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一组新的小热休克蛋白与小鼠PC12细胞线粒体相关并保护NADH:泛醌氧化还原酶免受热和氧化应激影响的证据。

Evidence for a novel set of small heat-shock proteins that associates with the mitochondria of murine PC12 cells and protects NADH:ubiquinone oxidoreductase from heat and oxidative stress.

作者信息

Downs C A, Jones L R, Heckathorn S A

机构信息

Department of Biology, Department of Physics, University of Charleston, 58 Coming Street, Charleston, South Carolina, 29424, USA.

出版信息

Arch Biochem Biophys. 1999 May 15;365(2):344-50. doi: 10.1006/abbi.1999.1177.

DOI:10.1006/abbi.1999.1177
PMID:10328830
Abstract

Several previously unreported small heat-shock proteins (sHsps) were detected in mitochondria from heat-stressed rat PC12 cells, but not in unstressed controls. Functional inactivation of the mitochondrial sHsps with murine Hsp25 antibody indicated that these sHsps protect NADH:ubiquinone oxidoreductase and NADH dehydrogenase activity (i.e., complex I) in submitochondrial vesicles during heat and oxidative stress. These results (i) confirm the existence of multiple sHsps in mammals and indicate that several of these sHsps associate with the mitochondria, (ii) indicate a conserved function between plant and mammalian mitochondrial sHsps in protecting electron transport during stress, and (iii) suggest that these sHsps may play an important role in diseases whose etiology is based upon oxidative damage of complex I.

摘要

在热应激大鼠PC12细胞的线粒体中检测到几种先前未报道的小分子热休克蛋白(sHsps),但在未受应激的对照细胞中未检测到。用鼠源Hsp25抗体使线粒体sHsps功能失活表明,这些sHsps在热应激和氧化应激期间保护亚线粒体小泡中的NADH:泛醌氧化还原酶和NADH脱氢酶活性(即复合体I)。这些结果(i)证实了哺乳动物中存在多种sHsps,并表明其中几种sHsps与线粒体相关,(ii)表明植物和哺乳动物线粒体sHsps在应激期间保护电子传递方面具有保守功能,(iii)表明这些sHsps可能在病因基于复合体I氧化损伤的疾病中起重要作用。

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