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. 1989 Feb 1;257(3):645–650. doi: 10.1042/bj2570645

Inhibition of phosphatidylethanolamine synthesis by glucagon in isolated rat hepatocytes.

L B Tijburg 1, M Houweling 1, M J Geelen 1, L M Van Golde 1
PMCID: PMC1135636  PMID: 2539092

Abstract

Exposure of isolated rat hepatocytes to glucagon or chlorophenylthio cyclic AMP led to an inhibition of the incorporation of [1,2-14C]ethanolamine into phosphatidylethanolamine. Pulse-chase experiments and measurement of the activities of the enzymes involved in the CDP-ethanolamine pathway provided evidence that the inhibitory effect of glucagon on the synthesis de novo of phosphatidylethanolamine was not caused by a diminished conversion of ethanolamine phosphate into CDP-ethanolamine. The observations suggested that the glucagon-induced inhibition of the biosynthesis of phosphatidylethanolamine is probably due to a decreased supply of diacylglycerols, resulting in a decreased formation of phosphatidylethanolamine from CDP-ethanolamine and diacylglycerols.

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Selected References

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