[Character of alpha-crystallin molecular chaperone activity in selenite cataract].
OBJECTIVE
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.


CONCLUSIONS
The reduction of alpha-crystallin chaperone activity in selenite cataract by preventing thermal aggregation of catalase is an important process in cataract formation.
Yan
H
H
Department of Ophthalmology, Xijing Hospital, Fourth Military Medical University, Xi'an 710032, China.
Hui
Y
Y
Li
M
M
Zhang
X
X
Zhang
Y
Y
Wu
L
L
D000818:Animals; D000831:Animals, Newborn; D002374:Catalase / Q000378:metabolism; D002386:Cataract / Q000139:chemically induced / Q000378:metabolism*; D007908:Lens, Crystalline / Q000737:chemistry / Q000378:metabolism; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D018038:Sodium Selenite; D038201:alpha-Crystallins / Q000737:chemistry / Q000378:metabolism*
D018832:Molecular Chaperones; D038201:alpha-Crystallins; D002374:Catalase; D018038:Sodium Selenite