Regulation of the synthesis of heat-shock proteins in heat-resistant variants of Chinese hamster fibroblasts.
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.
Laszlo
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Department of Radiology, Washington University School of Medicine, St. Louis, Missouri 63108.
D000222:Adaptation, Physiological; D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D003412:Cricetulus; D005347:Fibroblasts; D014644:Genetic Variation; D006360:Heat-Shock Proteins / Q000096:biosynthesis*; D006358:Hot Temperature
D006360:Heat-Shock Proteins