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Originally published In Press as doi:10.1074/jbc.M208661200 on February 3, 2003

J. Biol. Chem., Vol. 278, Issue 18, 16073-16081, May 2, 2003
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The Role of Apoptosis Signal-regulating Kinase 1 in Lymphotoxin-beta Receptor-mediated Cell Death*

Mei-Chieh Chenab, Ming-Jing Hwangc, Yang-Chieh Choua, Wei-Hsu Chencd, Genhong Chenge, Hiroyasu Nakanofk, Tien-Yau Luhg, Shen-Chih Maiah, and Shie-Liang Hsiehaij

From the a Institute and Department of Microbiology and Immunology, National Yang-Ming University, Taipei 11221, Taiwan, the c Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan, the i Immunology Research Center, National Yang-Ming University, Taipei 11221, Taiwan, the e Department of Microbiology, Immunology, and Molecular Genetics, Jonsson Comprehensive Cancer Center and Molecular Biology Institute, UCLA, Los Angeles, California 90095, the f Department of Immunology, Juntendo University School of Medicine, Tokyo 113, Japan, and the g Department of Chemistry, National Taiwan University, Taipei 106, Taiwan

LIGHT (homologous to lymphotoxins, shows inducible expression, and competes with herpes simplex virus glycoprotein D for herpesvirus entry mediator, a receptor expressed by T lymphocytes) is a member of the tumor necrosis factor superfamily that can interact with lymphotoxin-beta receptor (LTbeta R), herpes virus entry mediator, and decoy receptor (DcR3). In our previous study, we showed that LIGHT is able to induce cell death via the non-death domain containing receptor LTbeta R to activate both caspase-dependent and caspase-independent pathway. In this study, a LIGHT mutein, LIGHT-R228E, was shown to exhibit similar binding specificity as wild type LIGHT to LTbeta R, but lose the ability to interact with herpes virus entry mediator. By using both LIGHT-R228E and agonistic anti-LTbeta R monoclonal antibody, we found that signaling triggered by LTbeta R alone is sufficient to activate both caspase-dependent and caspase-independent pathways. Cross-linking of LTbeta R is able to recruit TRAF3 and TRAF5 to activate ASK1, whereas its activity is inhibited by free radical scavenger carboxyfullerenes. The activation of ASK1 is independent of caspase-3 activation, and kinase-inactive ASK1-KE mutant can inhibit LTbeta R-mediated cell death. This suggests that ASK1 is one of the factors involved in the caspase-independent pathway of LTbeta R-induced cell death.

* This work was mainly supported by National Science Council, Taiwan, Grants NSC 91-2320-B-010-053, NSC 91-2320-B010-092. Additional support came from the National Health Research Institute, Taiwan (NHRI-CN-BP-8902S) and the Ministry of Education (89-B-FA22-2-4) under the Program for Promoting Academic Excellence of Universities. This work was also supported by Chi-Mei Foundational Hospital, Tainan, Grant CMYM 8902.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.

b Present address: Dept. of Microbiology and Immunology, Taipei Medical University, Taipei 110, Taiwan.

d Present address: United Biomedical, Inc., New York, NY 11788.

h Present address: Anawrahta Biotechnology, Taipei 251, Taiwan.

j To whom all correspondence should be addressed: Institute of Microbiology and Immunology, National Yang-Ming University, Shih-Pai, Taipei 11221, Taiwan. Tel.: 886-2-28267161; Fax: 886-2-28212880; E-mail: slhsieh@ym.edu.tw.

k Supported by Precursory Research for Embryonic Science and Technology, Japan Science and Technology Corporation, and a grant from Human Frontier Science Program.

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