Effect of S-adenosylhomocysteine on insulin-independent release of pyruvate dehydrogenase activator from rat adipocyte plasma membranes

Abstract

The addition of insulin to adipocyte plasma membranes has been shown to release a low molecular weight, acid stable mediator which activates mitochondrial pyruvate dehydrogenase. The insulin-dependent release of this activator is dependent on the method used to prepare the plasma membranes. Adipocyte plasma membranes prepared in 0.25 M sucrose, 10 mM MOPS, pH 7.4 released an activator of pyruvate dehyrogenase in an insulin-independent manner. Insulin is required to stimulate phospholipid methylation in these membranes. The inhibition of insulin-stimulated phospholipid methylation with 1 mM S-adenosylhomocysteine resulted in a significant increase in amount and/or activity of the pyruvate dehydrogenase activator. The insulin-dependent release of mediators of insulin action from adipocyte plasma membranes may be regulated by phospholipid methylation.