Document Detail

Hsp72 inhibits Fas-mediated apoptosis upstream of the mitochondria in type II cells.
MedLine Citation:
PMID:  15632129     Owner:  NLM     Status:  MEDLINE    
Heat shock protein 72 (Hsp72) inhibits apoptosis induced by some stresses that trigger the intrinsic apoptosis pathway. However, with the exception of TNFalpha-induced apoptosis, a role for Hsp72 in modulating the extrinsic pathway of apoptosis has not been clearly established. In this study, it was demonstrated that Hsp72 could inhibit Fas-mediated apoptosis of type II CCRF-CEM cells, but not type I SW480 or CH1 cells. Similar results were obtained when Fas ligand or an agonistic Fas antibody initiated the Fas apoptosis pathway. In CCRF-CEM cells, Hsp72 inhibited mitochondrial membrane depolarization and cytochrome c release but did not alter surface Fas expression or processing of caspase-8 and Bid, indicating that Hsp72 acts upstream of the mitochondria to inhibit Fas-mediated apoptosis. Thus, the ability of Hsp72 to inhibit Fas-mediated apoptosis is limited to type II cells where involvement of the intrinsic pathway is required for efficient effector caspase activation.
Nicholas J Clemons; Katherine Buzzard; Rohan Steel; Robin L Anderson
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.     Date:  2005-01-04
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  280     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2005 Mar 
Date Detail:
Created Date:  2005-03-07     Completed Date:  2005-04-19     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  9005-12     Citation Subset:  IM    
Cancer Biology Laboratory, Peter MacCallum Cancer Centre, St Andrew's Place, East Melbourne 3002, Victoria, Australia.
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MeSH Terms
Amino Acid Chloromethyl Ketones / pharmacology
Antigens, CD95 / physiology*
Apoptosis / drug effects*
Caspases / antagonists & inhibitors,  metabolism
Cell Line
Cell Line, Tumor
Cysteine Proteinase Inhibitors / pharmacology
HSP72 Heat-Shock Proteins
Heat-Shock Proteins / physiology*
Mitochondria / physiology*
Grant Support
Reg. No./Substance:
0/Amino Acid Chloromethyl Ketones; 0/Antigens, CD95; 0/Cysteine Proteinase Inhibitors; 0/HSP72 Heat-Shock Proteins; 0/Heat-Shock Proteins; 0/benzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketone; EC 3.4.22.-/Caspases

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