Department of Biology, Science Faculty, Selçuk University, Konya, Turkey.
Curr Pharm Biotechnol. 2010 Feb;11(2):216-22. doi: 10.2174/138920110790909632.
Heat shock proteins (Hsps) protect protein substrates against conformational damage to promote the function of the proteins, prevent aggregation and prevent formation of toxic inclusion bodies. Protein aggregates and fibrils have been associated with neurodegenerative diseases and with inclusion bodies. High-level expression of recombinant protein for biotechnological purposes often leads to insoluble inclusion bodies. Therefore, misfolded proteins must be properly folded or must be degraded through heat shock protein action. This function protects cells against cytotoxic outcomes. In addition to their cytoprotective roles, Hsps are involved in other functions since Hsps exist in all types of cells and tissues. Therefore, several diseases are associated with alterations of these biochemical functions. This first review of the theme issue will discuss general properties of Hsps concisely along with their potential use in pharmaceutical and biotechnological applications.
热休克蛋白（Hsps）可保护蛋白质底物免受构象损伤，从而促进蛋白质的功能，防止聚集并防止形成有毒包涵体。蛋白质聚集体和纤维已与神经退行性疾病和包涵体有关。出于生物技术目的的重组蛋白的高水平表达通常会导致不溶性包涵体。因此，错误折叠的蛋白质必须正确折叠，或者必须通过热休克蛋白作用降解。该功能可保护细胞免受细胞毒性作用。除了具有细胞保护作用外，Hsps 还参与其他功能，因为 Hsps 存在于所有类型的细胞和组织中。因此，一些疾病与这些生化功能的改变有关。本主题问题的首次综述将简要讨论 Hsps 的一般特性及其在药物和生物技术应用中的潜在用途。
