Sodium-potassium-dependent ATPase. III. Cytochemical localization during the reversal ofin uteroinduced galactose cataracts in rat

Abstract

Our previous ultrastructural cytochemistry and spectrophotometric studies of the adult Sprague Dawl ey rat ocular lens exhibited a decrease in the level of ouabain-sensitive Na-K-ATPase activity during galactose-induced cataractogenesis. Most of the enzyme activity was reinstated 130-days following the switch to a galactose-free diet after the establishment of cataracts in the animals. At this stage, however, a small nuclear opacity remained and normal Na-K-ATPase activity was not reestablished. In contrast, in in utero induced cataracts (through maternal feeding of galactose during pregnancy) the opacity was completely reversed 30-days postpartum. Results on Na-K-ATPase activity levels and localization in lenses of the newborn undergoing the cataract reversal process are presented in the present report. Methods reported by Ernst (1972) for cytochemical localization and quantisation of this enzyme were used for this study. The electron-dense reaction product for Na-K-ATPase was located and confined to lat...