The short-term regulation of hepatic acetyl-CoA carboxylase during starvation and re-feeding in the rat.
, 280 ( Pt 3)
733 - 737.
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.
|Title:||The short-term regulation of hepatic acetyl-CoA carboxylase during starvation and re-feeding in the rat.|
|Keywords:||AMP-Activated Protein Kinases, Acetyl-CoA Carboxylase, Animals, Enzyme Stability, Female, Insulin, Liver, Multienzyme Complexes, Polyethylene Glycols, Protein Kinases, Protein-Serine-Threonine Kinases, Rats, Starvation|
|UCL classification:||UCL > School of Life and Medical Sciences > Faculty of Life Sciences > UCL School of Pharmacy > Pharmaceutical and Biological Chemistry|
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