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Volume 272, Number 46, Issue of November 14, 1997 pp. 29099-29103
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Influence of Protein-Glutathione Mixed Disulfide on the Chaperone-like Function of alpha -Crystallin

(Received for publication, August 4, 1997, and in revised form, September 10, 1997)

Mary Cherian Dagger , Jean B. Smith § , Xiang-Yu Jiang § and Edathara C. Abraham Dagger

From the Dagger  Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta, Georgia 30912-2100 and the § Department of Chemistry, University of Nebraska, Lincoln, Nebraska 68588-0304

In an earlier report we showed that incubation of alpha -crystallin with oxidized glutathione results in significant loss of its chaperone-like activity. In the present study, we determined the effect of protein-glutathione mixed disulfides (PSSG), formed at Cys-131 in bovine alpha A-crystallin, and Cys-131 and Cys-142 in human alpha A-crystallin, on the function of alpha -crystallin as a molecular chaperone. After incubation of calf and young human alpha L-crystallin fractions with oxidized glutathione, levels of PSSG were determined by performic acid oxidation of the mixed disulfides followed by reversed-phase high pressure liquid chromatography separation of phenylisothiocyanate-derivatized glutathione sulfonic acid. Levels of PSSG increased from 0.01 to 0.14 nmol/nmol (20 kDa) in bovine alpha L-crystallin and from 0.022 to 0.25 nmol/nmol in human alpha L-crystallin. The presence of glutathione adducts at Cys-131 and Cys-142 were confirmed by mass spectral analysis. The chaperone-like activity was determined by the heat denaturation assay using beta L-crystallin as the target protein. To examine the reversibility of the effect of mixed disulfides on chaperone activity, studies were done before and after reduction with the glutathione reductase system. Increased levels of PSSG resulted in lower chaperone activities. Treatment with the glutathione reductase system led to 80% reduction in PSSG levels with a concomitant recovery of the chaperone activity. These results suggest that cysteine(s) in the alpha A-crystallin subunit play an important role in the function of alpha -crystallin as a molecular chaperone.


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