Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0086543 (cataract)
 29,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Previous cytochemical and biochemical studies have shown an increase in the activity of acid phosphatase and arylsulfatase during the induction of galactose cataracts in rat lenses. It was postulated that these enzymes may be involved in lens fiber degradation observed during cataractogenesis, however, the role of these enzymes in the repair process was not ruled out. The present investigation has evaluated the level of acid phosphatase activity in lenses in which the induction of opacity is inhibited with the aldose reductase inhibitor sorbinil and during the recovery of galactose induced opacity. Sprague-Dawley rats received 50% galactose diet, or galactose diet with sorbinil, or laboratory chow diet. Following 20 days on this diet all rats received lab chow plus 50 mg kg-1 sorbinil (recovery diet). The lenses were removed at desired intervals following the initiation of the above three diets and following the transfer of animals to the recovery diet. Cytochemical localization and biochemical quantitation of acid phosphatase activity were performed with methods previously reported. Most of the enzyme activity was localized within the epithelial cells and superficial cortical fibers. In the epithelial cell layer, the enzyme activity was primarily localized in lysosomes and at extracellular sites near the epithelial cell membrane which abut each other and cortical fibers. In cortical fibers the enzyme activity was observed at various extracellular sites between the cell membranes of neighboring fibers. The effect of sorbinil, if any, and the possible role of acid hydrolases in the repair process during cataract reversal is discussed.
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PMID:Acid phosphatase II. Cytochemical localization in lenses of normal and galactose-fed rats. 392 63

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.
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PMID:Ultrastructural cytochemistry: effect of Sorbinil on arylsulfatases in cataractous lenses. 402 88