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J. Biol. Chem., Vol. 279, Issue 5, 3370-3374, January 30, 2004

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FAD Transport and FAD-dependent Protein Thiol Oxidation in Rat Liver Microsomes^*

Marianne Varsányi, András Szarka¶, Eszter Papp, Dóra Makai, Gábor Nardai, Rosella Fulceri||, Péter Csermely, József Mandl, Angelo Benedetti||, and Gábor Bánhegyi||**

From the Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, 1444 Budapest, Hungary, Endoplasmic Reticulum Research Group of the Hungarian Academy of Sciences and the Semmelweis University, 1444 Budapest, Hungary, ^¶Department of Biochemistry and Food Technology, Budapest University of Technology and Economics, 1521 Budapest, Hungary, and the ^||Department of Pathophysiology, Experimental Medicine and Public Health, University of Siena, 53100 Siena, Italy

The transport of FAD and its effect on disulfide bond formation was investigated in rat liver microsomal vesicles. By measuring the intravesicular FAD-accessible space, we observed that FAD permeates across the microsomal membrane and accumulates in the lumen. Rapid filtration experiments also demonstrated the uptake and efflux of the compound, which could be inhibited by atractyloside and 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid. FAD entering the lumen promoted the oxidation of protein thiols and increased the intraluminal oxidation of glucose-6-phosphate. These findings support the notion that, similar to yeast, free FAD may have a decisive role in the mechanism of oxidative protein folding in the endoplasmic reticulum lumen of mammalian cells.

Received for publication, July 18, 2003 , and in revised form, November 7, 2003.

^* This work was supported by a Hungarian-Italian Bilateral Intergovernmental S&T Cooperation Grant, by grants T32873, TS040865, and T37357 from the Hungarian Scientific Research Fund, by a grant from the Hungarian Academy of Sciences, by Grants ETT 32/03 and ETT 613/03 from the Ministry of Health and Welfare, Hungary, and by Grant RBAU014PJA from the Italian Ministry of University and Research. 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.

^** Recipient of a North Atlantic Treaty Organization-Consiglio Nazionale delle Ricerche Outreach Fellowship to Siena. To whom correspondence should be addressed. Tel./Fax: 36-1-2662615; E-mail: banhegyi{at}puskin.sote.hu.

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