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The First Department of Surgery [J. H., W. K., S. S., H. M.] and Department of Medical Genetics, Biomedical Research Center [J. H., S. K., T. I., Y. T.], and The First Department of Physiology [S. S.], Osaka University Medical School, 2-2 Yamadaoka, Suita 565, Japan
Fas (Apo-1/CD95) belongs to the tumor necrosis factor/nerve growth factor receptor family and transmits apoptotic signals by binding to its ligand. Interleukin-1ß-converting enzyme (ICE), which shows substantial homology to the product of the cell death gene, ced-3, of Caenorhabditis elegans, is reported to be involved in Fas-mediated apoptosis. Using two human carcinoma-derived cell lines with undetectable levels of ICE, we found that an agonistic antihuman Fas antibody induces the activation of CPP32/Yama(-like) proteases that are ICE(-like) protease family members, and that a tetrapeptide inhibitor of CPP32/Yama protease, DEVD-CHO, inhibits the Fas-mediated activation of the proteases, Fas-mediated apoptosis, and CPP32/Yama(-like) proteolytic activities in vitro. Fas-mediated apoptosis is inhibited by the CPP32/Yama inhibitor DEVD-CHO, but not by the ICE inhibitor YVAD-CHO, suggesting a dominant role for the CPP32/Yama(-like) proteases and not ICE itself in Fas-mediated apoptosis of the human carcinoma cell lines.
1 This work was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science, and Culture of Japan.
2 To whom requests for reprints should be addressed, at Department of Medical Genetics, Biomedical Research Center, Osaka University Medical School, 2-2 Yamadaoka, Suita 565, Japan. Phone: 81-6-879-3360; Fax: 81-6-879-3369; E-mail: tsujimot@gene.med.osaka-u.ac.jp.
Received 11/21/95. Accepted 2/28/96.
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