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J. Biol. Chem., Vol. 280, Issue 10, 9005-9012, March 11, 2005

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Hsp72 Inhibits Fas-mediated Apoptosis Upstream of the Mitochondria in Type II Cells^*

Nicholas J. Clemons, Katherine Buzzard, Rohan Steel, and Robin L. Anderson

From the Cancer Biology Laboratory, Peter MacCallum Cancer Centre, St Andrew's Place, East Melbourne 3002, Victoria, Australia

Heat shock protein 72 (Hsp72) inhibits apoptosis induced by some stresses that trigger the intrinsic apoptosis pathway. However, with the exception of TNF-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.

Received for publication, December 16, 2004

^* This work was supported by Grant CA81421 from the NCI, National Institutes of Health (to R. L. A.) and a Cancer Council Victoria postdoctoral fellowship (to K. B.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Cancer Biology Laboratory, Peter MacCallum Cancer Centre, Locked Bag #1, A'Beckett St., Melbourne 8006, Victoria, Australia. Tel.: 61-3-9656-1284; Fax: 61-3-9656-1411; E-mail: robin.anderson{at}petermac.org.

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