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.
Inhibition of phosphatidylethanolamine synthesis by glucagon in isolated rat hepatocytes
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L B M Tijburg, M Houweling, M J H Geelen, L M G Van Golde; Inhibition of phosphatidylethanolamine synthesis by glucagon in isolated rat hepatocytes. Biochem J 1 February 1989; 257 (3): 645–650. doi: https://doi.org/10.1042/bj2570645
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