title: Monoacylglycerol lipase activity in cardiac myocytes.
abstract: Monoacylglycerol lipase activity in homogenates of isolated myocardial cells (myocytes) from rat hearts was recovered in both particulate and soluble subcellular fractions. The activity present in the microsomal (100,000 X g pellet) fraction was solubilized by treatment with Triton X-100 and combined with the 100,000 X g supernatant fraction; the properties of monoacylglycerol lipase were investigated with this soluble enzyme preparation. The Km for the hydrolysis of a 2-monoolein substrate was 16 microM. The rates of hydrolysis of 1-monoolein and 2-monoolein were identical, and 1-monoolein was a competitive inhibitor (Ki = 20 microM) of the hydrolysis of 2-monoolein. Monoacylglycerol lipase activity was regulated by product inhibition according to the following order of potency: fatty acyl CoA greater than free fatty acids greater than fatty acyl carnitine.
authors.affiliation: Department of Pharmacology and Therapeutics, Faculty of Medicine, University of Calgary, Alta., Canada.
authors.forename: D L
authors.initials: DL
authors.lastname: Severson
authors.forename: M
authors.initials: M
authors.lastname: Hee-Cheong
mesh_terms: D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D006868:Hydrolysis; D008994:Monoacylglycerol Lipases / Q000378:metabolism*; D009206:Myocardium / Q000166:cytology / Q000201:enzymology*; D051381:Rats; D013347:Subcellular Fractions / Q000201:enzymology
chemical_list: D002265:Carboxylic Ester Hydrolases; D008994:Monoacylglycerol Lipases