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Horm Metab Res 1989; 21(11): 602-605
DOI: 10.1055/s-2007-1009298
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© Georg Thieme Verlag, Stuttgart · New York

Time Course of Hormonal Effects on Acetyl-CoA Carboxylase as Measured in Digitonin-Permeabilized Rat Hepatocytes

C. Bijleveld, W. J. Vaartjes, M. J. H. Geelen
  • Laboratory of Veterinary Biochemistry, University of Utrecht, Utrecht, The Netherlands
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Publication History

1988

1989

Publication Date:
14 March 2008 (online)

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Summary

Acetyl-CoA carboxylase activity was measured in digitonin-permeabilized rat hepatocytes by coupling the carboxylase reaction to the fatty acid synthase reaction. Using this assay the activity of acetyl-CoA carboxylase was covariant with the rate of fatty acid synthesis. Insulin and the tumor promotor phorbol myristate acetate were found to stimulate, and glucagon and noradrenaline to inhibit both cellular parameters. The stimulation of acetyl-CoA carboxylase by insulin developed slowly (15 to 30 min) whereas the phorbol myristate acetate effect developed faster (within 15 min). The inhibition of the enzyme caused by glucagon was already apparent within 1 min after hormone addition. Inhibition by noradrenaline, in the presence of propranolol, was also quite rapid and occurred within 2 min after addition of the agonist.

Key-Words

Fatty Acid Synthesis - Enzyme Regulation - Hormones - Acetyl-CoA Carboxylase - Digitonin - Rat Hepatocytes

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