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[Character of alpha-crystallin molecular chaperone activity in selenite cataract]
1Department of Ophthalmology, Xijing Hospital, Fourth Military Medical University, Xi'an 710032, China.
Purpose:
To evaluate the character of alpha-crystallin molecular chaperone activity in selenite cataract.
Methods:
alpha-Crystallin from lenses of normal young rats and lenses with selenite cataract were separated and purified by gel filtration chromatography. The chaperone activity of alpha-crystallin was assayed by mearsuring heat-induced aggregation and scattering of catalase.
Results:
alpha-Crystallin in both normal and cataractous lenses specifically prevented catalase against thermal aggregation compared with control proteins. The preventive ability in alpha H-crystallin was less than in alpha L-crystallin. Chaperone activity was diminished in selenite cataract. There was statistically significant difference in chaperone activity between normal and cataractous lenses in both alpha H-crystallin and alpha L-crystallin respectively.
Conclusion:
The reduction of alpha-crystallin chaperone activity in selenite cataract by preventing thermal aggregation of catalase is an important process in cataract formation.