Myocardial Lipase Research Articles

Inhibition of myocardial lipase by palmityl CoA

The lipase activity of the adult rat heart consists of at least two components; a lipoprotein lipase and a “hormone-sensitive” or triglyceride lipase. The control of the triglyceride lipase by intermediates of lipid metabolism was studied in rat heart homogenates. Perfusion of hearts with fatty acids, glucose or no exogenous substrate did not alter lipase activity. Bovine serum albumin (BSA) stimulated the in vitro lipase activity whereas palmityl-coenzyme A (CoA) was a potent inhibitor. Other fatty acid intermediates such as acetyl-CoA, acetyl-carnitine, palmityl-carnitine and palmitate had little or no effect. Long-chain acyl CoA may be an important intermediate for matching triglyceride hydrolysis with the supply of extracellular fatty acids and the rates of fatty acid oxidation.

Myocardial lipase activities in the diabetic rat heart

Myocardial lipase activities in the diabetic rat heart

Activity of myocardial lipase using natural edible oils as substrates

AbstractRat heart homogenates were tested for their lipolytic activity toward synthetic and natural substrates such as edible oils. Triolein was hydrolyzed very efficiently by myocardial lipase whereas trierucin was not cleaved by the enzyme. Among the natural substrates, safflower oil, which has the highest degree of unsaturation, was hydrolyzed to a greater extent than the other oils. Mustard oil rich in erucic acid formed a poor substrate for the myocardial lipase.

118) - Effects of isoproterenol and iodoacetamide on myocardial lipase activity in the rat

118) - Effects of isoproterenol and iodoacetamide on myocardial lipase activity in the rat