Arylsulfatase-cytochemical localization in lenses of normal and galactose-fed rats

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Abstract
The mechanism of repair in the ocular lens was studied. As lysosomal enzymes were shown to play an important role in tissue repair, the status of lysosomal enzymes, such as acid phosphatase and arylsulfatases, was investigated in the normal and injured lens. The presence, distribution and possible role of arylsulfatases (EC 3.1.6.1) were examined in lenses of normal and galactose-fed rats. Arylsulfatases were localized in lenses using the cytochemical procedure described by Hopsu-Havu and Helminen (1974) using p-nitrocatechol sulfate as a substrate and then examined at the ultrastructural level. The reaction product resulting from arylsulfatase activity was mainly localized in the epithelial cells with very little activity in the cortical fibers. The intracellular activity was confined to lysosomes. Some extracellular activity was visible in the intercellular regions in both the epithelium and superficial cortex. With the progression of galactose-induced lesion in the epithelium the number of lysosomes exhibiting enzyme reaction product was found to have increased and the lysosomes closely abutted the capsule. The biochemical assay indicated a considerable increase in the activity or arylsulfatases with the continuation of a galactose diet. The possible role of arylsulfatases in the normal and cataractous lens is discussed.