Thermotolerance and cell death are distinct cellular responses to stress: dependence on heat shock proteins

A1 Originalartikel i en vetenskaplig tidskrift (referentgranskad)


Interna författare/redaktörer


Publikationens författare: Samali A, Holmberg CI, Sistonen L, Orrenius S
Förläggare: ELSEVIER SCIENCE BV
Publiceringsår: 1999
Tidskrift: FEBS Letters
Tidskriftsakronym: FEBS LETT
Volym: 461
Nummer: 3
Artikelns första sida, sidnummer: 306
Artikelns sista sida, sidnummer: 310
Antal sidor: 5
ISSN: 0014-5793
eISSN: 1873-3468


Abstrakt

We tested the hypothesis that heat shock protein (Hsp) induction and cell death are mutually exclusive responses to stress. Despite activation of heat shock transcription factor 1 at temperatures ranging from 40 to 46 degrees C, Hsp72 and Hsp27 were not induced above 42 degrees C. Moreover, cells underwent apoptosis at 44 degrees C and necrosis at 46 degrees C, with mitochondrial cytochrome c release at both temperatures. However, only apoptosis was associated with caspase activation. Treatment of cells,vith z-VAD-fmk prior to heat shock at 44 degrees C failed to restore Hsp induction despite inhibition of heat-induced apoptosis. Furthermore, accumulation of Hsps after incubation at 42 degrees C rendered the cells resistant to apoptosis, These results suggest that lack of Hsp induction is the cause rather than the consequence of cell death.


Nyckelord

apoptosis, caspase, heat shock factor 1, heat shock protein, necrosis, thermotolerance

Senast uppdaterad 2019-21-05 vid 05:36