Decreased heat- and tumor necrosis factor-mediated hsp28 phosphorylation in thermotolerant HeLa cells.
Heat shock or tumor necrosis factor rapidly stimulated the phosphorylation of the mammalian low molecular weight stress protein hsp28. We have found that both phenomena are greatly decreased in cells which are made tolerant to heat. This observation correlated with a better survival of thermotolerant cells exposed to either heat or TNF treatment. The results suggest that the phosphorylation of hsp28 may be linked to the resistance of the cells to the deleterious effects induced by either heat or a mediator of inflammation such as TNF.
Arrigo
A P
AP
University Claude Bernard Lyon-I, Centre de Génétique Moléculaire et Cellulaire, CNRS-UMR 106, Villeurbanne, France.
Michel
M R
MR
D015180:Electrophoresis, Gel, Two-Dimensional; D006367:HeLa Cells; D006360:Heat-Shock Proteins / Q000187:drug effects / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D008970:Molecular Weight; D010766:Phosphorylation / Q000187:drug effects; D014409:Tumor Necrosis Factor-alpha / Q000494:pharmacology*
D006360:Heat-Shock Proteins; D014409:Tumor Necrosis Factor-alpha