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J. Biol. Chem., Vol. 279, Issue 6, 4811-4819, February 6, 2004

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VDAC1 Is a Transplasma Membrane NADH-Ferricyanide Reductase^*

Mark A. Baker, Darius J. R. Lane, Jennifer D. Ly, Vito De Pinto¶||, and Alfons Lawen**

From the Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Building 13D, 100 Wellington Road, Melbourne, Victoria 3800, Australia and the ^¶Department of Chemical Sciences, Laboratory of Biochemistry and Molecular Biology, Universita di Catania, viale A. Doria 6, Catania I-95125, Italy

Porin isoform 1 or VDAC (voltage-dependent anion-selective channel) 1 is the predominant protein in the outer mitochondrial membrane. We demonstrated previously that a plasma membrane NADH-ferricyanide reductase activity becomes up-regulated upon mitochondrial perturbation, and therefore suggested that it functions as a cellular redox sensor. VDAC1 is known to be expressed in the plasma membrane; however, its function there remained a mystery. Here we show that VDAC1, when expressed in the plasma membrane, functions as a NADH-ferricyanide reductase. VDAC1 preparations purified from both plasma membrane and mitochondria fractions exhibit NADH-ferricyanide reductase activity, which can be immunoprecipitated with poly- and monoclonal antibodies directed against VDAC(1). Transfecting cells with pl-VDAC1-GFP, which carries an N-terminal signal peptide, directs VDAC1 to the plasma membrane, as shown by confocal microscopy and FACS analysis, and significantly increases the plasma membrane NADH-ferricyanide reductase activity of the transfected cells. This novel enzymatic activity of the well known VDAC1 molecule may provide an explanation for its role in the plasma membrane. Our data suggest that a major function of VDAC1 in the plasma membrane is that of a NADH(-ferricyanide) reductase that may be involved in the maintenance of cellular redox homeostasis.

Received for publication, October 7, 2003 , and in revised form, October 22, 2003.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Current address: Dept. of Biological Science, University of Newcastle, Callaghan, New South Wales 2308, Australia.

^|| Supported by Italian Ministry of Research (FIRB) Grant RBNE01ARR4.

^** To whom correspondence should be addressed. Tel.: 61-3-9905-3711; Fax: 61-3-9905-3726; E-mail: alfons.lawen{at}med.monash.edu.au.

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