A1 Journal article – refereed
Heat stress downregulates FLIP and sensitizes cells to Fas receptor-mediated apoptosis




List of Authors: Tran SEF, Meinander A, Holmstrom TH, Rivero-Muller A, Heiskanen KM, Linnau EK, Courtney MJ, Mosser DD, Sistonen L, Eriksson JE
Publisher: NATURE PUBLISHING GROUP
Publication year: 2003
Journal: Cell Death and Differentiation
Journal name in source: CELL DEATH AND DIFFERENTIATION
Journal acronym: CELL DEATH DIFFER
Volume number: 10
ISSN: 1350-9047

Abstract
The heat shock response and death receptor-mediated apoptosis are both key physiological determinants of cell survival. We found that exposure to a mild heat stress rapidly sensitized Jurkat and HeLa cells to Fas-mediated apoptosis. We further demonstrate that Hsp70 and the mitogen-activated protein kinases, critical molecules involved in both stress-associated and apoptotic responses, are not responsible for the sensitization. Instead, heat stress on its own induced downregulation of FLIP and promoted caspase-8 cleavage without triggering cell death, which might be the cause of the observed sensitization. Since caspase-9 and -3 were not cleaved after heat shock, caspase-8 seemed to be the initial caspase activated in the process. These findings could help understanding the regulation of death receptor signaling during stress, fever, or inflammation.

Last updated on 2019-20-07 at 06:55