Heat shock factor (HSF), a transcriptional regulator with heat- activatable DNA binding ability, mediates the stress-induced expression of eukaryotic heat shock protein genes. Previous results from this laboratory demonstrated that a preparation of mixed male germ cell types from mouse testis exhibited a lower temperature threshold for activation of HSF1 DNA binding relative to other mouse cell types (Sarge, K. D., Bray, A. E., and Goodson, M. L. (1995) Nature 374, 126). The purpose of the present study was to determine whether the phenomenon of reduced HSF1 activation temperature is common to all testis cell types, both somatic and germ cell types, or whether it is a special property of male germ cells. The results show that a purified population of pachytene spermatocytes, one of the male germ cell types, exhibits a profile of reduced HSF1 activation temperature identical to that observed for the mixed germ cell preparation, with a threshold HSF1 activation temperature of 35 °C. Activation of HSF1 DNA binding in male germ cells by incubation at 38 °C is accompanied by the classic cellular stress response parameters of heat-induced HSF1 phosphorylation and increased expression of the hsp72 stress protein. In contrast, a preparation of somatic testis cell types exhibits HSF1 activation only at temperatures of 42 °C and above, a profile identical to that observed for mouse liver cells and mammalian cell lines. These results demonstrate that the phenomenon of reduced HSF1 activation temperature is a unique property of male germ cell types within the mammalian testis and demonstrate that HSF1 activated at this lower temperature threshold is fully capable of mediating a productive cellular stress response in these cell types.
|Number of pages||4|
|Journal||Journal of Biological Chemistry|
|State||Published - Aug 11 1995|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology