We have demonstrated an increase in activity of
arylsulfatase A and B during
galactose induced
cataract development in rats. Our recent investigation shows that
acid phosphatase activity, which increases substantially during
galactose cataract development in rats, could be contained to near normal level if
Sorbinil, an
aldose reductase inhibitor, was fed along with
galactose to the rat. We have observed that the activity of other lysosomal
enzymes,
arylsulfatase A and/or B, also increases during
galactose cataractogenesis. In the present report, we provide information with regards to the effect of
Sorbinil on the activity of these
enzymes during cataractogenesis. A modified Hopsu-Havu and Helminen method (1974) with p-nitrocatecholsulfate as substrate was used for localization of both
arylsulfatase A and B; and the method of Hara et al. (1979) was utilized to obtain quantitative data on the level of
arylsulfatase A and B activity. Ultrastructural cytochemistry shows that
arylsulfatase activity in all
lenses was primarily localized in epithelial cells in lysosomes with very little or no activity in cortical fibers. The number of
arylsulfatase positive lysosomes and the activity level of these
enzymes increased with the progression of
cataract development.
Galactose induced damage to lens morphology and increase in activity of
arylsulfatase A and B was inhibited by inclusion of 50mg/Kg (diet)
Sorbinil in the
galactose containing cataractogenic diet. However,
Sorbinil had no significant effect on the
enzyme activity following the establishment of mature
cataracts.