Interleukin 1{beta}-converting Enzyme Related Proteases/Caspases Are Involved in TRAIL-induced Apoptosis of Myeloma and Leukemia Cells

doi:10.1083/jcb.137.1.221

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© The Rockefeller University Press, 0021-9525/1997//221 $5.00
The Journal of Cell Biology, Volume 137, Number 1, , 1997 221-229

Article

Interleukin 1β-converting Enzyme Related Proteases/Caspases Are Involved in TRAIL-induced Apoptosis of Myeloma and Leukemia Cells

Sara M. Mariani, Bernd Matiba, Elena A. Armandola^*, and Peter H. Krammer

Tumor Immunology and ^* Molecular Immunology Program/Division of Immunogenetics, German Cancer Research Center, Heidelberg, Germany

The Fas/APO-1/CD95 ligand (CD95L) and the recently cloned TRAILligand belong to the TNFfamily and share the ability to induceapoptosis in sensitive target cells. Little information is availableon the degree of functional redundancy between these two ligandsin terms of target selectivity and intracellular signallingpathway(s). To address these issues, we have expressed andcharacterized recombinant mouse TRAIL. Specific detection withnewly developed rabbit anti-TRAIL antibodies showed that thefunctional TRAIL molecule released into the supernatant ofrecombinant baculovirus-infected Sf9 cells is very similar to that associated with the membrane fraction of Sf9 cells.CD95L resistant myeloma cells were found to be sensitive toTRAIL, displaying apoptotic features similar to those of theCD95L- and TRAIL-sensitive T leukemia cells Jurkat. To assessif IL-1β-converting enzyme (ICE) and/or ICE-related proteases(IRPs) (caspases) are involved in TRAIL-induced apoptosis of both cell types, peptide inhibition experiments were performed.The irreversible IRP/caspase-inhibitor AcYVAD-cmk and the reversibleIRP/caspase-inhibitor Ac-DEVD-CHO blocked the morphologicalchanges, disorganization of plasma membrane phospholipids, DNA fragmentation, and loss of cell viability associated withTRAIL-induced apoptosis. In addition, cells undergoing TRAIL-mediatedapoptosis displayed cleavage of poly(ADP)-ribose polymerase(PARP) that was completely blocked by Ac-DEVD-CHO.

These results indicate that TRAIL seems to complement the activityof the CD95 system as it allows cells, otherwise resistant,to undergo apoptosis triggered by specific extracellular ligands.Conversely, however, induction of apoptosis in sensitive cellsby TRAIL involves IRPs/caspases in a fashion similar to CD95L. Thus, differential sensitivity to CD95L and TRAIL seems tomap to the proximal signaling events associated with receptortriggering.

Abbreviations used in this paper: Ab, antibody; CD95, CD95/APO-1/ Fas receptor; CD95L, CD95/APO-1/Fas ligand; CHO, aldehyde; cmk, chloromethylketone; ICE, IL-1β converting enzyme; IRP, ICE-related protease; PARP, poly(ADP)-ribose polymerase; SN, supernatant.

Please address all correspondence to P.H. Krammer, Tumor Immunology Program, Division of Immunogenetics, German Cancer ResearchCenter, Im Neuenheimer Feld 280, D-69120 Heidelberg, Germany.Tel.: 49 6221 423717. Fax: 49 6221 411715. E-Mail: P.Krammer{at}DKFZ-Heidelberg.de

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