Targeted disruption of hsp70.1 sensitizes to osmotic stress
Targeted disruption of hsp70.1 sensitizes to osmotic stress
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DOI：
10.1093/embo-reports/kvf175
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发表时间：
2002-09-01
期刊：
影响因子：
7.7
通讯作者：
Seo, JS
中科院分区：
文献类型：
--
作者：
Shim, EH;Kim, JI;Seo, JS
70 kDa 热休克蛋白 (Hsp70) 在细胞存活和响应各种应激刺激的耐热性中发挥着关键作用。两个几乎相同的基因 hsp70.1 和 hsp70.3 在应对环境胁迫时迅速诱导 Hsp70。然而，目前尚不清楚这两个基因是否受到各种应激的差异调节。为了解决 hsp70.1 和 hsp70.3 基因在应激反应中的生理作用，我们培育了专门缺乏 hsp70.1 的小鼠。与快速诱导 hsp70.1 和 hsp70.3 mRNA 的热休克相反，渗透应激选择性诱导 hsp70.1 的转录。在 hsp70.1 缺陷的胚胎成纤维细胞中，渗透压显着降低了细胞活力。此外，当体内施加渗透压时，hsp70.1缺陷小鼠的肾髓质细胞凋亡增加。综上所述，我们的结果表明 hsp70 基因的差异表达有助于应激反应，并且 hsp70.1 基因在渗透压耐受性中起着关键作用。
The 70 kDa heat shock protein (Hsp70) plays a critical role in cell survival and thermotolerance in response to various stress stimuli. Two nearly identical genes, hsp70.1 and hsp70.3, in response to environmental stress, rapidly induce Hsp70. However, it remains unclear whether these two genes are differentially regulated by various stresses. To address the physiological role of the hsp70.1 and hsp70.3 genes in the stress response, we generated mice that specifically lack hsp70.1. In contrast to heat shock, which rapidly induced both hsp70.1 and hsp70.3 mRNA, osmotic stress selectively induced transcription of hsp70.1. In hsp70.1-deficient embryonic fibroblasts, osmotic stress markedly reduced cell viability. Furthermore, when osmotic stress was applied in vivo, hsp70.1-deficient mice exhibited increased apoptosis in the renal medulla. Taken together, our results demonstrate that differential expression of hsp70 genes contributes to the stress response and that the hsp70.1 gene plays a critical role in osmotolerance.