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从小鼠巨噬细胞样细胞系中分离和鉴定钙调蛋白。

Isolation and characterization of calmodulin from a murine macrophage-like cell line.

作者信息

Jamieson G A, Vanaman T C

出版信息

J Immunol. 1980 Sep;125(3):1171-7.

PMID:7410833
Abstract

Several lines of evidence implicate fluxes in the intracellular levels of CA++ and the cyclic nucleotiodes in the chemotactic, phagocytic, and cytotoxic responses of macrophages. Calmodulin, a ubiquitous small acidic Ca-binding protein, appears to link the intracellular second messengers--Ca++ and the cyclic nucleotides--through its ability to regulate numerous central metabolic enzymatic activities. A pure protein has been isolated and characterized from the macrophage-like cell line, P388D. This protein has been identified as calmodulin by demonstrating three of the Ca-dependent activities attributed to calmodulins. P388D calmodulin also has physiochemical properties similar to those of the previously characterized mammalian proteins. This study is the initial step of an examination of the role of this central regulatory protein in responses elicited by macrophages to external stimuli.

摘要

有几条证据表明,巨噬细胞的趋化、吞噬和细胞毒性反应与细胞内钙离子(Ca++)水平及环核苷酸的通量有关。钙调蛋白是一种普遍存在的小酸性钙结合蛋白,它似乎通过调节众多核心代谢酶活性的能力,将细胞内第二信使——钙离子和环核苷酸联系起来。已从巨噬细胞样细胞系P388D中分离并鉴定出一种纯蛋白。通过证明钙调蛋白的三种钙依赖性活性,该蛋白已被鉴定为钙调蛋白。P388D钙调蛋白还具有与先前鉴定的哺乳动物蛋白相似的理化性质。本研究是考察这种核心调节蛋白在巨噬细胞对外界刺激引发的反应中所起作用的第一步。

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