A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Heat stress downregulates FLIP and sensitizes cells to Fas receptor-mediated apoptosis
Tekijät: Tran SEF, Meinander A, Holmstrom TH, Rivero-Muller A, Heiskanen KM, Linnau EK, Courtney MJ, Mosser DD, Sistonen L, Eriksson JE
Kustantaja: NATURE PUBLISHING GROUP
Julkaisuvuosi: 2003
Journal: Cell Death and Differentiation
Tietokannassa oleva lehden nimi: CELL DEATH AND DIFFERENTIATION
Lehden akronyymi: CELL DEATH DIFFER
Vuosikerta: 10
Numero: 10
Aloitussivu: 1137
Lopetussivu: 1147
Sivujen määrä: 11
ISSN: 1350-9047
DOI: https://doi.org/10.1038/sj.cdd.4401278
Verkko-osoite: https://www.nature.com/articles/4401278
Tiivistelmä
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.
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.
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