Heat shock protein 70 (Hsp70): Membrane location, export and immunological relevance

Heat shock protein 70 (Hsp70): Membrane location, export and immunological relevance
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DOI:
10.1016/j.ymeth.2007.06.006
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发表时间:
2007-11-01
期刊:
影响因子:
4.8
通讯作者:
Multhoff, Gabriele
Multhoff, Gabriele
中科院分区:
生物学3区
文献类型:
--
作者:
Multhoff, Gabriele

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应激或热休克蛋白(HSPs)在所有生物体中都是非常保守的。它们的表达是对各种生理和环境损害的反应。在细胞质中,这些蛋白作为分子伴侣起着至关重要的作用,通过协助新生和应力积累的错误折叠蛋白的正确折叠,防止蛋白质聚集,蛋白质运输,并支持抗原加工和递呈。应激后,位于细胞内的热休克蛋白发挥保护功能,从而防止致死性损伤。相反,膜结合或细胞外定位的热休克蛋白作为危险信号,引发由适应性或先天免疫系统介导的免疫反应。在这里,热休克蛋白作为免疫原性肽的载体,诱导细胞因子释放或为自然杀伤(NK)细胞提供识别位点。本文将讨论膜结合热休克蛋白和细胞外热休克蛋白的检测方法以及测定其免疫功能的方法。(C) 2007年Elsevier Inc.出版
Stress or heat shock proteins (HSPs) are remarkably conserved in all living organisms. Their expression is induced in response to a variety of physiological and environmental insults. In the cytosol these proteins play an essential role as molecular chaperones by assisting the correct folding of nascent and stress-accumulated misfolded proteins, preventing protein aggregation, transport of proteins, and supporting antigen processing and presentation. Following stress, intracellularly located HSPs fulfill protective functions and thus prevent lethal damage. In contrast, membrane-bound or extracellularly located HSPs act as danger signals and elicit immune responses mediated either by the adaptive or innate immune system. Here, HSPs act as carriers for immunogenic peptides, induce cytokine release or provide recognition sites for natural killer (NK) cells. This article will discuss methods for the detection of membrane-bound and extracellular HSPs and methods for determining their immunological functions. (C) 2007 Published by Elsevier Inc.