类二十烷和细胞因子诱导人多形核粒细胞热休克蛋白的启动机制和诱导。

Eicosanoids Pub Date : 1992-01-01
W König, M Köller, J Brom
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引用次数: 0

摘要

用细胞因子(IL-3、IL-6、tnf - α)引发人多态核粒细胞(PMNs),然后再进行刺激(FMLP),导致肌动蛋白和gtpase活性的聚合增强,这与ras免疫反应性的丧失和Rab蛋白的表达增加有关。此外,代谢放射性标记和Western blotting(抗热休克蛋白72)证实,tnf - α和12-HETE在PMNs中诱导热休克蛋白(hsp 70家族)。这种应激反应的激活对随后细菌溶细胞素(杀白细胞素)的裂解攻击发挥了保护作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Priming mechanisms and induction of heat shock proteins in human polymorphonuclear granulocytes induced by eicosanoids and cytokines.

Priming of human polymorphonuclear granulocytes (PMNs) with cytokines (IL-3, IL-6, TNF-alpha) followed by a subsequent stimulation (FMLP) led to an enhanced polymerization of actin and GTPase-activity which correlated to a loss of ras immunoreactivity and an increased expression of Rab proteins. Furthermore TNF-alpha and 12-HETE induced the heat shock proteins (hsp 70 family) in PMNs as was demonstrated by metabolic radiolabeling and Western blotting (anti-hsp 72). This activation of the stress response exerted a protective function towards a subsequent lytic attack by a bacterial cytolysin (leukocidin).

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