The short-term regulation of hepatic acetyl-CoA carboxylase during starvation and re-feeding in the rat

Rapid inhibition of acetyl-CoA carboxylase (ACC) activity in rat liver in response to 6 h starvation and rapid re-activation in response to 2-6 h of re-feeding chow were shown to be due to changes in the expressed activity of existing enzyme. Decreases and increases in ACC concentration occurred at...

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Bibliographic Details
Published in:Biochemical journal 1991-12, Vol.280 (3), p.733-737
Main Authors: MUNDAY, M. R, MILIC, M. R, TAKHAR, S, HOLNESS, M. J, SUGDEN, M. C
Format: Article
Language:English
Subjects:
Acetyl-CoA Carboxylase - metabolism
AMP-Activated Protein Kinases
Animals
Biological and medical sciences
Enzyme Stability
Feeding. Feeding behavior
Female
Fundamental and applied biological sciences. Psychology
Insulin - blood
Liver - metabolism
Multienzyme Complexes - metabolism
Polyethylene Glycols
Protein Kinases - metabolism
Protein-Serine-Threonine Kinases
Rats
Starvation - metabolism
Vertebrates: anatomy and physiology, studies on body, several organs or systems
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Summary:Rapid inhibition of acetyl-CoA carboxylase (ACC) activity in rat liver in response to 6 h starvation and rapid re-activation in response to 2-6 h of re-feeding chow were shown to be due to changes in the expressed activity of existing enzyme. Decreases and increases in ACC concentration occurred at later stages of the transitions, i.e. 6-48 h starvation and 8-24 h re-feeding respectively. The decrease in expressed activity of ACC was due primarily to changes in its phosphorylation state, demonstrated by a significantly decreased Vmax. and significantly increased Ka for citrate of enzyme purified by avidin-Sepharose chromatography from 6 h- or 48 h-starved rats. These effects were totally reversed within 2-4 h of chow re-feeding. Changes in the activity of purified ACC closely correlated with reciprocal changes in the activity of AMP-activated protein kinase (AMP-PK) over the fed to starved to re-fed transition. Increases in the activity ratio of cyclic-AMP-dependent protein kinase in response to starvation lagged behind the increase in AMP-PK and the decrease in ACC activity. Changes in AMP-PK and ACC activities of rat liver closely correlated with changes in plasma insulin concentration in response to time courses of starvation and re-feeding.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2800733