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Originally published In Press as doi:10.1074/jbc.M102465200 on May 21, 2001

J. Biol. Chem., Vol. 276, Issue 29, 27432-27440, July 20, 2001
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Activation of Pro-death Bcl-2 Family Proteins and Mitochondria Apoptosis Pathway in Tumor Necrosis Factor-alpha -induced Liver Injury*

Yongge Zhao, Shuchen Li, Erin E. Childs, Diane K. Kuharsky, and Xiao-Ming YinDagger

From the Department of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261

Tumor necrosis factor-alpha (TNFalpha )-induced cytotoxicity contributes to the pathogenesis in inflammatory and immune responses. Here, we studied the role of pro-death Bcl-2 family proteins and the mitochondria apoptosis pathway in the development of TNFalpha -induced hepatic injury during endotoxemia. After treating mice with lipopolysaccharide or TNFalpha in the presence of D-galactosamine, Bid was cleaved and translocated to mitochondria in hepatocytes. Independently, Bax was also activated by the death receptor engagement and translocated to mitochondria. However, its subsequent insertion into the mitochondrial membrane depends on Bid. Nevertheless, Bid was required, but Bax could be dispensed for the mitochondrial release of cytochrome c from mitochondria, suggesting that Bid could activate additional downstream molecules other than Bax. The lack of this Bid-dependent mitochondria activation and cytochrome c release in the bid-deficient mice was responsible for the significantly delayed effector caspase activation and hepatocyte injury upon endotoxin treatment, culminating in a prolonged survival of the bid-deficient mice. Additional genetic factor(s) could further modify the dependence of TNFalpha toxicity on the mitochondria pathway as the bid-deficient 129/SvJ mice manifested an even higher resistance than the same type of mice in C57BL/6 background. The functional significance of the mitochondria apoptosis pathway was thus elucidated in the TNFalpha -mediated pathogenesis in vivo.

* This work was supported in part by the Howard Temin award (K01 CA74885) and R01 CA83817 from the National Institutes of Health, the Charlotte Geyer Foundation, and the Competitive Medical Research Fund from the University of Pittsburgh (to X.-M. Y.).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.

Dagger To whom correspondence should be addressed: Dept. of Pathology, University of Pittsburgh School of Medicine, 7th Floor, Scaife Hall, 3550 Terrace St., Pittsburgh, PA 15261. Tel.: 412-648-8436; Fax: 412-383-9594; E-mail: xmyin@pitt.edu.

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