Ascorbate‐mediated electron transfer in protein thiol oxidation in the endoplasmic reticulum

FEBS Letters

Mile, Valéria¹  Braun, László¹  Kupcsulik, Péter¹  Szarka, András¹  Kardon, Tamás¹  Csala, Miklós¹  Bánhegyi, Gábor¹  Mandl, József¹ 

[1] Department of Medical Chemistry, Semmelweis University of Medicine, P.O. Box 260, H-1444 Budapest, Hungary

关键词: Ascorbate;    Dehydroascorbate;    Protein thiol;    Hydrogen peroxide;    Gulonolactone oxidase;    Endoplasmic reticulum;    ER;    endoplasmic reticulum;    GSH;    glutathione;    GSSG;    glutathione disulfide;    Mops;    morpholinepropanesulfonic acid;    HPLC;    high-pressure liquid chromatography;   

DOI  :  10.1016/S0014-5793(99)01412-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Addition of, or gulonolactone oxidase-dependent in situ generation of, ascorbate provoked the oxidation of protein thiols, which was accompanied by ascorbate consumption in liver microsomal vesicles. The maximal rate of protein thiol oxidation was similar upon gulonolactone, ascorbate or dehydroascorbate addition. Cytochrome P450 inhibitors (econazole, proadifen, quercetin) decreased ascorbate consumption and the gulonolactone or ascorbate-stimulated thiol oxidation. The results demonstrate that the ascorbate/dehydroascorbate redox couple plays an important role in electron transfer from protein thiols to oxygen in the hepatic endoplasmic reticulum, even in gulonolactone oxidase deficient species.

【 授权许可】

Unknown