CELLS OVEREXPRESSING HSP27 SHOW ACCELERATED RECOVERY FROM HEAT-INDUCED NUCLEAR-PROTEIN AGGREGATION
CELLS OVEREXPRESSING HSP27 SHOW ACCELERATED RECOVERY FROM HEAT-INDUCED NUCLEAR-PROTEIN AGGREGATION
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DOI：
10.1006/bbrc.1994.2586
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发表时间：
1994-11-15
影响因子：
3.1
通讯作者：
LANDRY, J
中科院分区：
文献类型：
--
作者：
KAMPINGA, HH;BRUNSTING, JF;LANDRY, J
细胞暴露于热休克时的蛋白质变性/聚集是细胞死亡的可能原因。在细胞核中，蛋白质聚集通常与核定位过程的抑制和热诱导的细胞杀伤相关。在中国仓鼠023细胞中，通过预先加热（20 ± 44 ℃ +10小时37 ℃）诱导整个热休克蛋白（hsps）谱而使细胞耐热，热休克期间核蛋白聚集的程度降低，热休克后从聚集中恢复的速率提高。相反，仅过表达hsp 27的耐热中国仓鼠细胞系显示出对热形成核蛋白聚集体的敏感性不变，但显示出与耐热细胞相同的从核蛋白聚集体恢复的增强速率。这表明，加速恢复蛋白质聚集可能是部分负责热休克蛋白27介导的热保护。(C)1994年出版社出版。
Protein denaturation/aggregation upon cell exposure to heat shock is a likely cause of cell death. in the nucleus, protein aggregation has often been correlated to inhibition of nuclear located processes and heat-induced cell killing. in Chinese hamster 023 cells made thermotolerant by a prior heating (20'44 degrees C + 10h 37 degrees C) which induces the whole spectrum of heat shock proteins (hsps), the extent of nuclear protein aggregation during heat shock is reduced and the rate of recovery from aggregation after heat shock is enhanced. in contrast, a heat resistant Chinese hamster cell line overexpressing only hsp27 shows an unaltered sensitivity to formation of nuclear protein aggregates by heat, but shows the same enhanced rate of recovery from nuclear protein aggregation as thermo-tolerant cells. This suggests that accelerated recovery of protein aggregation could be partly responsible for hsp27-mediated thermoprotection. (C) 1994 Academic Press, Inc.