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, Gábor Bánhegyi

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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.

Original languageEnglish
Pages (from-to)3370-3374
Number of pages5
JournalJournal of Biological Chemistry
Issue number5
Publication statusPublished - Jan 30 2004


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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