HEAT-SHOCK IS LETHAL TO FIBROBLASTS MICROINJECTED WITH ANTIBODIES AGAINST HSP70
HEAT-SHOCK IS LETHAL TO FIBROBLASTS MICROINJECTED WITH ANTIBODIES AGAINST HSP70
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DOI：
10.1126/science.3175665
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发表时间：
1988-10-21
期刊：
影响因子：
56.9
通讯作者：
WELCH, WJ
中科院分区：
文献类型：
--
作者：
RIABOWOL, KT;MIZZEN, LA;WELCH, WJ
一小组高度保守的蛋白质的合成响应于升高的温度和诱导应激的其他试剂是原核和真核细胞的普遍特征。虽然相关证据表明，这些蛋白质在应激期间和应激后的生存中发挥作用，但在哺乳动物细胞中没有直接证据支持这一点。为了评估最高度保守的热休克蛋白（hsp）家族在热休克期间的作用，通过针微量注射将亲和纯化的hsp70单克隆抗体引入成纤维细胞。除了在温和的热休克处理后损害热诱导的hsp70蛋白向细胞核的移位外，注射的细胞不能在45 ℃的短暂温育中存活。C.注射对照抗体的细胞在类似的热休克中存活。这些结果表明，热应激期间和之后，这些细胞的存活需要功能性hsp70。
Synthesis of a small group of highly conserved proteins in response to elevated temperature and other agents that induce stress is a universal feature of prokaryotic and eukaryotic cells. Although correlative evidence suggests that these proteins play a role in enhancing survival during and after stress, there is no direct evidence to support this in mammalian cells. To assess the role of the most highly conserved heat shock protein (hsp) family during heat shock, affinity-purified monoclonal antibodies to hsp70 were introduced into fibroblasts by needle microinjection. In addition to impairing the heat-induced translocation of hsp70 proteins into the nucleus after mild heat shock treatment, injected cells were unable to survive a brief incubation at 45.degree. C. Cells injected with control antibodies survived a similar heat shock. These results indicate that functional hsp70 is reauired for survival of these cells during and after thermal stress.