SMG, and caused low expression of a water channel AQP5, in an organ culture system. Dec-RVKR-CMK also decreased the expression of PACE4, a SPC member, but not furin, another SPC member, suggesting the involvement of PACE4 in the SMG development. Heparin, which is known to translocate PACE4 in the extracellular matrix into the medium, and an antibody specific for the catalytic domain of PACE4, both reduced the branching morphogenesis and AQP5 expression in the SMG. The inhibitory effects of Dec-RVKR-CMK were partially rescued by the addition of recombinant BMP2, whose precursor is one of the candidate substrates for PACE4 in vivo. Further, the suppression of PACE4 expression by siRNAs resulted in decreased expression of AQP5 and inhibition of the branching morphogenesis in the present organ culture system. These observations suggest that PACE4 regulates the SMG development via the activation of some growth/differentiation factors.
- (キーワード)
- Amino Acid Chloromethyl Ketones / Animals / Aquaporin 5 / Extracellular Matrix / Furin / Gene Silencing / Heparin / Morphogenesis / Organ Culture Techniques / Proprotein Convertases / Rats / Rats, Sprague-Dawley / Submandibular Gland
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1016/j.ydbio.2008.10.015
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 19013448
- ● Search Scopus @ Elsevier (PMID): 19013448
- ● Search Scopus @ Elsevier (DOI): 10.1016/j.ydbio.2008.10.015
(DOI: 10.1016/j.ydbio.2008.10.015, PubMed: 19013448) Xuefei Li, Ahmad Azlina, Mileva Ratko Karabasil, Nunuk Purwanti, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi :
Degradation of submandibular gland AQP5 by parasympathetic denervation of chorda tympani and its recovery by cevimeline, an M3 muscarinic agonist,
American Journal of Physiology, Gastrointestinal and Liver Physiology, Vol.295, No.1, G112-G123, 2008.- (要約)
- By chorda tympani denervation (CTD, parasympathectomy), the aquaporin 5 (AQP5), but not AQP1, protein level in the rat submandibular gland (SMG) was significantly decreased, dropping to 37% of that of the contralateral gland at 4 wk. The protein levels of AQP5 and AQP1 were not significantly affected by denervation of the cervical sympathetic trunk (sympathectomy). Administration of cevimeline hydrochloride, an M3 muscarinic receptor agonist (10 mg/kg for 7 days po), but not pilocarpine (0.3 mg/kg for 7 days po), recovered the AQP5 protein level reduced by CTD and increased the AQP1 protein level above the control one. The mRNA level of AQP5 was scarcely affected by CTD and cevimeline hydrochloride administration. Administration of chloroquine (50 mg/kg for 7 days po), a denaturant of lysosomes, increased the AQP5 protein level reduced by CTD. An extract obtained from the submandibular lysosomal fraction degraded the AQP5 protein in the total membrane fraction in vitro. These results suggest the possible regulation of the AQP5 protein level in the SMG by the parasympathetic nerves/M3 muscarinic receptor agonist and imply the involvement of lysosomal enzymes, but not a transcriptional mechanism, in this regulation.
- (キーワード)
- Animals / Aquaporin 1 / Aquaporin 5 / Chorda Tympani Nerve / Gene Expression Regulation / Lysosomes / Male / Muscarinic Agonists / Parasympathectomy / Pilocarpine / Quinuclidines / RNA, Messenger / Rats / Rats, Sprague-Dawley / Submandibular Gland / Sympathectomy / Thiophenes / Time Factors
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1152/ajpgi.00359.2007
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18450949
- ● Search Scopus @ Elsevier (PMID): 18450949
- ● Search Scopus @ Elsevier (DOI): 10.1152/ajpgi.00359.2007
(DOI: 10.1152/ajpgi.00359.2007, PubMed: 18450949) Gen Akabane, Yuji Ogushi, Takahiro Hasegawa, Masakazu Suzuki and Shigeyasu Tanaka :
Gene cloning and expression of an aquaporin (AQP-h3BL) in the basolateral membrane of water-permeable epithelial cells in osmoregulatory organs of the tree frog.,
American Journal of Physiology. Regulatory, Integrative and Comparative Physiology, Vol.292, No.6, R2340-R2351, 2007.- (要約)
- An aquaporin (Hyla AQP-h3BL), consisting of 292 amino acid residues, has been cloned from the urinary bladder of Hyla japonica. In a swelling assay using Xenopus oocytes, AQP-h3BL cRNA-injected oocytes developed a sevenfold and 2.8-fold higher permeability to water and glycerol, respectively, than the water-injected oocytes. This permeability was inhibited by HgCl2. Immunofluorescence revealed that AQP-h3BL is localized in the basolateral plasma membrane of both granular cells in the ventral pelvic and dorsal skins and the secretory cells in the mucous glands. Immunopositive cells were also observed in the basolateral membrane of principal cells in the collecting ducts and in a portion of the late distal tubules in the kidneys, as well as in the principal cells of the urinary bladder. Sequence homology suggests that AQP-h3BL is a homolog to mammalian AQP3. This conclusion is supported by the observed localization of AQP-h3BL to the basolateral membrane in water- and glycerol-permeable epithelial cells. In ventral pelvic skins and urinary bladders, water enters into the cytoplasm through the apical plasma membrane at sites where AQP-h2, sometimes in association with AQP-h3, responds to stimulation by vasotocin; the water exits throughout AQP-h3BL to extracellular spaces. In the mucous glands, on the other hand, water enters throughout this AQP-h3BL and exits through AQP-x5, which is in the apical membrane of secretory cells. Thus, water homeostasis in the frog body is regulated by AQP-h3BL expressed in the basolateral membrane in concert with arginine vasotocin (AVT)-dependent or AVT-independent AQP.
- (キーワード)
- Animals / Aquaporins / Cells, Cultured / Cloning, Molecular / Epithelial Cells / Organ Specificity / Ranidae / Recombinant Proteins / Water / Water-Electrolyte Balance
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1152/ajpregu.00905.2006
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17332153
- ● Search Scopus @ Elsevier (PMID): 17332153
- ● Search Scopus @ Elsevier (DOI): 10.1152/ajpregu.00905.2006
(DOI: 10.1152/ajpregu.00905.2006, PubMed: 17332153) Takahiro Hasegawa, Toshiyuki Matsuzaki, Yuki Tajika, Abduxukur Ablimit, Takeshi Suzuki, Takeo Aoki, Haruo Hagiwara and Kuniaki Takata :
Differential localization of aquaporin-2 and glucose transporter 4 in polarized MDCK cells.,
Histochemistry and Cell Biology, Vol.127, No.3, 233-241, 2007.- (要約)
- Membrane water channel aquaporin-2 (AQP2) and glucose transporter 4 (GLUT4) exhibit a common feature in that they are stored in intracellular storage compartments and undergo translocation to the plasma membrane upon hormonal stimulation. We compared the intracellular localization and trafficking of AQP2 and GLUT4 in polarized Madin-Darby canine kidney cells stably transfected with human AQP2 (MDCK-hAQP2) by immunofluorescence microscopy. When expressed in MDCK-hAQP2 cells, GLUT4 and GLUT4-EGFP were predominantly localized in the perinuclear region close to and within the Golgi apparatus, similar to endogenous GLUT4 in adipocytes and myocytes. In addition, GLUT4 was occasionally seen in EEA1-positive early endosomes. AQP2, on the other hand, was sequestered in subapical Rab11-positive vesicles. In the basal state, the intracellular storage site of GLUT4 was distinct from that of AQP2. Forskolin induced translocation of AQP2 from the subapical storage vesicles to the apical plasma membrane, which did not affect GLUT4 localization. When forskolin was washed out, AQP2 was first retrieved to early endosomes from the apical plasma membrane, where it was partly colocalized with GLUT4. AQP2 was then transferred to Rab11-positive storage vesicles. These results show that AQP2 and GLUT4 share a common compartment after retrieval from the plasma membrane, but their storage compartments are distinct from each other in polarized MDCK-hAQP2 cells.
- (キーワード)
- Animals / Aquaporin 2 / Cell Line / Cell Polarity / Dogs / Endosomes / Glucose Transporter Type 4 / Humans / Kidney / Microscopy, Confocal / Protein Transport / Transfection
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1007/s00418-006-0264-4
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17206499
- ● Search Scopus @ Elsevier (PMID): 17206499
- ● Search Scopus @ Elsevier (DOI): 10.1007/s00418-006-0264-4
(DOI: 10.1007/s00418-006-0264-4, PubMed: 17206499) Shinya Yajima, Makoto Kubota, Takashi Nakakura, Takahiro Hasegawa, Nobuto Katagiri, Hideaki Tomura, Yuichi Sasayama and Masakazu Suzuki :
Cloning and expression of vacuolar proton-pumping ATPase subunits in the follicular epithelium of the bullfrog endolymphatic sac.,
Zoological Science, Vol.24, No.2, 147-157, 2007.- (要約)
- In an investigation aimed at clarifying the mechanism of crystal dissolution of the calcium carbonate lattice in otoconia (the mineral particles embedded in the otolithic membrane) of the endolymphatic sac (ELS) of the bullfrog, cDNAs encoding the A- and E-subunits of bullfrog vacuolar proton-pumping ATPase (V-ATPase) were cloned and sequenced. The cDNA of the A-subunit consisted of an 11-bp 5'-untranslated region (UTR), a 1,854-bp open reading frame (ORF) encoding a protein comprising 617 amino acids with a calculated molecular mass of 68,168 Da, and a 248-bp 3'-UTR followed by a poly(A) tail. The cDNA of the E-subunit consisted of a 72-bp 5'-UTR, a 681-bp ORF encoding a protein of 226 amino acids with a calculated molecular mass of 26,020 Da, and a 799-bp 3'-UTR followed by a poly(A) tail. Western blot and immunofluorescence analyses using specific anti-peptide antisera against the V-ATPase A- and E-subunits revealed that these subunits were present in the ELS, urinary bladder, skin, testes, and kidneys. In the ELS, positive cells were scattered in the follicular epithelium which, as revealed by electron microscopy, corresponds to the location of mitochondria-rich cells. These findings suggest that V-ATPase, including the A- and E-subunits, exists in mitochondria-rich cells of the ELS, which might be involved in dissolution of the calcium carbonate crystals in the lumen of the ELS.
- (キーワード)
- Amino Acid Sequence / Animals / Base Sequence / Blotting, Western / Cloning, Molecular / DNA, Complementary / Endolymphatic Sac / Epithelium / Fluorescent Antibody Technique / Gene Expression Regulation, Enzymologic / Molecular Sequence Data / Rana catesbeiana / Vacuolar Proton-Translocating ATPases
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.2108/zsj.24.147
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17409728
- ● Summary page in Scopus @ Elsevier: 2-s2.0-34248559896
(DOI: 10.2108/zsj.24.147, PubMed: 17409728, Elsevier: Scopus) Makoto Kubota, Takahiro Hasegawa, Takashi Nakakura, Haruna Tanii, Masakazu Suzuki and Shigeyasu Tanaka :
Molecular and cellular characterization of a new aquaporin, AQP-x5, specifically expressed in the small granular glands of Xenopus skin.,
The Journal of Experimental Biology, Vol.209, No.16, 3199-3208, 2006.- (要約)
- A new toad aquaporin (AQP) cDNA was cloned from a cDNA library constructed from the ventral skin of Xenopus laevis. This AQP (Xenopus AQP-x5) consisted of 273 amino acid residues with a high sequence homology to mammalian AQP5. The predicted amino acid sequence contained the two conserved Asn-Pro-Ala motifs found in all major intrinsic protein (MIP) family members and six putative transmembrane domains. The sequence also contained a mercurial-sensitive cysteine and a putative phosphorylation motif site for protein kinase A at Ser-257. The swelling assay using Xenopus oocytes revealed that AQP-x5 facilitated water permeability. Expression of AQP-x5 mRNA was restricted to the skin, brain, lungs and testes. Immunofluorescence and immunoelectron microscopical studies using an anti-peptide antibody (ST-156) against the C-terminal region of the AQP-x5 protein revealed the presence of immunopositive cells in the skin, with the label predominately localized in the apical plasma membrane of the secretory cells of the small granular glands. These glands are unique both in being close to the epidermal layer of the skin and in containing mitochondria-rich cells with vacuolar H+-ATPase dispersed among its secretory cells. Results from immunohistochemical experiments on the mucous or seromucous glands of several other anurans verified this result. We conclude that the presence of AQP-x5 in the apical plasma membrane of the small granular glands suggests its involvement in water secretion from the skins. The physiological roles of the AQP-x5 protein in the small or mucous glands are discussed.
- (キーワード)
- Amino Acid Sequence / Animals / Anura / Aquaporin 5 / Base Sequence / Brain / Cloning, Molecular / Gene Library / Lung / Male / Molecular Sequence Data / Oocytes / Protein Structure, Tertiary / RNA, Messenger / Secretory Vesicles / Sequence Analysis, Protein / Sequence Homology, Amino Acid / Skin / Testis / Water / Xenopus Proteins / Xenopus laevis
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1242/jeb.02351
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16888067
- ● Search Scopus @ Elsevier (PMID): 16888067
- ● Search Scopus @ Elsevier (DOI): 10.1242/jeb.02351
(DOI: 10.1242/jeb.02351, PubMed: 16888067) Akio Nakashima, Takahiro Hasegawa, Saori Mori, Masaru Ueno, Shigeyasu Tanaka, Takashi Ushimaru, Shusei Sato and Masahiro Uritani :
A starvation-specific serine protease gene, isp6+, is involved in both autophagy and sexual development in Schizosaccharomyces pombe.,
Current Genetics, Vol.49, No.6, 403-413, 2006.- (要約)
- Schizosaccharomyces pombe isp6(+) gene encodes a vacuolar serine protease, which is specifically induced during nitrogen starvation. An isp6-disruption mutant, isp6Delta, grew normally under normal conditions but was defective in large-scale protein degradation during nitrogen starvation, a hallmark of autophagy. Vacuoles are the organelles for such drastic protein degradation but those of isp6Delta were apparently aberrant. isp6Delta was infertile under nitrogen source-free conditions with poor expression of ste11(+), a gene critical for sexual development. A protein kinase A-disruption mutant, pka1Delta, is prone to sexual development because expression of ste11(+) is derepressed. However, isp6Deltapka1Delta still showed defects in ste11(+) expression and sexual development under nitrogen source-free conditions. isp6Delta and isp6Deltapka1Delta were able to initiate sexual development to produce spores when only a small amount of a nitrogen source was present. Pat1 protein kinase negatively controls meiosis, and a temperature-sensitive mutant of pat1, pat1-114, initiates meiosis irrespective of ploidy at the restrictive temperature. However, isp6Deltapat1-114 did not start meiosis under nitrogen source-free conditions even at the restrictive temperature. These observations suggest that isp6(+) contributes to sexual development by providing a nitrogen source through autophagy.
- (キーワード)
- Autophagy / Epistasis, Genetic / Gene Expression Regulation, Fungal / Meiosis / Membrane Proteins / Nitrogen / Schizosaccharomyces / Schizosaccharomyces pombe Proteins / Serine Endopeptidases / Signal Transduction / Transcription Factors
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1007/s00294-006-0067-0
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16550352
- ● Search Scopus @ Elsevier (PMID): 16550352
- ● Search Scopus @ Elsevier (DOI): 10.1007/s00294-006-0067-0
(DOI: 10.1007/s00294-006-0067-0, PubMed: 16550352) Takahiro Hasegawa, Masakazu Suzuki and Shigeyasu Tanaka :
Immunocytochemical studies on translocation of phosphorylated aquaporin-h2 protein in granular cells of the frog urinary bladder before and after stimulation with vasotocin.,
Cell and Tissue Research, Vol.322, No.3, 407-415, 2005.- (要約)
- We have generated a specific antibody against phosphorylated aquaporin-h2 (pAQP-h2) protein to investigate the role of phosphorylation in the translocation of AQP-h2 protein within the granule cells of the urinary bladder of the frog (Hyla japonica). The antibody was generated against a synthetic peptide (ST-160) corresponding to amino acids 255-268, with a phosphorylated Ser-262, a residue that is putatively phosphorylated by protein A kinase. Using this antibody, we found, by Western blot analysis, that phosphorylation of the AQP-h2 protein rapidly increased within 2 min after vasotocin (AVT) stimulation and remained at a higher than normal level for 15 min. Moreover, quantitative immunoelectron microscopy indicated that the location of the AQP-h2 protein dramatically changed after AVT stimulation. Before stimulation, pAQP-h2 protein was localized in only a small number of intracellular vesicles near the nucleus of the granular cells, whereas the labeling density of the intracellular vesicles and the apical membrane rapidly increased after stimulation. This finding was also confirmed by the results of an immunofluorescence study. Thus, phosphorylation of AQP-h2 protein seems to be essential for translocation of the protein from the cytoplasmic pool to the apical plasma membrane of the granular cells in frog urinary bladder.
- (キーワード)
- Amino Acid Sequence / Animals / Antibodies / Antibody Specificity / Anura / Aquaporins / Blotting, Western / Enzyme-Linked Immunosorbent Assay / Fluorescent Antibody Technique / Immunohistochemistry / Microscopy, Immunoelectron / Molecular Sequence Data / Peptide Fragments / Phosphorylation / Urinary Bladder / Vasotocin
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1007/s00441-005-0037-8
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 16047161
- ● Search Scopus @ Elsevier (PMID): 16047161
- ● Search Scopus @ Elsevier (DOI): 10.1007/s00441-005-0037-8
(DOI: 10.1007/s00441-005-0037-8, PubMed: 16047161) Shigeyasu Tanaka, Takahiro Hasegawa, Haruna Tanii and Masakazu Suzuki :
Immunocytochemical and phylogenetic distribution of aquaporins in the frog ventral skin and urinary bladder.,
Annals of the New York Academy of Sciences, Vol.1040, 483-485, 2005.- (要約)
- We recently cloned three cDNAs encoding frog aquaporin (AQP-h1, BAC07470; AQP-h2, BAC82379; and AQP-h3, BAC07471) from the ventral pelvic skin of the tree frog, Hyla japonica. The present study demonstrated that Hyla AQP-h2 was translocated from cytoplasmic pools to the apical plasma membranes of the granular cells in the bladder after antidiuretic hormone stimulation and that Hyla AQP-h2 and AQP-h3 behaved similarly in the ventral pelvic skin. Further, we found that terrestrial and tree frogs, but not aquatic and semiterrestrial-adapted frogs, absorbed water from their ventral pelvic skin by AQP-h3-like protein in concert with AQP-h2-like protein.
- (キーワード)
- Animals / Anura / Aquaporin 1 / Aquaporin 2 / Aquaporin 3 / Aquaporins / Bufonidae / Immunohistochemistry / Phylogeny / Rana catesbeiana / Skin / Urinary Bladder / Xenopus laevis
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1196/annals.1327.097
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15891096
- ● Search Scopus @ Elsevier (PMID): 15891096
- ● Search Scopus @ Elsevier (DOI): 10.1196/annals.1327.097
(DOI: 10.1196/annals.1327.097, PubMed: 15891096) Takahiro Hasegawa, Yuriko Sugawara, Masakazu Suzuki and Shigeyasu Tanaka :
Spatial and temporal expression of the ventral pelvic skin aquaporins during metamorphosis of the tree frog, Hyla japonica.,
The Journal of Membrane Biology, Vol.199, No.2, 119-126, 2004.- (要約)
- Most adult anurans absorb water through their ventral skin to maintain the proper water balance. We examined spatial and temporal expression of frog (Hyla japonica) aquaporins, Hyla AQP-h2 and AQP-h3 proteins, in the ventral pelvic skin by using specific antibodies. Immunofluorescence indicates that AQP-h2 and AQP-h3 first appear in the granular cells of the pelvic skin of the tadpoles at Gosner stage 42, and such labeling is seen in later stages as well. These findings were confirmed by Western blot analysis. In addition, Northern blot analysis demonstrated that V2-type vasotocin (AVT)-receptor mRNA is first expressed at the same stage as are the AQP proteins, which suggests a functional relationship between expression of AQP proteins and AVT receptor. Also, AQP expression in the ventral pelvic skin is consistent with the morphological changes that occur in the skin for adaptation from life in water to that on land.
- (キーワード)
- Animals / Anura / Aquaporins / Larva / Metamorphosis, Biological / Pelvis / Receptors, Vasopressin / Skin / Tissue Distribution
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1007/s00232-004-0677-8
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 15383922
- ● Search Scopus @ Elsevier (PMID): 15383922
- ● Search Scopus @ Elsevier (DOI): 10.1007/s00232-004-0677-8
(DOI: 10.1007/s00232-004-0677-8, PubMed: 15383922) Takahiro Hasegawa, Haruna Tanii, Masakazu Suzuki and Shigeyasu Tanaka :
Regulation of water absorption in the frog skins by two vasotocin-dependent water-channel aquaporins, AQP-h2 and AQP-h3.,
Endocrinology, Vol.144, No.9, 4087-4096, 2003.- (要約)
- A new frog aquaporin (AQP) cDNA was cloned from a cDNA library constructed from the ventral skin of the tree frog Hyla japonica. This AQP (Hyla AQP-h2) consisted of 268 amino acid residues with a high homology to mammalian AQP2. The predicted amino acid sequence contained the two conserved Asn-Pro-Ala motifs found in all the major intrinsic protein family members and the putative six transmembrane domains. The sequence also contained a mercurial compound: cysteine, one potential N-glycosylation site at Asn-124, and a putative phosphorylation site recognized by protein kinase A at Ser-262. In a swelling assay using Xenopus oocytes, AQP-h2 facilitated water permeability, especially in response to cAMP. Expression of AQP-h2 mRNA was restricted to several tissues including the ventral skin, kidney, and urinary bladder; but with immunofluorescence staining using an antipeptide antibody (ST-140) against the AQP-h2 protein, immunopositive cells were found only in the ventral skin and urinary bladder. In the ventral pelvic skin, the label for AQP-h2 was localized in the entire plasma membrane of the granular cells beneath the outmost layer of the skin and in the basolateral membrane of the granular cells in this layer. In response to vasotocin, however, the label for AQP-h2 became more intense in the apical membrane in the granular cells of the outermost layer, similar to the case for the earlier studied AQP-h3, which was specifically expressed in the ventral skin. Taken together, these findings suggest that not only AQP-h3, but also AQP-h2 acts as a regulator of the water balance in this frog.
- (キーワード)
- Amino Acid Sequence / Animals / Antibody Specificity / Anura / Aquaporins / Base Sequence / Biological Transport / Cloning, Molecular / DNA, Complementary / Epidermis / Gene Expression / Molecular Sequence Data / Oocytes / RNA, Messenger / Vasotocin / Water / Water-Electrolyte Balance / Xenopus laevis
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1210/en.2003-0418
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12933683
- ● Search Scopus @ Elsevier (PMID): 12933683
- ● Search Scopus @ Elsevier (DOI): 10.1210/en.2003-0418
(DOI: 10.1210/en.2003-0418, PubMed: 12933683) Takashi Ushimaru, Takahiro Hasegawa, Toyoki Amano, Masao Katayama, Shigeyasu Tanaka and Hideo Tsuji :
Chloroplasts in seeds and dark-grown seedlings of lotus.,
Journal of Plant Physiology, Vol.160, No.3, 321-324, 2003.- (要約)
- In most higher plants, mature dry seeds have no chloroplasts but etioplasts. Here we show that in a hydrophyte, lotus (Nelumbo nucifera), young chloroplasts already exist in shoots of mature dry seeds and that they give rise to mature chloroplasts during germination, even in darkness. These shoots contain chlorophyll and chlorophyll-binding proteins CP1 and LHCP. The unique features of chloroplast formation in N. nucifera suggest a unique adaptive strategy for seedling development correlated with the plant's habitat.
- (キーワード)
- Adaptation, Physiological / Chlorophyll / Chloroplasts / Darkness / Germination / Light / Light-Harvesting Protein Complexes / Lotus / Microscopy, Electron / Photosynthetic Reaction Center Complex Proteins / Plant Shoots / Seeds
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1078/0176-1617-00964
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12749089
- ● Search Scopus @ Elsevier (PMID): 12749089
- ● Search Scopus @ Elsevier (DOI): 10.1078/0176-1617-00964
(DOI: 10.1078/0176-1617-00964, PubMed: 12749089) Haruna Tanii, Takahiro Hasegawa, Noboru Hirakawa, Masakazu Suzuki and Shigeyasu Tanaka :
Molecular and cellular characterization of a water-channel protein, AQP-h3, specifically expressed in the frog ventral skin.,
The Journal of Membrane Biology, Vol.188, No.1, 43-53, 2002.- (要約)
- Two cDNAs encoding frog aquaporin (AQP) were cloned from a cDNA library constructed for the ventral skin of the tree frog, Hyla japonica and sequenced. One AQP (Hyla AQP-h1) consisted of 271 amino-acid residues with high homology to toad AQP-t1, Rana CHIP28 (AQP1), and rat AQP1. The other AQP (AQP-h3) consisted of 271 amino-acid residues with higher homology to mammalian AQP2 than to mammalian AQP3. The predicted amino-acid sequence contained the conserved two NPA motifs found in all MIP family members and the putative six transmembrane domains. The sequence also confers mercurial sensitivity, which is common to all the AQPs except AQP0, AQP4 and AQP7. Potential N-glycosylation sites were present at Asn-44 in AQP-h1, and at Asn-124 and Asn-125 in AQP-h3. In addition, AQP-h3 had a putative phosphorylation site by protein kinase A at Ser-255, which is identical to mammalian AQP2. In swelling assays using Xenopus oocytes, AQP-h1 facilitates water permeability, whereas AQP-h3 displayed weak water permeability. Searching for the expression of these two AQP mRNAs revealed that AQP-h1 was expressed in most tissues, whereas AQP-h3 was observed only in the ventral skin. An antibody (ST-141) against the C-terminal peptide of the AQP-h3 protein recognized a 29.0 kDa-protein with a molecular mass close to that of the Hyla AQP-h3 protein and immunostained predominantly in the abdominal pelvic skin. In pelvic skin, the label for AQP-h3 was more intense in the upper layer of the stratum granulosum and was localized to both the apical and basolateral plasma membranes of the principal cells. These findings suggest that Hyla AQP-h3 plays a pivotal role in constitutively absorbing water from ventral pelvic skin.
- (キーワード)
- Animals / Anura / Aquaporins / Base Sequence / DNA, Complementary / Gene Expression / Gene Expression Regulation / Gene Library / Molecular Sequence Data / Oocytes / Pelvis / Reverse Transcriptase Polymerase Chain Reaction / Sequence Analysis, DNA / Skin / Xenopus
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1007/s00232-001-0172-4
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 12172646
- ● Search Scopus @ Elsevier (PMID): 12172646
- ● Search Scopus @ Elsevier (DOI): 10.1007/s00232-001-0172-4
(DOI: 10.1007/s00232-001-0172-4, PubMed: 12172646) - MISC
- Chenjuan Yao, Tetsuya Akamatsu, Takahiro Hasegawa and Hiroshi Yoshimura :
The Defense System of Oral Cavity: Lipopolysaccharide Induced Inflammatory Response in the Mice Salivary Gland,
BIT's 1st Annual World Congress of Oral & Dental Medicine Conference Abstract Book, 107, 2014.- (キーワード)
- 唾液腺 (salivary gland) / 炎症 (inflammation) / 炎症性サイトカイン (inflammatory cytokine) / リポ多糖
Salivary Gland Development, Differentiation, and Regeneration - Role of Subtilisin-like Proprotein Convertase PACE4/SPC4,
BIT's 1st Annual World Congress of Oral & Dental Medicine Conference Abstract Book, 59, 2014.- (キーワード)
- 唾液腺 (salivary gland) / 発生 (development) / 分化 (differentiation) / 再生 (regeneration) / 前駆体蛋白質変換酵素
ユビキチンリガーゼによるAQP5のユビキチン化亢進とダウンレギュレーション,
Journal of Oral Biosciences, Vol.Suppl., 204, 2014年.- (キーワード)
- 水チャネル (water channel) / ユビキチン化 / ダウンレギュレーション / AQP5
唾液腺再生モデルにおける水チャネルAQP5の発現,
Journal of Oral Biosciences, Vol.Suppl., 204, 2014年.- (キーワード)
- 唾液腺 (salivary gland) / 再生 (regeneration) / 水チャネル (water channel) / AQP5
唾液腺再生モデルにおけるサチライシン様前駆体蛋白質変換酵素の発現誘導,
Journal of Oral Biosciences, Vol.Suppl., 138, 2014年.- (キーワード)
- 唾液腺 (salivary gland) / 再生 (regeneration) / 前駆体蛋白質変換酵素
- 総説・解説
- Kazuo Hosoi, Chenjuan Yao, Takahiro Hasegawa, Hiroshi Yoshimura and Tetsuya Akamatsu :
Dynamics of Salivary Gland AQP5 under Normal and Pathologic Conditions,
International Journal of Molecular Sciences, Vol.21, No.4, 1182, Feb. 2020.- (徳島大学機関リポジトリ)
- ● Metadata: 114575
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.3390/ijms21041182
- (文献検索サイトへのリンク)
- ● Summary page in Scopus @ Elsevier: 2-s2.0-85079334066
(徳島大学機関リポジトリ: 114575, DOI: 10.3390/ijms21041182, Elsevier: Scopus) Kuniaki Takata, Toshiyuki Matsuzaki, Yuki Tajika, Abduxukur Ablimit and Takahiro Hasegawa :
Localization and trafficking of aquaporin 2 in the kidney.,
Histochemistry and Cell Biology, Vol.130, No.2, 197-209, Jun. 2008.- (要約)
- Aquaporins (AQPs) are membrane proteins serving in the transfer of water and small solutes across cellular membranes. AQPs play a variety of roles in the body such as urine formation, prevention from dehydration in covering epithelia, water handling in the blood-brain barrier, secretion, conditioning of the sensory system, cell motility and metastasis, formation of cell junctions, and fat metabolism. The kidney plays a central role in water homeostasis in the body. At least seven isoforms, namely AQP1, AQP2, AQP3, AQP4, AQP6, AQP7, and AQP11, are expressed. Among them, AQP2, the anti-diuretic hormone (ADH)-regulated water channel, plays a critical role in water reabsorption. AQP2 is expressed in principal cells of connecting tubules and collecting ducts, where it is stored in Rab11-positive storage vesicles in the basal state. Upon ADH stimulation, AQP2 is translocated to the apical plasma membrane, where it serves in the influx of water. The translocation process is regulated through the phosphorylation of AQP2 by protein kinase A. As soon as the stimulation is terminated, AQP2 is retrieved to early endosomes, and then transferred back to the Rab 11-positive storage compartment. Some AQP2 is secreted via multivesicular bodies into the urine as exosomes. Actin plays an important role in the intracellular trafficking of AQP2. Recent findings have shed light on the molecular basis that controls the trafficking of AQP2.
- (キーワード)
- Animals / Aquaporin 2 / Cyclic AMP-Dependent Protein Kinases / Glucose Transporter Type 4 / Humans / Kidney / Kidney Diseases / Protein Transport / Rats / Vesicular Transport Proteins / rab GTP-Binding Proteins
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1007/s00418-008-0457-0
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 18566824
- ● Search Scopus @ Elsevier (PMID): 18566824
- ● Search Scopus @ Elsevier (DOI): 10.1007/s00418-008-0457-0
(DOI: 10.1007/s00418-008-0457-0, PubMed: 18566824) Masakazu Suzuki, Takahiro Hasegawa, Yuji Ogushi and Shigeyasu Tanaka :
Amphibian aquaporins and adaptation to terrestrial environments: a review.,
Comparative Biochemistry and Physiology. Part A: Molecular & Integrative Physiology, Vol.148, No.1, 72-81, Sep. 2007.- (要約)
- In many anurans, the pelvic patch of the ventral skin and the urinary bladder are important osmoregulatory organs. Since the discovery of water channel protein, aquaporin (AQP), in mammalian erythrocytes, 17 distinct full sequences of AQP mRNAs have been identified in anurans. Phylogenetic tree of AQP proteins from amphibians and mammals suggested that anuran AQPs can be divided into six types: i.e. types 1, 2, 3, and 5, and anuran-specific types a1 and a2. Among them, two types of anuran AQPs (types 1 and a2) are localized in the skin and urinary bladder by immunohistochemistry. Tree frog type-a2 AQPs, AQP-h2 and AQP-h3, are vasotocin-regulated water channels predominant in the osmoregulatory organs. Both the AQP-h2 and AQP-h3 are expressed at the granular cells underneath the keratinized layer in the pelvic patch, whereas only AQP-h2 is detected at the granular cells in the urinary bladder. In response to vasotocin, both the molecules seem to be translocated from the cytoplasmic pool to the apical plasma membrane of the granular cells. On the other hand, type-1 AQPs, Rana FA-CHIP and Hyla AQP-h1, are detected at the endothelial cells of blood capillaries in frog osmoregulatory organs. These findings suggest that AQP-h2 and AQP-h3 are key players for transepithelial water movement, and that FA-CHIP and AQP-h1 might be important for the transport of absorbed water into the blood flow. Comparative investigation of type-a2 AQPs in anurans further revealed that AQP-h2 and -h3-like molecules might exist at the urinary bladder and the pelvic skin, respectively, in various anurans from aquatic species to arboreal dwellers. AQP-h2-like protein is also detected in the pelvic skin of terrestrial and arboreal species. It is possible that this molecule might have occurred in the pelvic skin as anurans penetrated into drier environments.
- (キーワード)
- Adaptation, Physiological / Amino Acid Sequence / Amphibians / Animals / Ecosystem / Molecular Sequence Data
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.1016/j.cbpa.2006.12.021
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 17270476
- ● Search Scopus @ Elsevier (PMID): 17270476
- ● Search Scopus @ Elsevier (DOI): 10.1016/j.cbpa.2006.12.021
(DOI: 10.1016/j.cbpa.2006.12.021, PubMed: 17270476) - 講演・発表
- Yuka Hiroshima, Mika Bandou, Takahiro Hasegawa, Yuji Inagaki and Chie Wada -Mihara :
Resistin release from neutrophils is induced by Porphyromonas gingivalis lipopolysaccharide.,
IADR (International Association of Dental Research) Barcelona, Spain, July 14-17, 2010, Chenjuan Yao, Tetsuya Akamatsu, Takahiro Hasegawa and Hiroshi Yoshimura :
Induced expression of a subtilisin-like proprotein convertase PACE4 in the regeneration model of rat submandibular gland.,
The 4th International Symposium on Salivary Glands in Honor of Niels Stensen, Okazaki (Japan), Nov. 2016. Tetsuya Akamatsu, Chenjuan Yao, Takahiro Hasegawa and Hiroshi Yoshimura :
Sexual difference in the regeneration model of the rat submandibular gland.,
The 4th International Symposium on Salivary Glands in Honor of Niels Stensen, Okazaki (Japan), Nov. 2016. Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Hiroshi Yoshimura :
Post-translational modifications of water channel aquaporin-5 in salivary gland cells, Oral Neuroscience 2016,
Oral Neuroscience 2016, Osaka, Oct. 2016. Hiroshi Yoshimura, Tetsuya Akamatsu, Chenjuan Yao and Takahiro Hasegawa :
Synaptic plasticity in the brain -Roles of NMDA receptor- (Invited lecture at Nantong University),
Sep. 2016.- (キーワード)
- synaptic plasticity / NMDA受容体 (NMDA-receptors)
The Defense System of Oral Cavity: Lipopolysaccharide Induced Inflammatory Response in the Mice Salivary Gland,
BIT's 1st Annual International Congress of Oral & Dental Medicine, Session 9: Oral Immunological Diseases, Allergy and Inflammation, Haikou, China, Nov. 2014.- (キーワード)
- 唾液腺 (salivary gland) / 炎症 (inflammation) / 炎症性サイトカイン (inflammatory cytokine) / リポ多糖
Salivary Gland Development, Differentiation, and Regeneration - Role of Subtilisin-like Proprotein Convertase PACE4/SPC4,
BIT's 1st Annual International Congress of Oral & Dental Medicine, Session 3: Oral Biology, Haikou, China, Nov. 2014.- (キーワード)
- 唾液腺 (salivary gland) / 発生 (development) / 分化 (differentiation) / 再生 (regeneration) / 前駆体蛋白質変換酵素
Effects of natural point mutation of rat aquaporin 5 expressed in vitro on its capacity of water permeability and membrane trafficking,
The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 398-400, Tokushima, Dec. 2009.- (要約)
- In the colony of Sprague-Dawley (SD) strain, we found that there were rats expressing a mutant AQP5, which has a point mutation at nt 308 (G308A), leading to a replacement of (103)Gly with (103)Asp in the 3rd transmembrane domain. The mutant molecule scarcely expressed in the acinar cells, probably because of ineffective trafficking. The mutant molecule, however, showed normal water permeability when assessed by the oocyte system.
- (キーワード)
- Amino Acid Sequence / Animals / Aquaporin 5 / Biological Transport / Cell Membrane Permeability / Female / Models, Animal / Molecular Sequence Data / Oocytes / Point Mutation / Rats / Rats, Sprague-Dawley / Submandibular Gland / 水チャネル (water channel) / Xenopus laevis
- (徳島大学機関リポジトリ)
- ● Metadata: 111488
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.2152/jmi.56.398
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224238
- ● Search Scopus @ Elsevier (PMID): 20224238
- ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.398
(徳島大学機関リポジトリ: 111488, DOI: 10.2152/jmi.56.398, PubMed: 20224238) Purevjav Javkhlan, Yuka Hiroshima, Azlina Ahmad, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Jun-ichi Kido, Toshihiko Nagata and Kazuo Hosoi :
Induction of calprotectin mRNAs by lipopolysaccharide in the salivary gland of mice,
The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 287-289, Tokushima, Dec. 2009.- (要約)
- Calprotectin is a major cytosolic calcium-binding protein of leukocytes which belongs to the S100 protein family. S100A8 and S100A9, major types of calprotectin are heterodimeric complexes being composed of light- and heavy-chain subunits. The calprotectin levels in the plasma, feces, synovial fluid, gingival crevicular fluid, dental calculus and saliva change when the host animal suffers from several inflammatory diseases. Members of Toll-like receptor (TLR) family are pattern-recognition receptors for lipopolysaccharide (LPS) and other pathogens. Here we examined if the biological role of TLR receptor is reflected to the calprotectin expression in the salivary gland. Time course study by using real-time RT-PCR detected higher levels of S100A8 and S100A9 mRNA at 1.5-3 h after injection of LPS in both the submandibular gland (SMG) and parotid gland (PG) of C3H/HeN mice but not in the same tissues of C3H/HeJ, a TLR-4 mutant strain, indicating that this induction is mediated via the TLR-4. These results indicate that, an inflammatory marker, calprotectin, is expressed in the mouse salivary gland and that LPS stimulated its synthesis. Calprotectin (S100A8/A9) showed minimum expression in all cellular segments in the SMG except excretory duct cells, which showed strong signal at the cytoplasm. LPS induced their expressions in the granular convoluted tubular cells and striated duct cells. In the PG, these proteins were expressed very weakly in both duct and acinar cells with a little stronger staining for the former cells. LPS injection induced calprotectin (S100A8/A9) in both duct and acinar cells especially in the former cells.
- (キーワード)
- Animals / Calgranulin A / Calgranulin B / Leukocyte L1 Antigen Complex / Lipopolysaccharides / Mice / Mice, Inbred C3H / Mice, Mutant Strains / Parotid Gland / RNA, Messenger / 唾液腺 (salivary glands) / Submandibular Gland / Toll-Like Receptor 4
- (徳島大学機関リポジトリ)
- ● Metadata: 111354
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.2152/jmi.56.287
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224205
- ● Search Scopus @ Elsevier (PMID): 20224205
- ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.287
(徳島大学機関リポジトリ: 111354, DOI: 10.2152/jmi.56.287, PubMed: 20224205) Azlina Ahmad, Xuefei Li, Purevjav Javkhlan, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi :
Down-regulation of submandibular gland AQP5 following parasympathetic denervation in rats,
The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 273-276, Tokushima, Dec. 2009.- (要約)
- Following chorda tympani denervation (CTD, parasympathetomy), the protein levels of aquaporin5 (AQP5) as well as AQP1 and Na(+)K(+)ATPase alpha-subunit in the rat submandibular gland (SMG) were found to be decreased significantly. However, the level of another membrane protein, dipeptidyl peptidase IV was not affected by CTD, suggesting a selective reduction of AQP5, AQP1, and Na(+)K(+)ATPase alpha -subunit proteins by CTD. However, the AQP5 mRNA level was scarcely affected by CTD, which suggested that transcription process of AQP5 was unaffected by this operation. AQP5 protein was shown to be degraded in vitro by the extract of the SMG obtained from normal rat; inhibitor experiments in vitro suggested cathepsin B was a responsible enzyme. Co-localization of AQP5 and LAMP-2, a lysosomal marker, implicated AQP5 is degraded in lysosomes. A significant increase in the protein levels of LC3-II, an autophagy marker, at day 1 after CTD, and co-localization of the LC3 protein and AQP5, suggested that CTD activated autophagy of SMG, leading to AQP5 degradation.
- (キーワード)
- Animals / Aquaporin 1 / Aquaporin 5 / オートファジー (autophagy) / Chorda Tympani Nerve / Down-Regulation / Lysosomal-Associated Membrane Protein 2 / Male / Microtubule-Associated Proteins / Parasympathectomy / RNA, Messenger / Rats / Rats, Sprague-Dawley / Sodium-Potassium-Exchanging ATPase / Submandibular Gland
- (徳島大学機関リポジトリ)
- ● Metadata: 111348
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.2152/jmi.56.273
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224200
- ● Search Scopus @ Elsevier (PMID): 20224200
- ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.273
(徳島大学機関リポジトリ: 111348, DOI: 10.2152/jmi.56.273, PubMed: 20224200) Nunuk Purwanti, Azlina Ahmad, Mileva Ratko Karabasil, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi :
Involvement of the IL-6/STAT3/Sca-1 system in proliferation of duct cells following duct ligation in the submandibular gland of mice,
The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 253-254, Tokushima, Dec. 2009.- (要約)
- Ligation of the main excretory duct (MED) of the mouse submandibular gland (SMG) induced the expression of Sca-1, a stem cell marker. Sca-1 expression increased prominently in almost all of cells in the duct system, except the acinar cells. Sca-1 induction was accompanied with phosphorylated-STAT3 (Y705) elevation, which was localized in the nuclei of all duct cells. Electrophoretic mobility shift assay (EMSA) confirmed the specific binding of STAT3 to the GAS sequence, a biding site of gamma interferon activating site. Present study suggested one of the initial steps of the tissue regeneration after injury includes STAT3 pathway.
- (キーワード)
- Animals / Antigens, Ly / Cell Proliferation / 炎症 (inflammation) / Interleukin-6 / Ligation / male / Membrane Proteins / Mice / Mice, Inbred C57BL / 再生 (regeneration) / STAT3 Transcription Factor / シグナル伝達 (signal transduction) / Submandibular Gland
- (徳島大学機関リポジトリ)
- ● Metadata: 111340
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.2152/jmi.56.253
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224192
- ● Search Scopus @ Elsevier (PMID): 20224192
- ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.253
(徳島大学機関リポジトリ: 111340, DOI: 10.2152/jmi.56.253, PubMed: 20224192) Tetsuya Akamatsu, Azlina Ahmad, Purevjav Javkhlan, Takahiro Hasegawa, Chenjuan Yao and Kazuo Hosoi :
Salivary Gland Development: Its mediation by a subtilisin-like proprotein convertase, PACE4,
The Journal of Medical Investigation : JMI, Vol.56, No.Suppl, 241-246, Tokushima, Dec. 2009.- (要約)
- The submandibular gland (SMG) develops under the epithelial-mesenchymal interaction. Its process is regulated by various growth/differentiation factors, which are synthesized as inactive precursors and activated via the limited proteolysis at their multi basic amino acid site(s) such as Arg-X-Lys/Arg-Arg. Although many of these processing steps are elucidated to be catalyzed by subtilisin-like proprotein convertases (SPCs), little is known about the role of SPCs in the SMG development. Here, we focused upon the physiological role of PACE4 (SPC4), a member of SPC family, in the SMG development. In the organ culture system of rat embryonic SMG (E15), Dec-RVKR-CMK, a potent inhibitor for SPCs, inhibited the salivary branching and the expression of an exocrine gland type water channel, AQP5. However, other peptidyl-CMKs and inhibitors for trypsin-like serine proteases including leupeptin did not affect the salivary branching and AQP5 expression. Dec-RVKR-CMK also suppressed the expression of PACE4, but not furin, another member of the family. The specific antibody for the catalytic domain of PACE4 suppressed the salivary branching and AQP5 expression similarly. These inhibitory effects of Dec-RVKR-CMK were partially rescued by the addition of recombinant BMP2 whose precursor is a candidate for the physiological substrates of PACE4. Further, the transcriptional silencing of PACE4 by its specific siRNAs caused the suppression of both the salivary branching and AQP5 expression in the present organ culture system. These observations strongly support the idea that PACE4 mediates the SMG development.
- (キーワード)
- Animals / Aquaporin 5 / Bone Morphogenetic Protein 2 / Morphogenesis / Proprotein Convertases / Rats / Salivary Glands / Signal Transduction
- (徳島大学機関リポジトリ)
- ● Metadata: 111337
- (出版サイトへのリンク)
- ● Publication site (DOI): 10.2152/jmi.56.241
- (文献検索サイトへのリンク)
- ● PubMed @ National Institutes of Health, US National Library of Medicine (PMID): 20224189
- ● Search Scopus @ Elsevier (PMID): 20224189
- ● Search Scopus @ Elsevier (DOI): 10.2152/jmi.56.241
(徳島大学機関リポジトリ: 111337, DOI: 10.2152/jmi.56.241, PubMed: 20224189) Chenjuan Yao, Ahmad Azlina, Javkhlan Purevjav, Takahiro Hasegawa, Tetsuya Akamatsu and Kazuo Hosoi :
Potential down-regulation of parotid gland AQP5 by LPS via cross-coupling of NF-κB/AP1,
The 11th International Symposium on Exocrine Secretion, Tokushima 09 ''Exocrine Secretion Mechanism and Disease'', Tokushima, Jul. 2009. Ahmad Azlina, Nunuk Purwanti, Mileva R. Karabasil, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Kazuo Hosoi :
Is AQP5 down-regulated via autophagic pathway following chorda tympani denervation?,
The International Symposium on Oral Sciences to Improve the Quality of Life, organized by Toshihiko Nagata, Tokushima, Sep. 2008. Mileva R. Karabasil, Takahiro Hasegawa, Ahmad Azlina, Nunuk Purwanti, Chenjuan Yao, Tetsuya Akamatsu, Shigemasa Tomioka and Kazuo Hosoi :
Analyses of rat AQP5 G103D mutant expressed in MDCK-II cells and Xenopus oocytes,
The International Symposium on Oral Sciences to Improve the Quality of Life, organized by Toshihiko Nagata, Tokushima, Sep. 2008. Nunuk Puwanti, Daisuke Tsuji, Mileva Ratko Karabasil, Chenjuan Yao, Takahiro Hasegawa, Tetsuya Akamatsu, Kouji Itou and Kazuo Hosoi :
Activation of IL-6/STAT3/Sca-1 system induces proliferation of duct cells in the duct-ligated mouse submandibular gland,
The 2nd International Symposium on The Future Direction of Oral Sciences in The 21st Century-Oral Sciences for Our Healthy Life-, organized by Toshihiko Nagata, Tokushima, Dec. 2007. Mileva R. Karabasil, Kwartarini Murdiastuti, Takahiro Hasegawa, Nunuk Purwanti, Ahmad Azlina, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi :
A naturally occurring point mutation in rat AQP5 influencing its membrane trafficking in and water secretion from salivary gland,
The 5th International Conference of Aquaporin, Nara, Jul. 2007. Mileva R. Karabasil, Takahiro Hasegawa, Nunuk Purwanti, Kwartarini Murdiastuti, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi :
Point mutation of AQP5 in Sprague-Dawley rats and its implication for salivary gland physiology,
The 1st International Symposium and Workshop on The Future Direction of Oral Sciences in The 21st Century, organized by Bando, E., Awaji, Mar. 2007. Mileva R. Karabasil, Takahiro Hasegawa, Nunuk Purwanti, Kwartarini Murdiastuti, Xuefei Li, Chenjuan Yao, Tetsuya Akamatsu, Norio Kanamori and Kazuo Hosoi :
Molecular and cellular analyses of mutant AQP5 which occurred naturally in Spraque - Dawley rats,
3rd International Symposium on Salivary Glands in Honor of Niels Stensen, Okazaki, Japan, Oct. 2006. 平田 愛佳, 佐藤 匠, 田中 寛人, 増田 尚輝, 姚 陳娟, 向井 理恵, 長谷川 敬展, 吉村 弘, 渡辺 崇人, 三戸 太郎, 赤松 徹也 :
食品成分が唾液腺機能に及ぼす影響,
第34回唾液腺談話会, 2022年9月. 福田 崇子, 楠 進太郎, 前田 さおり, 長谷川 敬展, 姚 陳娟, 赤松 徹也, 吉村 弘 :
周辺環境が主観的感覚および摂食行動に及ぼす影響:筋電図を用いた研究,
日本味と匂学会第55回大会, 2021年9月. 楠 進太郎, 福田 崇子, 前田 さおり, 姚 陳娟, 長谷川 敬展, 赤松 徹也, 吉村 弘 :
快・不快環境下における脳活動と摂食行動の関連性,
第55回日本味と匂い学会, 2021年9月. 佐藤 匠, 姚 陳娟, 長谷川 敬展, 吉村 弘, 赤松 徹也 :
サチライシン様前駆体蛋白質変換酵素PACE4のラット顎下腺発生過程における局在,
第62回歯科基礎医学会学術大会, 2020年9月. 佐藤 匠, 姚 陳娟, 長谷川 敬展, 吉村 弘, 赤松 徹也 :
ラット唾液腺発生過程におけるサチライシン様前駆体蛋白質変換酵素PACE4の局在,
第93回日本生化学会大会, 2020年9月. Maeda Saori, Hiroshi Yoshimura, Miyaji Yuji, Hiroyuki Kanayama, Takahiro Hasegawa, Chenjuan Yao and Tetsuya Akamatsu :
Increase in theta-band EEG activities under tasting chocolate with unmatched odor stimulation,
第41回日本神経科学大会, Jul. 2018.- (キーワード)
- 脳波 (electroencephalogram) / シータ波
匂いと味の不一致が引き起こすシータ波領域脳活動,
第95回日本生理学大会, 2018年3月. 前田 さおり, 宮地 裕司, 金山 宏幸, 長谷川 敬展, 姚 陳娟, 赤松 徹也, 吉村 弘 :
甘味とニオイのミスマッチが甘味認知に与える影響,
第69回日本生理学会中国・四国地方会, 2017年10月. 畑 美緒, 赤松 徹也, 姚 陳娟, 前田 さおり, 宮地 裕司, 金山 宏幸, 長谷川 敬展, 吉村 弘 :
唾液腺再生モデルにおける雌雄差の影響,
第69回日本生理学会中国・四国地方会, 2017年10月. 前田 さおり, 吉村 弘, 宮地 ゆうじ, 長谷川 敬展, 姚 陳娟, 赤松 徹也 :
味と匂いのミスマッチが味覚認知に与える影響:脳波周波数分析を用いた研究,
日本味と匂学会第51回大会, 2017年9月. 吉村 弘, 須貝 外喜夫, 加藤 伸郎, 冨永 貴志, 冨永 洋子, 長谷川 敬展, 姚 陳娟, 赤松 徹也 :
カフェイン投与により誘発される視覚野オシレーション におけるnon-NMDA受容体とNMDA受容体の相互交錯的関与,
第40回日本神経科学大会, 2017年7月. Maeda Saori, Miyachi Yuki, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu and Hiroshi Yoshimura :
Influences of olfactory stimulation on taste perception: An electroencephalogram frequency analysis study,
The 94th Annual Meeting of the Physiological Science of Japan, Mar. 2017.- (キーワード)
- taste perception / olfaction / 脳波 (electroencephalogram)
唾液腺再生過程で見られる雌雄差について,
第58回歯科基礎医学会学術大会, 2016年8月. 嶋谷 達哉, 嶺岸 誠, 赤松 徹也, 姚 陳娟, 長谷川 敬展, 吉村 弘 :
唾液腺再生モデルにおけるサチライシン様前駆体蛋白質変換酵素PACE4の発現誘導-Part II-,
第58回歯科基礎医学会学術大会, 2016年8月. Hiroshi Yoshimura, 川邊 真道, 須貝 外喜夫, 加藤 伸郎, Takahiro Hasegawa, Chenjuan Yao and Tetsuya Akamatsu :
Influences of oral impairment on neural oscilltion and wave propagation in the neocortex of rats,
第38回日本神経科学大会, Jul. 2015. 姚 陳娟, 赤松 徹也, 長谷川 敬展, 吉村 弘 :
唾液腺再生モデルにおける水チャネルAQP5の発現,
第56回歯科基礎医学会, 2014年9月.- (キーワード)
- 唾液腺 (salivary gland) / 再生 (regeneration) / 水チャネル (water channel) / AQP5
ユビキチンリガーゼによるAQP5のユビキチン化亢進とダウンレギュレーション,
第56回歯科基礎医学会, 2014年9月.- (キーワード)
- 水チャネル (water channel) / ユビキチン化 / ダウンレギュレーション / AQP5
唾液腺再生モデルにおけるサチライシン様前駆体蛋白質変換酵素の発現誘導,
第56回歯科基礎医学会(福岡国際会議場/福岡県), 2014年9月.- (キーワード)
- 唾液腺 (salivary gland) / 再生 (regeneration) / 前駆体蛋白質変換酵素
唾液腺再生におけるサチライシン様前駆体蛋白質変換酵素PACE4の関与,
第55回歯科基礎医学会(2013年9月19日-21日), 2013年9月. 長谷川 敬展, 姚 陳娟, 赤松 徹也, 吉村 弘 :
ヒト唾液腺HSG細胞における構成的なAQP5の取り込み,
第55回歯科基礎医学会[2013年9月19日(金)-21日(日)], 2013年9月. 赤松 徹也, 姚 陳娟, 長谷川 敬展, 吉村 弘 :
唾液腺再生におけるサチライシン様前駆体蛋白質変換酵素PACE4の関与,
Journal of Oral Biosciences, Vol.55, No.Suppl., 199, 2013年9月. 赤松 徹也, 姚 陳娟, 長谷川 敬展, 吉村 弘 :
唾液腺再生におけるサチライシン様前駆体蛋白質変換酵素PACE4の関与,
第55回歯科基礎医学会[2013年9月19日(金)-21日(日)], 2013年9月. 吉村 弘, 須貝 外喜夫, 姚 陳娟, 赤松 徹也, 長谷川 敬展, 加藤 伸郎 :
ラット大脳皮質におけるnon-NMDA受容体活動に依存する20Hzオシレーション,
第36回日本神経科学大会[2013年6月20日(木)-23日(日)], 2013年6月. 長谷川 敬展, 姚 陳娟, 赤松 徹也, 吉村 弘 :
ヒト唾液腺HSG細胞における構成的なAQP5の取り込み,
Journal of Oral Biosciences, Vol.55, No.Suppl., 199, 2013年. 長谷川 敬展, 姚 陳娟, 赤松 徹也, 細井 和雄 :
唾液腺細胞におけるアクアポリン5の翻訳後修飾,
第53回歯科基礎医学会学術大会 サテライトシンポジウムSS11, 2011年9月. 長谷川 敬展, 姚 陳娟, 赤松 徹也, 細井 和雄 :
唾液腺細胞におけるアクアポリン5の翻訳後修飾, --- 第53回歯科基礎医学会学術大会(2011年9月30日-10月2日)サテライトシンポジウムSS11 ---,
Journal of Oral Biosciences, Vol.53, No.Supplement, 104, 2011年9月. Purevjav Javkhlan, Yuka Hiroshima, Ahmad Azlina, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Toshihiko Nagata and Kazuo Hosoi :
Calprotectin expression in the mouse salivary gland: Induction by lipopolysaccharide,
第52回歯科基礎医学会(2010年9月20-22日), Sep. 2010. 廣島 佑香, Purevjav Javkhlan, Ahmad Azlina, 長谷川 敬展, 赤松 徹也, 細井 和雄 :
Porphyromonas gingivalis由来LPSはヒト好中球からのレジスチンの遊離を促進する,
第52回歯科基礎医学会(2010年9月20-22日), 2010年9月. 長谷川 敬展, Ahmad Azlina, Purevjav Javkhlan, 廣島 佑香, 姚 陳娟, 赤松 徹也, 細井 和雄 :
唾液腺細胞におけるアクアポリン5リン酸化のシグナル伝達機構,
第52回歯科基礎医学会(2010年9月20-22日), 2010年9月. Purevjav Javkhlan, Yuka Hiroshima, Ahmad Azlina, Takahiro Hasegawa, Chenjuan Yao, Tetsuya Akamatsu, Toshihiko Nagata and Kazuo Hosoi :
Calprotectin expression in the mouse salivary gland: Induction by lipopolysaccharide,
Journal of Oral Biosciences, Vol.52, No.supplement, 94, Sep. 2010. 廣島 佑香, フルジャフ ジャフラン, Ahmad Azlina, 長谷川 敬展, 赤松 徹也, 細井 和雄 :
Porphyromonas gingivalis由来LPSはヒト好中球からのレジスチンの遊離を促進する,
Journal of Oral Biosciences, Vol.52, No.supplement, 148, 2010年9月. 長谷川 敬展, Ahmad Azlina, フルジャフ ジャフラン, 廣島 佑香, 姚 陳娟, 赤松 徹也, 細井 和雄 :
唾液腺細胞におけるアクアポリン5リン酸化のシグナル伝達機構,
Journal of Oral Biosciences, Vol.52, No.supplement, 164, 2010年9月. 姚 陳娟, Ahmad Azlina, フルジャフ ジャフラン, 長谷川 敬展, 赤松 徹也, 細井 和雄 :
NF-κB/AP-1の複合体を介した耳下腺AQP5のLPSによるdown-regulation,
第51回歯科基礎医学会, 2009年9月. 赤松 徹也, Ahmad Azlina, フルジャフ ジャフラン, 長谷川 敬展, 姚 陳娟, 細井 和雄 :
唾液腺の発生と細胞分化,
第51回歯科基礎医学会, 2009年9月. 長谷川 敬展, Ahmad Azlina, フルジャフ ジャフラン, 姚 陳娟, 赤松 徹也, 細井 和雄 :
アクアポリン5のユビキチン化とその細胞内膜輸送系における役割,
第51回歯科基礎医学会, 2009年9月. フルジャフ ジャフラン, 廣島 佑香, Ahmad Azlina, 長谷川 敬展, 姚 陳娟, 赤松 徹也, 永田 俊彦, 細井 和雄 :
マウス唾液腺でのリポ多糖によるカルプロテクチン誘導,
第51回歯科基礎医学会, 2009年9月. Ahmad Azlina, フルジャフ ジャフラン, 長谷川 敬展, 姚 陳娟, 赤松 徹也, 細井 和雄 :
ラット顎下腺での副交感神経切除に続くオートファジーを介したAQP5分解,
第51回歯科基礎医学会, 2009年9月. カラバシル ミレーバ, 長谷川 敬展, アズリナ アハマド, プルワンティ ヌヌク, 姚 陳娟, 赤松 徹也, 細井 和雄 :
SDラットで見られるAQP5 G103D変異は正常な水透過性を示すが,膜へのトラフィッキングが低下した,
第50回歯科基礎医学会, 2008年9月. 姚 陳娟, アズリナ アハマド, プルワンティ ヌヌク, カラバシル ミレーバ, 長谷川 敬展, 赤松 徹也, 細井 和雄 :
唾液腺AQP5のLPSによるdown-regulationの機構,
第50回歯科基礎医学会, 2008年9月. アズリナ アハマド, プルワンティ ヌヌク, カラバシル ミレーバ, 姚 陳娟, 長谷川 敬展, 赤松 徹也, 細井 和雄 :
副交感神経切除による顎下腺AQP5のダウンレギュレーション,
第50回歯科基礎医学会, 2008年9月. プルワンティ ヌヌク, アズリナ アハマド, カラバシル ミレーバ, 姚 陳娟, 長谷川 敬展, 赤松 徹也, 細井 和雄 :
導管結紮マウス顎下腺における導管細胞の増殖へのIL-6-STAT3-Sca-1系の関与,
第50回歯科基礎医学会, 2008年9月. 姚 陳娟, アズリナ アハマド, プルワンティ ヌヌク, カラバシル ミレーバ, 長谷川 敬展, 赤松 徹也, 細井 和雄 :
LPSによる耳下腺AQP5の発現制御とそのシグナル伝達経路,
第59回日本生理学会中国四国地方会, 2007年11月. 赤松 徹也, アズリナ アハマド, プルワンティ ヌヌク, カラバシル ミレーバ, 長谷川 敬展, 姚 陳娟, 細井 和雄 :
唾液腺腺房細胞の発生・分化・成熟化と水チャネルAQP5発現,
第59回日本生理学会中国四国地方会, 2007年11月. プルワンティ ヌヌク, 辻 大輔, アズリナ アハマド, カラバシル ミレーバ, 姚 陳娟, 長谷川 敬展, 赤松 徹也, 伊藤 孝司, 細井 和雄 :
導管結紮によるマウス顎下腺での一過性のIL-6の増加が幹細胞マーカーSca-1の持続的な上昇を引き起す,
第49回歯科基礎医学会学術大会, 2007年8月. カラバシル ミレーバ, 長谷川 敬展, アズリナ アハマド, プルワンティ ヌヌク, 姚 陳娟, 赤松 徹也, 細井 和雄 :
MDCK II細胞で発現させたラット変異AQP5の機能解析,
第49回歯科基礎医学会, 2007年8月. アズリナ アハマド, カラバシル ミレーバ, プルワンティ ヌヌク, 姚 陳娟, 長谷川 敬展, 赤松 徹也, 細井 和雄 :
リソゾーム系による顎下腺AQP5蛋白質発現の調節,
第49回歯科基礎医学会, 2007年8月. 姚 陳娟, アズリナ アハマド, プルワンティ ヌヌク, カラバシル ミレーバ, 長谷川 敬展, 赤松 徹也, 細井 和雄 :
唾液腺AQP5およびAQP1発現のLPSによるdown-regulation,
第49回歯科基礎医学会, 2007年8月. 赤松 徹也, アズリナ アハマド, プルワンティ ヌヌク, カラバシル ミレーバ, 長谷川 敬展, 姚 陳娟, 細井 和雄 :
唾液腺腺房細胞の分化とAQP5発現,
第49回歯科基礎医学会, 2007年8月. カラバシル ミレーバ, 長谷川 敬展, プルワンティ ヌヌク, 李 雪飛, 姚 陳娟, 赤松 徹也, 金森 憲雄, 細井 和雄 :
in vitroシステムで発現したラット変異AQP5の機能解析と異常唾液分泌への影響,
第48回歯科基礎医学会, 2006年9月.
- 研究会・報告書
- 姚 陳娟, 長谷川 敬展, 赤松 徹也, 吉村 弘 :
マウス耳下腺における水チャネルAQP5のイソプロテレノールによるdouwn-regulationの機構,
Journal of Oral Biosciences, Vol.54, No.Suppl., 153, 姚 陳娟, 佐藤 匠, 長谷川 敬展, 赤松 徹也, 吉村 弘 :
イソプロパノール反復投与によるマウス唾液腺機能に及ぼす影響,
第34回唾液腺談話会, 2022年9月.- (キーワード)
- イソプロパノール / 水チャネル (water channel)
唾液腺再生モデルにおけるサチライシン様前駆体蛋白質変換酵素PACE4の発現誘導-Part II-,
Journal of Oral Biosciences, Vol.Suppl., 415, 2016年8月. 赤松 徹也, 姚 陳娟, 長谷川 敬展, 吉村 弘 :
唾液腺再生過程で見られる雌雄差について,
Journal of Oral Biosciences, Vol.Suppl., 451, 2016年8月. 赤松 徹也, 姚 陳娟, 長谷川 敬展, 吉村 弘 :
唾液腺再生への subtilisin-like proprotein convertase PACE4の関与,
自然科学研究機構生理学研究所研究会「唾液腺形態形成研究会~機能解析から器官再生へ~」, 2014年8月.- (キーワード)
- 唾液腺 (salivary gland) / 再生 (regeneration) / 前駆体蛋白質変換酵素
マウス耳下腺における水チャネルAQP5のイソプロテレノールによるdouwn-regulationの機構,
第54回歯科基礎医学会, 2012年9月. 吉村 弘, 長谷川 敬展, 姚 陳娟, 赤松 徹也 :
細胞内cAMP上昇が大脳皮質味覚野から口腔体性感覚野への信号伝播速度に与える影響,
第54回歯科基礎医学会, 2012年9月. 姚 陳娟, 長谷川 敬展, 赤松 徹也, 吉村 弘 :
マウス耳下腺における水チャネルAQP5のイソプロテレノールによるdouwn-regulationの機構,
Journal of Oral Biosciences, Vol.54, No.Suppl., 153, 2012年9月. 吉村 弘, 長谷川 敬展, 姚 陳娟, 赤松 徹也 :
細胞内cAMP上昇が大脳皮質味覚野から口腔体性感覚野への信号伝播速度に与える影響,
Journal of Oral Biosciences, Vol.54, No.Suppl., 131, 2012年9月.
- 特許
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- 作品
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- 補助金・競争的資金
- 唾液分泌を司る水チャネル翻訳後修飾の分子調節機構 (研究課題/領域番号: 25462891 )
唾液腺水チャネル・アクアポリン5の翻訳後修飾調節とその生理的役割 (研究課題/領域番号: 23792124 )
口腔乾燥症の克服に向けた唾液腺腺房細胞の分化・成熟と機能発現の分子機構の解明 (研究課題/領域番号: 23592737 )
病態時における外分泌腺型水チャネル、AQP5の発現と機能調節の分子機構 (研究課題/領域番号: 23592736 )
翻訳後修飾による水チャネルアクアポリン5の細胞内局在・輸送制御 (研究課題/領域番号: 21791806 )
水チャネルアクアポリン2の細胞内輸送調節〜比較生物学からのアプローチ〜 (研究課題/領域番号: 19770054 )
外分泌腺における水チャネル、特にアクアポリン5の発現と機能調節の分子機構 (研究課題/領域番号: 18390493 )
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2024年11月13日更新
- 専門分野・研究分野
- 分子細胞生物学 (Molecular and Cellular Biology)
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- 受賞
- 2017年3月, 徳島大学歯学部ベストメンター賞 (歯学部)
2023年4月, 令和4年度「教養教育賞」 (徳島大学) - 活動
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2024年11月10日更新
2024年11月9日更新
Jグローバル
- Jグローバル最終確認日
- 2024/11/9 01:27
- 氏名(漢字)
- 長谷川 敬展
- 氏名(フリガナ)
- ハセガワ タカヒロ
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- Hasegawa Takahiro
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- 徳島大学 講師
リサーチマップ
- researchmap最終確認日
- 2024/11/10 01:50
- 氏名(漢字)
- 長谷川 敬展
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- Hasegawa Takahiro
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2024年11月9日更新
- 研究者番号
- 50447273
- 所属(現在)
- 2024/4/1 : 徳島大学, 大学院医歯薬学研究部(歯学域), 講師
- 所属(過去の研究課題
情報に基づく)*注記 - 2015/4/1 : 徳島大学, 大学院医歯薬学研究部, 助教
2011/4/1 – 2014/4/1 : 徳島大学, ヘルスバイオサイエンス研究部, 助教
2013/4/1 : 徳島大学, 大学院ヘルスバイオサイエンス 研究部(歯学系), 助教
2007/4/1 – 2012/4/1 : 徳島大学, 大学院・ヘルスバイオサイエンス研究部, 助教
- 審査区分/研究分野
-
研究代表者
生物系 / 生物学 / 基礎生物学 / 動物生理・行動
生物系 / 医歯薬学 / 歯学 / 機能系基礎歯科学研究代表者以外
生物系 / 医歯薬学 / 歯学 / 機能系基礎歯科学
- キーワード
-
研究代表者
アクアポリン2 / 腎臓集合管 / 小胞輸送 / プルダウンアッセイ / 結合タンパク質 / リン酸化 / アクアポリン / 翻訳後修飾 / ユビキチン化 / 細胞内膜輸送 / 唾液腺 / アクアポリン5 / アクアポリン5(AQP5) / 細胞内輸送 / 口腔生理学 / 細胞内シグナル伝達
研究代表者以外
アクアポリン / 唾液腺 / カテプシン / 副交感神経 / 塩酸セビメリン / MDCK細胞 / トラフィッキング / GFP-AQP5キメラ分子 / アクアポリン5 / LPS / 遺伝子変異 / 鼓索神経切除 / 顎下腺 / 腺房細胞 / 発生・分化・再生 / サチライシン様前駆体蛋白質変換酵素 / PACE4 / 水チャネル / AQP5 / bHLH型転写因子 / HSG細胞
研究課題
研究成果
共同研究者
注目研究はありません。