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Originally published In Press as doi:10.1074/jbc.M107005200 on August 23, 2001

J. Biol. Chem., Vol. 276, Issue 43, 39938-39944, October 26, 2001
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Apoptosis-inducing Membrane Vesicles
A NOVEL AGENT WITH UNIQUE PROPERTIES*

Satoshi JodoDagger §, Sheng XiaoDagger , Andreas Hohlbaum, David StrehlowDagger , Ann Marshak-Rothstein, and Shyr-Te JuDagger ||

From the Departments of Dagger  Medicine and  Microbiology, the Arthritis Center, School of Medicine, Boston University School of Medicine, Boston, Massachusetts 02118

The CD95 ligand (FasL) transmembrane protein is found on activated T cells and cells outside the immune system. A well-known turnover process of membrane FasL is mediated by matrix metalloproteinase, which generates soluble FasL (sFasL). Here, we demonstrate that membrane FasL turnover occurs effectively through the release of membrane vesicles. Quantitative analysis indicates that this process is as effective as sFasL release for FasL-3T3 cells but somewhat less effective for FasL-expressing T cells. The apoptosis-inducing membrane vesicles display unique properties not found in FasL-expressing cells and sFasL. Unlike sFasL, vesicle-associated FasL remained bioactive, killing the same panel of targets that are susceptible to FasL-expressing cells. In contrast to FasL-expressing T cells, FasL-mediated killing by vesicles do not involve LFA-1/ICAM interaction and do not depend on de novo protein synthesis. These observations indicate that the release of FasL-bearing vesicles contributes to the turnover of cell-associated FasL, but the impact of the bioactive FasL-expressing vesicles on the function of cell-associated FasL is different from that of sFasL.


* This work was supported in part by National Institute of Health Grants AI36938 and ES10244 (to S. T. J.) and GM58724 and CA90691 (to A. M. R.).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.

§ Supported by a grant from the Ministry of Education, Japan.

|| To whom correspondence should be addressed: K508. Arthritis Center, 715 Albany Street, Boston University Medical Campus, Boston, MA 02118. Tel.: 617-638-4303; Fax: 617-638-5226; E-mail: jushyrte@acs.bu.edu


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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