Regulation of the multiple molecular forms of rat liver glucose 6-phosphate dehydrogenase by insulin and dietary restriction.
Insulin treatment of virgin female rats increased the hepatic activity of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase to levels 3.4 and 1.5 fold higher than controls. The increase in glucose 6-phosphate dehydrogenase activity was attributed to increased activity of all three dimer species. Thus dimer bands, 1, 2 and 3 of insulin-treated animals were 5, 3 and 2-fold higher respectively than controls. The activity of glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase decreased with fasting to 55% and 72% respectively of controls. The decrease in glucose 6-phosphate dehydrogenase activity reflected a lower activity of dimer bands 2 and 3 only, which were 62% and 39% of control activity respectively after three days fasting. A shift towards band 1 was observed under both conditions of starvation as well as under conditions of insulin treatment.
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005508:Food Deprivation; D005954:Glucosephosphate Dehydrogenase / Q000378:metabolism*; D007328:Insulin / Q000494:pharmacology*; D008099:Liver / Q000187:drug effects / Q000201:enzymology*; D051381:Rats; D011919:Rats, Inbred Strains
D007328:Insulin; D005954:Glucosephosphate Dehydrogenase