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肾上腺嗜铬细胞Ca(2+)触发分泌过程中丝切蛋白的激活

Cofilin activation during Ca(2+)-triggered secretion from adrenal chromaffin cells.

作者信息

Birkenfeld J, Kartmann B, Betz H, Roth D

机构信息

Department of Neurochemistry, Max-Planck-Institute for Brain Research, Deutschordenstrasse 46, Frankfurt, 60528, Germany.

出版信息

Biochem Biophys Res Commun. 2001 Aug 24;286(3):493-8. doi: 10.1006/bbrc.2001.5435.

Abstract

Cofilin is one of the major actin depolymerizing proteins in eukaryotic cells and involved in many membrane modulating activities, such as cell growth and motility. Here we examined whether cofilin is activated upon Ca(2+) regulated noradrenalin secretion from bovine adrenal chromaffin cells. We found that triggering exocytosis by nicotine causes a dephosphorylation and thereby activation of cofilin. Furthermore, in permeabilized chromaffin cells the addition of Ca(2+) alone is sufficient to trigger both, regulated exocytosis and cofilin activation. This is consistent with cofilin activation being required for actin reorganization during exocytosis.

摘要

丝切蛋白是真核细胞中主要的肌动蛋白解聚蛋白之一,参与许多膜调节活动,如细胞生长和运动。在这里,我们研究了丝切蛋白是否在牛肾上腺嗜铬细胞受Ca(2+)调节的去甲肾上腺素分泌过程中被激活。我们发现,尼古丁触发胞吐作用会导致丝切蛋白去磷酸化,从而激活丝切蛋白。此外,在透化的嗜铬细胞中,单独添加Ca(2+)足以触发调节性胞吐作用和丝切蛋白激活。这与胞吐作用期间肌动蛋白重组需要丝切蛋白激活是一致的。

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