Reports of atypical heat shock response in some tumour cell lines emphasize the possibilities of alternate stress response mechanisms. We demonstrate here that P388D1, a mouse macrophage tumour cell line, failed to induce heat shock proteins (HSPs) in response to either heat stress (42°C, 1. h) or to heavy metal stress induced by arsenic trioxide (5-20. μM). Heat shock transcriptional factor 1 (HSF1) that mediates transcriptional up regulation of HSPs during stress was found to be deficient in transactivation despite its binding to the promoter region of HSP genes. Interestingly, cells exhibited thermotolerance in the absence of induced HSPs. However, the tolerance was abrogated in cells treated with cycloheximide (250. ng/ml) suggested that thermotolerance was dependent on de novo protein synthesis.
|Number of pages||5|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - Jan 4 2013|
- Heat shock response
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology