Sodium-potassium--dependent ATPase. II. Cytochemical localization during the reversal of galactose cataracts in rat.
The importance of enzyme Na-K-ATPase in the development of galactose-induced cataractogenesis is now well realized. In our recent studies we reported decreased level of activity of this enzyme with an increased duration of galactose feeding and the induced alterations in rat ocular lens. Our approach was to determine the level of Na-K-ATPase activity by ultrastructural cytochemical analysis of lenses and spectrophotometric analysis of the incubating media used for cytochemical localization as described by Ernst. Using these approaches, we have determined the activity level of this enzyme during the reversal phase of the galactose-induced injury to the lens. Our findings are presented in this report and show that the activity of Na-K-ATPase recovers rapidly and attains the normal level when the animals were transferred to Rat Chow diet after the establishment of mature cataracts resulting from galactose feeding. This study supports the previous biochemical and morphological findings that partial reversal of galactose-induced cataractous lens occurs upon discontinuation of feeding of cataractogenic agent galactose.
D000818:Animals; D002386:Cataract / Q000139:chemically induced / Q000201:enzymology*; D004032:Diet; D005260:Female; D005690:Galactose / Q000009:adverse effects; D006651:Histocytochemistry; D007908:Lens, Crystalline / Q000166:cytology / Q000201:enzymology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D051381:Rats; D012075:Remission, Spontaneous; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis*
D000254:Sodium-Potassium-Exchanging ATPase; D005690:Galactose