Deamidation in human γS-crystallin from cataractous lenses is influenced by surface exposure

被引：62

作者：

Lapko, VN

Purkiss, AG

Smith, DL

Smith, JB

机构：

[1] Univ Nebraska, Dept Chem, Lincoln, NE 68588 USA

[2] Univ London Birkbeck Coll, Sch Crystallog, London, England

来源：

BIOCHEMISTRY | 2002年 / 41卷 / 27期

关键词：

D O I：

10.1021/bi015924t

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A major component of human nuclear cataracts is water-insoluble, high molecular weight protein. A significant component of this protein is disulfide bonded gammaS-crystallin that can be reduced to monomers by dithiothreitol. Analysis of this reduced gammaS-crystallin showed that deamidation of glutamine and asparagine residues is a principal modification. Deamidation is one of the modifications of lens crystallins associated with aging and cataractogenesis. One proposed hypothesis of cataractogenesis is that it develops in response to altered surface charges that cause conformational changes, which, in turn, permit formation of disulfide bonds and crystallin insolubility. This report, showing deamidation among the disulfide bonded gammaS-crystallins from cataractous lenses, supports this hypothesis.

引用

页码：8638 / 8648

页数：11

共 49 条

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