hsp27 protects mitochondria of thermotolerant cells against apoptotic stimuli
Samali, Afshin ; Robertson, John D. ; Peterson, Elisabeth ; Manero, Florence ; van Zeijl, Leone ; Paul, Catherine ; Cotgreave, Ian A. ; Arrigo, André-Patrick ; Orrenius, Sten
Samali, Afshin
Robertson, John D.
Peterson, Elisabeth
Manero, Florence
van Zeijl, Leone
Paul, Catherine
Cotgreave, Ian A.
Arrigo, André-Patrick
Orrenius, Sten
Repository DOI
Publication Date
2001-01-01
Type
Article
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Citation
Samali, Afshin; Robertson, John D. Peterson, Elisabeth; Manero, Florence; van Zeijl, Leone; Paul, Catherine; Cotgreave, Ian A.; Arrigo, André-Patrick; Orrenius, Sten (2001). hsp27 protects mitochondria of thermotolerant cells against apoptotic stimuli. Cell Stress & Chaperones 6 (1), 49-58
Abstract
Enhanced cell survival and resistance to apoptosis during thermotolerance correlates with an increased expression of heat shock proteins (Hsps). Here we present additional evidence in support of the hypothesis that the induction of Hsp27 and Hsp72 during acquired thermotolerance in Jurkat T-lymphocytes prevents apoptosis. In thermotolerant cells, Hsp27 was shown to associate with the mitochondrial fraction, and inhibition of Hsp27 induction during thermotolerance in cells transfected with hsp27 antisense potentiated mitochondrial cytochrome c release after exposure to various apoptotic stimuli, despite the presence of elevated levels of Hsp72. Caspase activation and apoptosis were inhibited under these conditions. In vitro studies revealed that recombinant Hsp72 more efficiently blocked cytochrome c-mediated caspase activation than did recombinant Hsp27. A model is presented for the inhibition of apoptosis during thermotolerance in which Hsp27 preferentially blocks mitochondrial cytochrome c release, whereas Hsp72 interferes with apoptosomal caspase activation.
Funder
Publisher
Springer Nature
Publisher DOI
10.1379/1466-1268(2001)006<0049:hpmotc>2.0.co;2
Rights
Attribution-NonCommercial-NoDerivs 3.0 Ireland