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

摘要: Rapid inhibition of acetyl-CoA carboxylase (ACC) activity in rat liver response to 6 h starvation and rapid re-activation 2-6 re-feeding chow were shown be due changes the expressed existing enzyme. Decreases increases ACC concentration occurred at later stages transitions, i.e. 6-48 8-24 respectively. The decrease was primarily its phosphorylation state, demonstrated by a significantly decreased Vmax. increased Ka for citrate enzyme purified avidin-Sepharose chromatography from h- or 48 h-starved rats. These effects totally reversed within 2-4 re-feeding. Changes closely correlated with reciprocal AMP-activated protein kinase (AMP-PK) over fed starved re-fed transition. Increases ratio cyclic-AMP-dependent lagged behind increase AMP-PK activity. activities plasma insulin time courses