Walsh D, Grantham J, Zhu X O, Wei Lin J, van Oosterum M, Taylor R, Edwards M
School of Anatomy, Department of Medicine, The University of New South Wales, Sydney, Australia.
Environ Med. 1999 Dec;43(2):79-87.
Heat shock proteins (HSPs) have been identified in all cells, prokaryotic and eukaryotic, to protect the cells from harmful insults and stress. Increased HSP synthesis can also result during normal cellular functions and also respond to exposure from environmental stress and infection. Although the molecular mechanisms responsible for HSP cellular protection are still not fully understood, their expression is critical for cellular survival and can be modified by cell signal transducers such as intracellular pH, cyclic AMP, Ca2+ Na+, inositol [correction of inostitol] triphosphate, protein kinase C, and protein phosphates. Most HSPs interact, assemble, fold, unfold, bind, transport, translocate and 'chaperone' other proteins in the cell and alter their function.
热休克蛋白（HSPs）已在所有细胞（包括原核细胞和真核细胞）中被鉴定出来，其作用是保护细胞免受有害损伤和应激。在正常细胞功能过程中也会出现热休克蛋白合成增加的情况，并且它还会对环境应激和感染作出反应。尽管热休克蛋白对细胞保护作用的分子机制仍未完全明确，但其表达对于细胞存活至关重要，并且可以被细胞信号转导分子所调节，如细胞内pH值、环磷酸腺苷、钙离子、钠离子、肌醇三磷酸、蛋白激酶C和蛋白磷酸酶。大多数热休克蛋白在细胞内与其他蛋白质相互作用、组装、折叠、展开、结合、运输、易位并“陪伴”它们，从而改变其功能。
