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• W2022754926 endingPage "1949" @default.
• W2022754926 startingPage "1941" @default.
• W2022754926 abstract "The effect of zinc ions on carbohydrate metabolism and intracellular Zn2+ was studied in hepatocytes from fed rats. The addition of ZnCl2 to the medium led to an almost 3-fold increase in lactate production and an increase in net glucose production of about 50%. Half-maximal rates occurred at about 40 μM ZnCl2. These effects were not seen with Mn2+, Co2+, or Ni2+ up to 80 μM, whereas Cu2+ at 80 μM and Cd2+ or Pb2+ at 8 μM exhibited similar effects as 80 μM ZnCl2. Changes in intracellular Zn2+ were followed by single cell epifluorescence using zinquin as a specific probe. Intracellular free Zn2+ in isolated hepatocytes was 1.26 ± 0.27 μM, and the addition of ZnCl2 led to a concentration-dependent increase in epifluorescence. CdCl2 or PbCl2 at 8 μM was as potent as ZnCl2 at 20-80 μM, whereas NiCl2 at 80 μM was without effect. ZnCl2 completely abolished the inhibition of glycolysis by glucagon (cAMP). Glucagon led to a pronounced drop in cytosolic Zn2+. Both glucagon and zinc stimulated glycogenolysis by increasing the phosphorylation of glycogen phosphorylase but acted oppositely on glycolysis. Zinc overcame the inactivation of pyruvate kinase by glucagon without changing the hormone-induced protein phosphorylation. The antagonistic action of zinc and cAMP on glycolysis together with the rapid and marked decrease in free zinc concentration induced by glucagon (cAMP) may indicate an as yet unknown role of zinc as an important mediator of regulation of carbohydrate metabolism. The effect of zinc ions on carbohydrate metabolism and intracellular Zn2+ was studied in hepatocytes from fed rats. The addition of ZnCl2 to the medium led to an almost 3-fold increase in lactate production and an increase in net glucose production of about 50%. Half-maximal rates occurred at about 40 μM ZnCl2. These effects were not seen with Mn2+, Co2+, or Ni2+ up to 80 μM, whereas Cu2+ at 80 μM and Cd2+ or Pb2+ at 8 μM exhibited similar effects as 80 μM ZnCl2. Changes in intracellular Zn2+ were followed by single cell epifluorescence using zinquin as a specific probe. Intracellular free Zn2+ in isolated hepatocytes was 1.26 ± 0.27 μM, and the addition of ZnCl2 led to a concentration-dependent increase in epifluorescence. CdCl2 or PbCl2 at 8 μM was as potent as ZnCl2 at 20-80 μM, whereas NiCl2 at 80 μM was without effect. ZnCl2 completely abolished the inhibition of glycolysis by glucagon (cAMP). Glucagon led to a pronounced drop in cytosolic Zn2+. Both glucagon and zinc stimulated glycogenolysis by increasing the phosphorylation of glycogen phosphorylase but acted oppositely on glycolysis. Zinc overcame the inactivation of pyruvate kinase by glucagon without changing the hormone-induced protein phosphorylation. The antagonistic action of zinc and cAMP on glycolysis together with the rapid and marked decrease in free zinc concentration induced by glucagon (cAMP) may indicate an as yet unknown role of zinc as an important mediator of regulation of carbohydrate metabolism." @default.
• W2022754926 created "2016-06-24" @default.
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• W2022754926 date "1996-01-01" @default.
• W2022754926 modified "2023-10-03" @default.
• W2022754926 title "Intracellular Zinc Movement and Its Effect on the Carbohydrate Metabolism of Isolated Rat Hepatocytes" @default.
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• W2022754926 doi "https://doi.org/10.1074/jbc.271.4.1941" @default.
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