Mirkes P E
Department of Pediatrics, University of Washington, Seattle 98195, USA.
Mutat Res. 1997 Dec 12;396(1-2):163-73. doi: 10.1016/s0027-5107(97)00182-6.
Available data indicate that heat shock proteins act as chaperones under non-stress conditions by assisting in: (1) the folding of newly synthesized proteins, (2) the intracellular translocation of proteins, and (3) the function of other proteins. As we gain additional information concerning cellular physiology, we may find that heat shock proteins play a key role in many additional cellular functions. When cells experience thermal or chemical stress, heat shock proteins take on a new role, conserved from bacteria to humans, of protecting cells from the detrimental effects of stress. This latter role takes on added significance for the embryo in which the developmental program must be read linearly, with little opportunity to cycle backward to complete a missed segment of the program. Although circumstantial evidence clearly implicates heat shock proteins in protecting embryos from thermal stress, definitive evidence is still lacking. The challenge for the future is to obtain such definitive data. Ideally, such information will lead to new therapeutic paradigms that will afford protection to the human embryo/fetus exposed to thermal/chemical stress.
现有数据表明，热休克蛋白在非应激条件下作为伴侣蛋白发挥作用，具体方式包括：（1）协助新合成蛋白质的折叠；（2）蛋白质的细胞内转运；（3）其他蛋白质的功能发挥。随着我们获取更多有关细胞生理学的信息，我们可能会发现热休克蛋白在许多其他细胞功能中发挥关键作用。当细胞受到热应激或化学应激时，热休克蛋白会发挥一种从细菌到人类都保守的新作用，即保护细胞免受应激的有害影响。后一种作用对胚胎具有额外的重要性，因为胚胎的发育程序必须线性读取，几乎没有机会回溯以完成程序中遗漏的部分。尽管间接证据明确表明热休克蛋白在保护胚胎免受热应激方面发挥作用，但确凿证据仍然缺乏。未来的挑战是获取此类确凿数据。理想情况下，此类信息将带来新的治疗模式，为暴露于热应激/化学应激的人类胚胎/胎儿提供保护。
