Regulation of rat hepatic lipase by the composition of monomolecular films of lipid

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Abstract
The regulation of hepatic lipase (HL) by the lipid composition of monomolecular substrate films was examined using a monolayer technique at constant surface pressure. HL-catalyzed hydrolysis of triacylglycerol, a poor substrate for HL in pure monomolecular films, was activated by diradylglycerol and its phosphorylated derivatives in mixed films containing 10 mol % triacylglycerol. When triacylglycerol was progressively diluted with dialkylglycerol, triacylglycerol hydrolysis by HL was maximal between 90 and 98 mol % dialkylglycerol. The best activators, dialkylphosphatidic acid and dialkylphosphatidylethanolamine, increased triacylglycerol hydrolysis 13-14-fold, and the enhancement of HL-catalyzed triacylglycerol hydrolysis by the activator lipids was inversely related to the average mean molecular area of the mixed films. The hydrolysis of 5 mol % triacylglycerol in mixed films that also contained phosphatidylcholine and 0-20 mol % cholesterol was inhibited approximately 80% when the concentration of cholesterol was 10-13 mol %. Interestingly, between 15 and 17 mol % cholesterol the hydrolysis rate was restored to about 50% of the uninhibited rate, but at 20 mol % cholesterol this value decreased back to 80% inhibition of hydrolysis. The hydrolysis of phosphatidylethanolamine in mixed films with 0-20 mol % cholesterol decreased approximately 30% in films containing 10-12 mol % cholesterol. However, at 15 mol % cholesterol the hydrolysis rate was restored to the same level observed for a pure phosphatidylethanolamine film. This enhancement of HL activity occurred at about the same cholesterol concentration as the restoration of triacylglycerol hydrolysis observed for the triacylglycerol/phosphatidylcholine/cholesterol films.(ABSTRACT TRUNCATED AT 250 WORDS)

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