Heat shock protein 27 prevents gamma radiation-induced apoptosis

2002 ◽  
Vol 38 ◽  
pp. S145
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Gamma Radiation ◽  
Heat Shock Protein 27 ◽  
Radiation Induced ◽  
Induced Apoptosis

scholarly journals Upregulation of heat shock protein 27 confers resistance to actinomycin D-induced apoptosis in cancer cells

FEBS Journal ◽  
2013 ◽  
Vol 280 (18) ◽  
pp. 4612-4624 ◽  
Author(s):  
Wenbo Ma ◽  
Yan Teng ◽  
Hui Hua ◽  
Jinlin Hou ◽  
Ting Luo ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Actinomycin D ◽  
Heat Shock Protein 27 ◽  
Induced Apoptosis ◽  
Apoptosis In Cancer Cells

scholarly journals Inhibition of Daxx-Mediated Apoptosis by Heat Shock Protein 27

2000 ◽  
Vol 20 (20) ◽  
pp. 7602-7612 ◽  
Author(s):  
Steve J. Charette ◽  
Josée N. Lavoie ◽  
Herman Lambert ◽  
Jacques Landry
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Major Change ◽  
Heat Shock Protein 27 ◽  
Supramolecular Organization ◽  
Protective Function ◽  
Cellular Protection ◽  
Hsp27 Phosphorylation ◽  
Fas Pathway ◽  
Induced Apoptosis

ABSTRACT Heat shock protein 27 (HSP27) confers cellular protection against a variety of cytotoxic stresses and also against physiological stresses associated with growth arrest or receptor-mediated apoptosis. Phosphorylation modulates the activity of HSP27 by causing a major change in the supramolecular organization of the protein, which shifts from oligomers to dimers. Here we show that phosphorylated dimers of HSP27 interact with Daxx, a mediator of Fas-induced apoptosis, preventing the interaction of Daxx with both Ask1 and Fas and blocking Daxx-mediated apoptosis. No such inhibition was observed with an HSP27 phosphorylation mutant that is only expressed as oligomers or when apoptosis was induced by transfection of a Daxx mutant lacking its HSP27 binding domain. HSP27 expression had no effect on Fas-induced FADD- and caspase-dependent apoptosis. However, HSP27 blocked Fas-induced translocation of Daxx from the nucleus to the cytoplasm and Fas-induced Daxx- and Ask1-dependent apoptosis. The observations revealed a new level of regulation of the Fas pathway and suggest a mechanism for the phosphorylation-dependent protective function of HSP27 during stress and differentiation.

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