Glutathione reductase from human cataract lenses can be revived by reducing agents and by a molecular chaperone, α-crystallin

被引:12
|
作者
Rachdan, D
Lou, MF
Harding, JJ
机构
[1] Univ Oxford, Nuffield Lab Ophthalmol, Oxford OX2 6AW, England
[2] Univ Nebraska, Dept Vet & Biomed Sci, Lincoln, NE USA
关键词
alpha-crystallin; captopril; cataract; dithiothrietol; glutathione reductase;
D O I
10.1080/02713680590953110
中图分类号
R77 [眼科学];
学科分类号
100212 ;
摘要
Purpose: The aim of this study was to investigate how glutathione reductase (GR) loses its activity during cataract formation and whether it is possible to revive it back to the normal levels. Method: In this study, endogenous as well as synthetic reducing systems (GSH, TTase, DTT, captopril) and alpha-crystallin at different concentrations were incubated with the soluble fraction of human cataract lens protein. The activity of glutathione reductase with or without the reducing agents and alpha-crystallin was tested, and the difference in activity gained was calculated. Results: Five agents (GSH, DTT, TTase, captopril, alpha-low crystallin) were able to revive the activity of GR from human cataract lenses to different extents. Conclusion: This study shows that human lens GR activity was revived by different reducing agents as well as by a molecular chaperone (alpha-crystallin).
引用
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页码:919 / 925
页数:7
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