Abstract
A phospholipid has been purified from rat liver membranes which copurified with an insulin-sensitive glyco-phospholipid isolated from H35 hepatoma cells. The polar head group of this phospholipid was generated by treatment with a phosphatidylinositol-specific phospholipase C from Staphylococcus aureus and purified through a C18 extraction column. Like insulin, the addition of this polar head group to isolated rat adipocytes inhibited the stimulatory effect of isoproterenol on phospholipid methyltransferase. The polar head group was also active on a subcellular fraction. The addition of the polar head group to microsomes isolated from isoproterenol-treated adipocytes produced a time-dependent inactivation of phospholipid methyl-transferase, approaching basal activity. It is proposed that the effects of insulin on phospholipid methyl-transferase may be mediated by this polar head group.
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