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肾上腺嗜铬旁细胞收缩蛋白与刺激-分泌偶联

Adrenal paraneurone contractile proteins and stimulus-secretion coupling.

作者信息

Trifaró J M, Kenigsberg R L, Côté A, Lee R W, Hikita T

出版信息

Can J Physiol Pharmacol. 1984 Apr;62(4):493-501. doi: 10.1139/y84-079.

Abstract

Actin, myosin, and alpha-actinin have been isolated from adrenal chromaffin cells and characterized. Their physicochemical properties have been studied and their cell localization revealed by biochemical, immunocytochemical, and ultrastructural techniques. Alpha-actinin is a component of chromaffin granule membranes and some of the cell actin copurifies with these secretory granules. Myosin is not detected in the granules but is present mainly in the cytosol. Trifluoperazine, a calmodulin antagonist, blocks stimulation-induced hormone release from chromaffin cells at a step distal from Ca2+ entry. High affinity calmodulin binding sites have also been found in chromaffin granule membranes. Furthermore, microinjection of calmodulin antibodies into chromaffin cells blocks hormone output in response to stimulation. In view of the above findings, the possible roles of contractile proteins and calmodulin in chromaffin cell functions is discussed.

摘要

肌动蛋白、肌球蛋白和α-辅肌动蛋白已从肾上腺嗜铬细胞中分离出来并进行了表征。通过生化、免疫细胞化学和超微结构技术研究了它们的物理化学性质,并揭示了它们在细胞中的定位。α-辅肌动蛋白是嗜铬颗粒膜的一个组成部分,一些细胞肌动蛋白与这些分泌颗粒共同纯化。在颗粒中未检测到肌球蛋白,其主要存在于细胞质中。三氟拉嗪是一种钙调蛋白拮抗剂,在远离Ca2+进入的步骤中阻断刺激诱导的嗜铬细胞激素释放。在嗜铬颗粒膜中也发现了高亲和力的钙调蛋白结合位点。此外,将钙调蛋白抗体显微注射到嗜铬细胞中可阻断刺激后的激素分泌。鉴于上述发现,讨论了收缩蛋白和钙调蛋白在嗜铬细胞功能中的可能作用。

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