Alterations in the lenticular protein profile in experimental @entity11822 -induced cataractogenesis and prevention by XXXX .

@entity3978 @entity231 @entity11822 @entity35 @entity13983
BACKGROUND: Accumulating evidence suggests that oxidative stress underlies age-related formation of @entity231 , and that antioxidants retard cataractogenesis. This study aimed to evaluate whether @entity13983 , a natural @entity3978 with antioxidant properties, prevents alterations in the lenticular protein profile in an experimental model of @entity11822 @entity231 . METHODS: Alterations in lenticular protein were determined by two-dimensional electrophoresis (2DE) and image analysis. Eluted aA-crystallin spots were analyzed by mass spectrometry. Western blot analysis was also performed to confirm the differential expression of certain crystallins and cytoskeletal proteins. RESULTS: In @entity231 lenses, 2DE and image analysis revealed approximately 45 and 60 prominent spots in soluble and insoluble protein fractions respectively. Analysis of the pI and molecular weight of protein spots revealed differences in the expression of crystallin proteins in soluble and insoluble fractions. Western blot analysis confirmed changes in the expression of aA- and bB1- crystallins in both soluble and insoluble protein fractions, while mass spectrometry confirmed the degradation of aA-crystallin in @entity11822 @entity231 lenses. Western blot analysis also confirmed the occurrence of altered expression of certain cytoskeletal proteins in insoluble fractions. However, the lenticular protein profile in lenses from @entity11822 -challenged, @entity13983 -treated @entity35 was essentially similar to that noted in lenses from normal @entity35 . CONCLUSIONS: The present study confirms the importance of structural and cytoskeletal proteins in the maintenance of lenticular transparency; the results also suggest that @entity13983 prevents lenticular protein alterations induced by @entity11822 in an experimental setting.
