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膜联蛋白I通过大鼠胰岛表面结合位点对胰岛素分泌的影响。

Effect of annexin I on insulin secretion through surface binding sites in rat pancreatic islets.

作者信息

Hong Shin-Hee, Won Jong Hak, Yoo Seung-Ah, Auh Chung-Kyoon, Park Young Min

机构信息

Department of Biological Sciences, SungKyunKwan University, Suwon 440-746, South Korea.

出版信息

FEBS Lett. 2002 Dec 4;532(1-2):17-20. doi: 10.1016/s0014-5793(02)03613-x.

DOI:10.1016/s0014-5793(02)03613-x
PMID:12459455
Abstract

This study investigates the effect of extracellular annexin I (Anx I) on regulating insulin secretion in isolated rat pancreatic islets. Results show that Anx I stimulates insulin release in pancreatic islets regardless of the presence or absence of extracellular Ca2+. In particular, confocal microscopy shows that Anx I binds to the surface of islet cells in the absence of extracellular Ca2+. However, insulin secretion through Anx I significantly decreases in trypsin-treated islets. Likewise, there is minimal binding of Anx I to the surface of trypsin-treated islets. Anti-Anx I polyclonal antibody also inhibits the stimulating effect of Anx I on insulin secretion. These results indicate that Anx I is capable of binding to the cell surface receptor, in order to regulate the stimulation of insulin release in rat pancreatic islets.

摘要

本研究调查了细胞外膜联蛋白I(Anx I)对分离的大鼠胰岛中胰岛素分泌调节的影响。结果表明,无论细胞外Ca2+是否存在,Anx I均可刺激胰岛中的胰岛素释放。特别是,共聚焦显微镜显示在细胞外Ca2+不存在的情况下,Anx I可结合到胰岛细胞表面。然而,在胰蛋白酶处理的胰岛中,通过Anx I介导的胰岛素分泌显著减少。同样,Anx I与胰蛋白酶处理的胰岛表面的结合也极少。抗Anx I多克隆抗体也抑制Anx I对胰岛素分泌的刺激作用。这些结果表明,Anx I能够结合到细胞表面受体,从而调节大鼠胰岛中胰岛素释放的刺激过程。

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