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Titolo:
Activation of Fas inhibits heat-induced activation of HSF1 and up-regulation of hsp70
Autore:
Schett, G; Steiner, CW; Groger, M; Winkler, S; Graninger, W; Smolen, J; Xu, QB; Steiner, G;
Indirizzi:
Univ Vienna, Div Rheumatol, Dept Internal Med 3, A-1090 Vienna, Austria Univ Vienna Vienna Austria A-1090 Internal Med 3, A-1090 Vienna, Austria Univ Vienna, Dept Immunodermatol, A-1090 Vienna, Austria Univ Vienna Vienna Austria A-1090 Immunodermatol, A-1090 Vienna, Austria Univ Vienna, Div Infectiol, Dept Internal Med 1, A-1090 Vienna, Austria Univ Vienna Vienna Austria A-1090 Internal Med 1, A-1090 Vienna, Austria Austrian Acad Sci, Inst Biomed Aging Res, Innsbruck, Austria Austrian AcadSci Innsbruck Austria iomed Aging Res, Innsbruck, Austria Ludwig Boltzmann Inst Rheumatol & Balneol, Vienna, Austria Ludwig Boltzmann Inst Rheumatol & Balneol Vienna Austria ienna, Austria
Titolo Testata:
FASEB JOURNAL
fascicolo: 8, volume: 13, anno: 1999,
pagine: 833 - 842
SICI:
0892-6638(199905)13:8<833:AOFIHA>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
TUMOR-NECROSIS-FACTOR; STRESS-INDUCED APOPTOSIS; SHOCK-PROTEIN HSP70; MEDIATED APOPTOSIS; MONOCLONAL-ANTIBODY; ICE/CED-3 PROTEASE; DEATH FACTOR; ICE-LIKE; CELLS; EXPRESSION;
Keywords:
Fas activation; antibody; heat shock element; apoptosis hsp;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Schett, G Univ1090nna, Div Rheumatol, Dept Internal Med 3, Wahringer Gurtel 18-20, A- Univ Vienna Wahringer Gurtel 18-20 Vienna Austria A-1090 20, A-
Citazione:
G. Schett et al., "Activation of Fas inhibits heat-induced activation of HSF1 and up-regulation of hsp70", FASEB J, 13(8), 1999, pp. 833-842

Abstract

Activation of heat shock factor (HSF) 1-DNA binding and inducible heat shock protein (hsp) 70 (also called hsp72) expression enables cells to resist various forms of stress and survive. Fas, a membrane-bound protein, is a central proapoptotic factor; its activation leads to a cascade of events, resulting in programmed cell death. These two mechanisms with contradictory functions, promoting either cell survival or death, were examined for their potential to inhibit each other's activation. Induction of FAS-mediated signaling was followed by a rapid decrease in HSF1-DNA binding and inducible hsp70 expression. Inhibition of HSF1-DNA binding was demonstrated to be basedon absent hyperphosphorylation of HSF1 during FAS signaling. These effectsof FAS activation on the HSF1/hsp70 stress response were blocked by ICE (caspase 1) inhibitors, suggesting an ICE-mediated process. Furthermore, inhibition of HSF1/hsp70 was accompanied by an increase in apoptosis rates from20% to 50% in response to heat stress. When analyzing the effects of HSF1/hsp70 activation on Fas-mediated apoptosis, protection from apoptosis was seen in cells with induced hsp70 protein levels, but not in cells that were just induced for HSF1-DNA binding. Thus, we conclude that inhibition of HSF1/hsp70 stress response during Fas-mediated apoptosis and vice versa may facilitate a cell. to pass a previously chosen pathway, stress resistance or apoptosis, without the influence of inhibitory signals.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 31/10/20 alle ore 00:31:56