Adrenaline and the regulation of acetyl-coenzyme A carboxylase in rat epididymal adipose tissue. Inactivation of the enzyme is associated with phosphorylation and can be reversed on dephosphorylation

• Published in: Biochemical journal 1979-10, Vol.184 (1), p.23-32
• Main Authors: Brownsey, R W, Hughes, W A, Denton, R M
• Format: Article
• Language: English
• Subjects: Acetyl-CoA Carboxylase - antagonists & inhibitors; Adipose Tissue - drug effects; Adipose Tissue - enzymology; Animals; Calcium - pharmacology; Citrates - pharmacology; Densitometry; Epididymis - drug effects; Epididymis - enzymology; Epinephrine - pharmacology; In Vitro Techniques; Ligases - antagonists & inhibitors; Magnesium - pharmacology; Male; Phosphates - metabolism; Phosphoprotein Phosphatases - metabolism; Phosphorylation; Rats
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj1840023

1. Exposure of rat epididymal fat-pads or isolated fat-cells to adrenaline results in a decrease in acetyl-CoA carboxylase activity measured both in initial extracts and in extracts incubated with potassium citrate; in addition the concentration of citrate required to give half-maximal activation may also be increased. 2. Incorporation of 32Pi into acetyl-CoA carboxylase within intact fat-cells was investigated and evidence is presented that adrenaline increases the extent of phosphorylation of the enzyme. 3. Dephosphorylation of 32P-labelled acetyl-CoA carboxylase was studied in cell extracts. The rate of release of 32P is increased by 5mM-MgCl2 plus 10--100 microM-Ca2+, whereas it is inhibited by the presence of bivalent metal ion chelators such as EDTA and citrate. 4. The effects of adrenaline on the kinetic properties of acetyl-CoA carboxylase disappear if pad or cell extracts are treated with Mg2+ and Ca2+ under conditions that also lead to dephosphorylation of the enzyme. 5. The results of this study represent convincing evidence that adrenaline inactivates acetyl-CoA carboxylase in adipose-tissue preparations by increasing the degree of phosphorylation of the enzyme.