Immunobiology Research Unit, K Floor, School of Medicine and Biomedical Sciences, University of Sheffield, Beech Hill Road, Sheffield S10 2RX, UK.
Cell Stress Chaperones. 2009 Nov;14(6):545-53. doi: 10.1007/s12192-009-0113-1. Epub 2009 Apr 9.
Although heat shock (stress) proteins are typically regarded as being exclusively intracellular molecules, it is now apparent that they can be released from cells in the absence of cellular necrosis. We and others have reported the presence of Hsp60 (HSPD1) and Hsp70 (HSPA1A) in the circulation of normal individuals and our finding that increases in carotid intima-media thicknesses (a measure of atherosclerosis) in subjects with hypertension at a 4-year follow-up are less prevalent in those having high serum Hsp70 (HSPA1A) levels at baseline suggests that circulating Hsp70 (HSPA1A) has atheroprotective effects. Given that circulating Hsp70 (HSPA1A) levels can be in the range which has been shown to elicit a number of biological effects in vitro, and our preliminary findings that Hsp70 (HSPA1A) binds to and is internalised by human endothelial cell populations, we speculate on the mechanisms that might be involved in the apparent atheroprotective properties of this protein.
尽管热休克（应激）蛋白通常被认为是细胞内分子，但现在显然它们可以在细胞坏死的情况下从细胞中释放出来。我们和其他人已经报道了 HSP60（HSPD1）和 HSP70（HSPA1A）在正常个体循环中的存在，并且我们发现，在高血压患者中，颈动脉内膜中层厚度（动脉粥样硬化的一种衡量标准）的增加在 4 年随访中，那些在基线时具有高血清 HSP70（HSPA1A）水平的患者中较少见，这表明循环 HSP70（HSPA1A）具有抗动脉粥样硬化作用。鉴于循环 HSP70（HSPA1A）水平可以在体外已经显示出引起多种生物学效应的范围内，并且我们的初步发现 HSP70（HSPA1A）与人类内皮细胞群体结合并被内化，我们推测可能涉及这种蛋白的明显抗动脉粥样硬化特性的机制。
