Involvement of aquaporin-5 water channel in osmoregulation in parotid secretory granules
Involvement of aquaporin-5 water channel in osmoregulation in parotid secretory granules
复制标题
DOI:
10.1007/s00232-005-0736-9
复制
发表时间:
2005-02-01
影响因子:
2.4
通讯作者:
Sugiya, H
中科院分区:
文献类型:
--
作者:
Matsuki, N;Hashimoto, S;Sugiya, H
Aquaporins (AQPs) are a family of channel proteins that allow water or very small Solutes to pass, functioning in tissues where the rapid and regulated transport of fluid is necessary, Such as the kidney, lung. and salivary glands. Aquaporin-5 (AQP5) has been demonstrated to localize on the luminal Surface of the acinar cells of the salivary glands. In this paper, we investigated the expression and function of AQP5 in the secretory granules of the rat parotid gland. AQP5 was detected in the secretory uranule Membranes by immunoblot analysis. The ummunoelectron microscopy experiments confirmed that AQP5 was to be found in the secretory granule membrane. Anti-AQP5 antibody evoked lysis of the secretory granules but anti-aquaporin-1 antibody did not and AQP1 was not detected in the secretory granule membranes by immunoblot analysis. When chloride ions were removed from the solution prepared for suspending secretory (granules, the granule lysis induced by anti-AQP5 antibody was inhibited. Furthermore, 4,4'-dii'sothiocyanatostilbene-2,2'-di-sulfonic acid, an anion channel blocker, blocked the anti-AQP5 antibody-induced secretory granule lysis. These results suggest that AQP5 is, expressed in the parotid gland secretory granule membrane and is involved in osmoregulation in the secretory granules.