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Originally published In Press as doi:10.1074/jbc.M111860200 on May 14, 2002

J. Biol. Chem., Vol. 277, Issue 30, 27385-27392, July 26, 2002
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Regulation of Cellular Oncosis by Uncoupling Protein 2*

Edward M. MillsDagger , Dong XuDagger , María M. FergussonDagger , Christian A. Combs§, Yuhui Xu, and Toren FinkelDagger ||

From the Dagger  Cardiovascular Branch, § Confocal Core, and  Electron Microscopy Core, NHLBI, National Institutes of Health, Bethesda, Maryland 20892

Cell death can proceed through at least two distinct pathways. Apoptosis is an energy-dependent process characterized morphologically by cell shrinkage, whereas oncosis is a form of cell death induced by energy depletion and initially characterized by cell swelling. We demonstrate in HeLa cells but not in normal diploid fibroblasts that modest increases in the expression level of uncoupling protein 2 (UCP-2) leads to a rapid and dramatic fall in mitochondrial membrane potential and to a reduction of mitochondrial NADH and intracellular ATP. In HeLa cells, increased UCP-2 expression leads to a form of cell death that is not inhibited by the anti-apoptotic gene product Bcl-2 and that morphologically resembles cellular oncosis. We further describe the creation of a dominant interfering mutant of UCP-2 whose expression increases resting mitochondrial membrane potential and selectively increases the resistance to cell death following oncotic but not apoptotic stimuli. These results suggest that distinct genetic programs may regulate the cellular response to either apoptotic or oncotic stimuli.

* 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.

|| To whom correspondence should be addressed: Cardiovascular Branch, 10 Center Dr., Bldg. 10/6N-240, Bethesda, MD 20892-1622. Tel.: 301-402-4081; Fax: 301-402-9311; E-mail: finkelt@nih.gov.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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