論文

査読有り
2011年9月

Novel phosphorylation of aquaporin-5 at its threonine 259 through cAMP signaling in salivary gland cells

AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY
  • Takahiro Hasegawa
  • ,
  • Ahmad Azlina
  • ,
  • Purevjav Javkhlan
  • ,
  • Chenjuan Yao
  • ,
  • Tetsuya Akamatsu
  • ,
  • Kazuo Hosoi

301
3
開始ページ
C667
終了ページ
C678
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1152/ajpcell.00058.2011
出版者・発行元
AMER PHYSIOLOGICAL SOC

Hasegawa T, Azlina A, Javkhlan P, Yao C, Akamatsu T, Hosoi K. Novel phosphorylation of aquaporin-5 at its threonine 259 through cAMP signaling in salivary gland cells. Am J Physiol Cell Physiol 301: C667-C678, 2011. First published June 1, 2011; doi: 10.1152/ajpcell.00058.2011.-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 Ca2+, signaling pathways, and that this phosphorylation does not contribute to AQP5 trafficking in the salivary gland cells.

Web of Science ® 被引用回数 : 16

リンク情報
DOI
https://doi.org/10.1152/ajpcell.00058.2011
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/21633078
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000294339400016&DestApp=WOS_CPL

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