Intrapolypeptide disulfides in human αA-crystallin and their effect on chaperone-like function

被引：27

作者：

Cherian-Shaw M. ^{[1
]}

Smith J.B. ^{[2
]}

Jiang X.-Y. ^{[2
]}

Abraham E.C. ^{[1
,3
]}

机构：

[1] Dept. of Biochem. and Molec. Biology, Medical College of Georgia, Augusta, GA

[2] Department of Chemistry, University of Nebraska, Lincoln, NE

[3] Dept. Biocheistry and Molec. Biol., Medical College of Georgia, Augusta

来源：

Molecular and Cellular Biochemistry | 1999年 / 199卷 / 1-2期

基金：

美国国家卫生研究院;

关键词：

Alpha-crystallin; Chaperone; Disulfides; Human lens;

D O I：

10.1023/A:1006906615469

中图分类号：

学科分类号：

摘要：

We report studies on the role of protein-protein disulfides (PSSP) in the age-related loss of chaperone activity of α-cristallins. α1-Crystallin fraction was isolated from human lenses of different ages and the chaperone-like activity was determined before and after treatment with glutathione reductase (GR) and NADPH. The results confirmed an age-dependent decrease in chaperone-like function and significant improvement of this function by GR treatment. Electrospray ionization mass spectrometric (ESIMS) analysis of αA-crystallin suggested the presence of very little protein-glutathione mixed disulfides. ESIMS analysis of Asp-N digests of αA-crystallin revealed that nearly all the remaining portion of Cys-131 and Cys-142 of αA-crystallin was present in the form of intrapolypeptide disulfide bonds. These results show for the first time that predominantly disulfide bonds formed during aging contribute to the age-dependent loss in chaperone activity of α-crystallin in human lenses.

引用

页码：163 / 167

页数：4

共 23 条

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