Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P20020 (adenosine triphosphatase)
 3,299 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Changes in the cation balance cause hydration and initiate the process of lens opacification. Such alterations were studied in human cataractous lenses and during the development of alloxan-induced diabetic cataract in rats by biochemical and histochemical techniques. The development of alloxan-induced cataract in rats was examined in vivo which showed cortical opacities beginning after 32 days. These opacities did progress to maturity after 64 days and finally the lenses were completely opacified after 96 days of alloxan treatment. The histochemical localization of sodium-potassium-activated adenosine triphosphatase using three different methods provided information on the possible role of this enzyme in normal and cataractous lenses. In human cataractous lenses, sodium-potassium adenosine triphosphatase activity was found to be considerably decreased, whereas no activity of this enzyme was localized in human diabetic cataractous lenses. An animal model provided evidence that an apparent decrease of sodium-potassium adenosine triphosphatase may be involved in the initiation of alloxan-induced diabetic cataract in rats.
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PMID:Studies on cataractogenesis in humans and in rats with alloxan-induced diabetes. I. Cation transport and sodium-potassium-dependent ATPase. 298 22