Abstract
Acyl-CoA: 1,2-diacylglycerol O-acyltransferase (EC 2.3.1.20) activity of rat liver microsomes was found to be stimulated by 1-acyl- sn-glycero-3-phosphocholine at low concentrations, but was inhibited above 0.2 mM. Diacylglycerol acylation was optimal at 75 μM lysophosphatidylcholine, resulting in a more than 2-fold activation of the enzyme. Acyltransferase activity disappeared above 0.5 mM lysophosphatidylcholine levels. 0.05% sodium taurocholate supplementation reduced diacylglycerol acyltransferase activity by approx. 2 3 over the entire range of lysophosphatidylcholine concentrations. 1- O-Hexadecylpropanediol-3-phosphocholine was shown to mimic lysophosphatidylcholine at stimulatory and at inhibitory concentrations in the absence and in the presence of sodium taurocholate, thus ruling out acyl-CoA depletion due to lysophos-phatidylcholine acylation as a cause of depressed triacylglycerol synthesis at higher lysophosphatidylcholine levels. 1-Acyl- sn-glycero-3-phosphoethanolamine stimulated diacylglycerol acyltransferase to a lesser extent, without showing inhibition at higher concentrations. The data point towards a direct effect of the lysophospholipids on the acyltransferase system.
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