JBC Transcription and Nuclear Factor Monoclonals

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Originally published In Press as doi:10.1074/jbc.M210756200 on February 10, 2003

J. Biol. Chem., Vol. 278, Issue 17, 14723-14731, April 25, 2003
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BcR-induced Apoptosis Involves Differential Regulation of C16 and C24-Ceramide Formation and Sphingolipid-dependent Activation of the Proteasome*

Bart-Jan KroesenDagger §, Susan JacobsDagger , Benjamin J. Pettus, Hannie Sietsma||, Jan Willem Kok**, Yusuf A. Hannun, and Lou F. M. H. de LeijDagger

From the Dagger  Department of Pathology and Laboratory Medicine, Medical Biology branch, University Hospital Groningen, Hanzeplein 1, 9713 GZ Groningen, The Netherlands,  Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, South Carolina 29425, || Department of Pathology, University Hospital Groningen, Hanzeplein 1, 9713 GZ Groningen, The Netherlands, and ** Department of Cell Biology, University of Groningen, Antonius Deusinglaan 1, 9713AV Groningen, The Netherlands

In this study, we describe an ordered formation of long- and very long-chain ceramide species in relation to the progression of B-cell receptor (BcR) triggering induced apoptosis. An early and caspase-independent increase in long-chain ceramide species, in which C16- ceramide predominated, was observed 6 h after BcR triggering. In contrast, very long-chain ceramide species were generated later, 12-24 h after BcR triggering. The formation of these very long-chain ceramide species, in which C24-ceramide predominated, required the activation of effector caspases. BcR-induced formation of long-chain ceramide species resulted in proteasomal activation and degradation of XIAP and subsequent activation of effector caspases, demonstrating an important cell-biological mechanism through which long-chain ceramides may be involved in the progression of BcR triggering induced apoptosis and subsequent formation of very long-chain ceramide species. BcR-induced activation of the proteasome was blocked with ISP-1/myriocin, a potent and selective inhibitor of serine palmitoyl transferase that catalyzes the first and rate-limiting step in the de novo formation of ceramide. Both ISP-1 and clasto-lactacystin beta -lactone, an irreversible inhibitor of the proteasome, prevented BcR cross-linking-induced XIAP degradation. Also, a mutant XIAP lacking the ubiquitin-ligating ring finger motif was completely resistant to proteasome-mediated degradation, and Ramos cells overexpressing XIAP became highly resistant to BcR cross-linking-induced activation of caspases. The formation of C16-ceramide in response to BcR cross-linking was found unaltered in XIAP overexpressing Ramos cells, whereas C24-ceramide formation was completely abolished. These results demonstrate how de novo generated long-chain ceramide species may be involved in the activation of downstream effector caspases and subsequent formation of very long-chain ceramide species. As such, these results provide novel and important insights into the significance of specific ceramide species in defined stages of apoptosis.

* The costs of publication of this article were defrayed in part by the payment of page charges. The 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: Dept. Pathology and Laboratory Medicine/Medical Biology Branch, University Hospital Groningen, Hanzeplein 1, 9713 GZ Groningen, The Netherlands. Tel.: 31-50-3614291; Fax: 31-50-3619911; E-mail: b.j.kroesen@thorax.azg.nl.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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