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Originally published In Press as doi:10.1074/jbc.M112311200 on March 1, 2002

J. Biol. Chem., Vol. 277, Issue 19, 16441-16447, May 10, 2002
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Purification and Characterization of a Doxorubicin-inhibited NADH-quinone (NADH-ferricyanide) Reductase from Rat Liver Plasma Membranes*

Chinpal KimDagger §, Frederick L. Crane, W. Page Faulk||, and D. James MorréDagger §

From the Departments of Dagger  Medicinal Chemistry and Molecular Pharmacology and  Biological Science, Purdue University, West Lafayette, Indiana 47907 and || Faulk Pharmaceutical Research, Indianapolis, Indiana 46240

Plasma membrane-associated redox systems play important roles in regulation of cell growth, internal pH, signal transduction, apoptosis, and defense against pathogens. Stimulation of cell growth and stimulation of the redox system of plasma membranes are correlated. When cell growth is inhibited by antitumor agents such as doxorubicin, capsaicin, and antitumor sulfonylureas, redox activities of the plasma membrane also are inhibited. A doxorubicin-inhibited NADH-quinone reductase was characterized and purified from plasma membranes of rat liver. First, an NADH-cytochrome b5 reductase, which was doxorubicin-insensitive, was removed from the plasma membranes by the lysosomal protease, cathepsin D. After removal of the NADH-cytochrome b5 reductase, the plasma membranes retained a doxorubicin-inhibited NADH-quinone reductase activity. The enzyme, with an apparent molecular mass of 57 kDa, was purified 200-fold over the cathepsin D-treated plasma membranes. The purified enzyme had also an NADH-coenzyme Q0 reductase (NADH: external acceptor (quinone) reductase; EC 1.6.5..) activity. Partial amino acid sequence of the enzyme showed that it was unique with no sequence homology to any known protein. Antibody against the enzyme (peptide sequence) was produced and affinity-purified. The purified antibody immunoprecipitated both the NADH-ferricyanide reductase activity and NADH-coenzyme Q0 reductase activity of plasma membranes and cross-reacted with human chronic myelogenous leukemia K562 cells and doxorubicin-resistant human chronic myelogenous leukemia K562R cells. Localization by fluorescence microscopy showed that the reaction was with the external surface of the plasma membranes. The doxorubicin-inhibited NADH-quinone reductase may provide a target for the anthracycline antitumor agents and a candidate ferricyanide reductase for plasma membrane electron transport.

* This work was supported in part by a grant from Eli Lilly Research Laboratories (Indianapolis, IN).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 may be addressed: Dept. of Medicinal Chemistry and Molecular Pharmacology, Hansen Life Science Research Building, Purdue University, West Lafayette, IN 47907. Tel.: 765-494-1388; Fax: 765-494-4007; E-mail: morre@pharmacy.purdue.edu (D. J. M.) or chinpal{at}purdue.edu (C. K.).

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