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Originally published In Press as doi:10.1074/jbc.M010563200 on January 2, 2001

J. Biol. Chem., Vol. 276, Issue 12, 8825-8828, March 23, 2001
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Protein-disulfide Isomerase- and Protein Thiol-dependent Dehydroascorbate Reduction and Ascorbate Accumulation in the Lumen of the Endoplasmic Reticulum*

Gábor Nardai, László Braun, Miklós Csala, Valéria Mile, Péter CsermelyDagger , Angelo Benedetti§, József Mandl, and Gábor Bánhegyi

From the Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University, 1444 Budapest, Hungary and the § Dipartimento di Fisiopatologia e Medicina Sperimentale, Università di Siena, 53100 Siena, Italy

The transport and intraluminal reduction of dehydroascorbate was investigated in microsomal vesicles from various tissues. The highest rates of transport and intraluminal isotope accumulation (using radiolabeled compound and a rapid filtration technique) were found in hepatic microsomes. These microsomes contain the highest amount of protein-disulfide isomerase, which is known to have a dehydroascorbate reductase activity. The steady-state level of intraluminal isotope accumulation was more than 2-fold higher in hepatic microsomes prepared from spontaneously diabetic BioBreeding/Worcester rats and was very low in fetal hepatic microsomes although the initial rate of transport was not changed. In these microsomes, the amount of protein-disulfide isomerase was similar, but the availability of protein thiols was different and correlated with dehydroascorbate uptake. The increased isotope accumulation was accompanied by a higher rate of dehydroascorbate reduction and increased protein thiol oxidation in microsomes from diabetic animals. The results suggest that both the activity of protein-disulfide isomerase and the availability of protein thiols as reducing equivalents can play a crucial role in the accumulation of ascorbate in the lumen of the endoplasmic reticulum. These findings also support the fact that dehydroascorbate can act as an oxidant in the protein-disulfide isomerase-catalyzed protein disulfide formation.

* This work was supported by a Ministry of Health grant, Ministry of Education Grant FKFP 0652/97, Országos Tudományos Kutatási Alap Grants T032873, F022495, and F25206, Hungarian Academy of Sciences Grant F-226/98, an Italian-Hungarian intergovernmental research and development project grant, and a NATO linkage grant.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.

Dagger International Research Scholar of the Howard Hughes Medical Institute.

To whom correspondence should be addressed: Dept. of Medical Chemistry, Semmelweis University, P. O. Box 260, H-1444 Budapest, Hungary. Tel./Fax: 36-1-266-2615; E-mail: banhegyi@puskin.sote.hu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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