Abstract
We have examined the expression of the heat shock protein (hsp70) gene in human cells. The transcription of the hsp70 gene and accumulation of cytoplasmic hsp70 mRNA is induced by serum stimulation. Populations of HeLa cells and human embryonic kidney cells (cell line 293) were serum starved. Upon serum stimulation, the level of hsp70 mRNA transiently increases between 12 and 18 hr to a 10-fold higher level. The increased levels of hsp70 mRNA can be accounted for by a 10- to 15-fold increase in the rate of transcription of the hsp70 gene. When cells were serum-stimulated in the presence of an inhibitor of DNA synthesis, 1-beta-D-arabinofuranosylcytosine (araC), the levels of hsp70 mRNA were induced to only 20% of the maximal level detected in the absence of the inhibitor. This suggests that the expression of the hsp70 gene is coupled to DNA synthesis. The cloned human hsp70 gene contains regulatory sequences that confer serum-stimulated transcriptional control. The endogenous hsp70 gene and the transfected chimeric gene containing sequences upstream of the hsp70 gene fused to bacterial chloramphenicol acetyltransferase are both temporally expressed in stable transfectants of cell line 293 cells. The endogenous hsp70 mRNA and the chimeric mRNA reach maximum levels 12-18 hr after serum stimulation.