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首页> 外文期刊>Life sciences >Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model?
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Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model?

机译：热激蛋白47与胶原蛋白的相互作用和应激反应：非常规的伴侣模型？

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摘要

Heat shock proteins (HSPs) are upregulated and manifested upon cellular stress and possess chaperoning functions. HSP47 is an endoplasmic reticulum (ER)-resident, collagen-specific chaperone and plays a key role in collagen biosynthesis and its structural assembly. The collagen scaffold is a primary structural target of recent interest due to its applications in tissue engineering and drug delivery and in treatment of clinical disorders. This review highlights the fundamental aspects of HSPs in protein folding and quality control, in the elicitation of a stress response in connective tissue and in the characterization of HSP47 in collagen folding and assembly. The significant features of HSP47 which are distinct in its cellular capabilities are discussed. We propose that targeting the stress response is a key factor in identifying connective tissue biomarkers. We also address the issues and strategies involved in the stress response of connective tissue diseases. In conclusion, we describe the prospects of collagen biochemistry in correlation to the science of HSPs.
机译：热休克蛋白（HSPs）在细胞应激时被上调并表现出来，并具有伴侣功能。 HSP47是内质网（ER）驻留的胶原蛋白特异性伴侣分子，在胶原蛋白生物合成及其结构组装中起关键作用。胶原蛋白支架由于其在组织工程和药物递送以及在临床疾病的治疗中的应用而成为近期关注的主要结构靶标。这篇综述着重介绍了HSPs在蛋白质折叠和质量控制中的基本方面，在结缔组织中引起应激反应以及在胶原蛋白折叠和组装中HSP47的表征。讨论了HSP47在细胞功能上不同的重要特征。我们建议针对应激反应是确定结缔组织生物标志物的关键因素。我们还将解决结缔组织疾病应激反应中涉及的问题和策略。总之，我们描述了与HSPs科学相关的胶原蛋白生物化学的前景。

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