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中国仓鼠成纤维细胞耐热变体中热休克蛋白合成的调控。

Regulation of the synthesis of heat-shock proteins in heat-resistant variants of Chinese hamster fibroblasts.

作者信息

Laszlo A

机构信息

Department of Radiology, Washington University School of Medicine, St. Louis, Missouri 63108.

出版信息

Radiat Res. 1988 Dec;116(3):427-41.

PMID:3205908
Abstract

The synthesis of the major heat-shock proteins (hsp) was compared in normal and heat-resistant Chinese hamster fibroblasts which express higher levels of the 70 kDa heat-shock protein (hsp70). Following exposure to a variety of experimental conditions that induce the elevated synthesis of the hsp, higher relative levels of hsp70 and lower relative levels of hsp89 and hsp110 were found in the heat-resistant variants. This effect was observed with all inducers tested. The relatively greater synthesis of hsp70 and relatively lower synthesis of hsp89 occurred at all temperatures tested and was found to be independent of cell culture conditions. The relatively greater increase in the levels of hsp70 in the heat-resistant variants after a mild heat shock was found to be a reflection of elevated levels of messenger RNA coding for this polypeptide. These results indicate that the heat-shock response in mammalian cells displays coordinate regulatory features and that the alteration of the expression of one of the hsp may affect the expression of the others.

摘要

在正常和耐热的中国仓鼠成纤维细胞中比较了主要热休克蛋白(hsp)的合成情况,这些细胞表达较高水平的70kDa热休克蛋白(hsp70)。在暴露于多种诱导hsp合成增加的实验条件后,在耐热变体中发现hsp70的相对水平较高,而hsp89和hsp110的相对水平较低。在所有测试的诱导剂中都观察到了这种效应。在所有测试温度下,hsp70的合成相对较多,而hsp89的合成相对较少,并且发现这与细胞培养条件无关。发现在轻度热休克后,耐热变体中hsp70水平的相对较大增加反映了编码该多肽的信使RNA水平的升高。这些结果表明,哺乳动物细胞中的热休克反应具有协同调节特征,并且一种hsp表达的改变可能会影响其他hsp的表达。

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