Abstract
Fru 2,6-P2 was present in isolated foetal hepatocytes at a concentration of 1.6 nmol per g cells. When foetal hepatocytes were exposed to glucagon no changes were observed either in the concentration of Fru 2,6-P2 and lactate release or in the activities of 6-phosphofructo-2-kinase and pyruvate kinase. Incubation of purified 6-phosphofructo-2-kinase with the catalytic subunit of protein kinase did not change the enzyme activity. The inhibition by sn-glycerol 3-phosphate was much lower for the foetal than for adult enzyme. These results suggest that an isoenzyme of 6-phosphofructo-2-kinase in foetal hepatocytes different from that of adult hepatocytes may be present.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cyclic AMP / biosynthesis
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Cyclic AMP / pharmacology
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Fructosediphosphates / metabolism*
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Glucagon / pharmacology
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Glycerophosphates / pharmacology
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Hexosediphosphates / metabolism*
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Lactates / metabolism
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Lactic Acid
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Liver / drug effects
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Liver / embryology*
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Liver / metabolism
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Phosphofructokinase-1 / antagonists & inhibitors
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Phosphofructokinase-1 / metabolism
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Protein Kinases / metabolism
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Pyruvate Kinase / metabolism
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Rats
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Rats, Inbred Strains
Substances
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Fructosediphosphates
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Glycerophosphates
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Hexosediphosphates
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Lactates
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Lactic Acid
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fructose 2,6-diphosphate
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Glucagon
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alpha-glycerophosphoric acid
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Cyclic AMP
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Protein Kinases
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Phosphofructokinase-1
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Pyruvate Kinase