Acid phosphatase II. Cytochemical localization in lenses of normal and galactose-fed rats

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.