The role of phosphorylation in the α-adrenergic-mediated inhibition of rat hepatic pyruvate kinase |
| |
Authors: | Kurt E. Steiner Timothy M. Chan Thomas H. Claus John H. Exton Simon J. Pilkis |
| |
Affiliation: | Department of Physiology and the Laboratories of the Howard Hughes Medical Institute, Vanderbilt University Medical School, Nashville, TN 37232, U.S.A. |
| |
Abstract: | Phenylephrine in the presence of 1-methyl-3-isobutylxanthine and propanolol caused a 40–50% inhibition of pyruvate kinase (type L) activity in isolated hepatocytes, which was accompanied by a 2–3-fold increase in the phosphate content of the enzyme. These changes were blocked by the α-adrenergic antagonist dihydroergocryptine and could not be accounted for by the slight increase in cyclic AMP-dependent protein kinase activity generated by the α-adrenergic agonist. It is concluded that a significant component of the inhibition of hepatic pyruvate kinase mediated by α-adrenergic agonists can be attributed to a cyclic AMP-independent alteration in the phosphorylation state of the enzyme. |
| |
Keywords: | α-Adrenergic action Glucagon Phosphorylation Pyruvate kinase |
本文献已被 ScienceDirect 等数据库收录! |