Stimulation of a neutral triacylglycerol hydrolase from rat heart by phosphatidylethanolamine and lysophosphatidylethanolamine.
Triacylglycerol hydrolase activity measured at pH 7.5 in a pH 5.2 precipitate fraction from rat heart was increased two- to three-fold by the presence of phosphatidylethanolamine (PE) or lysophosphatidylethanolamine (LPE). This stimulatory effect also could be obtained in assays with particulate and soluble subcellular fractions and was observed with two different methods of preparing triolein substrate emulsions. Ethanolamine and glycerophosphorylethanolamine had no effect on hydrolase activity, whereas phosphatidylcholine (PC) and acidic phospholipids such as cardiolipin were inhibitory. Palmitic acid, palmityl CoA and palmityl carnitine inhibited PE-stimulated hydrolase activity, but ethyl esters of palmitate had no effect. The preparation of acetone-ether powders resulted in a marked reduction of triacylglycerol hydrolase activity, but PE and LPE now stimulated hydrolase activity by ten-fold or greater, suggesting that these phospholipids may have an obligatory role in modulating triacylglycerol hydrolase activity. Triton X-100 also stimulated hydrolase activity in acetone-ether powders.
D000818:Animals; D002250:Carbon Radioisotopes; D007700:Kinetics; D008049:Lipase / Q000302:isolation & purification / Q000378:metabolism*; D008246:Lysophospholipids; D009206:Myocardium / Q000201:enzymology*; D010714:Phosphatidylethanolamines / Q000494:pharmacology*; D051381:Rats; D014304:Triolein
D002250:Carbon Radioisotopes; D008246:Lysophospholipids; D010714:Phosphatidylethanolamines; C008301:lysophosphatidylethanolamine; D014304:Triolein; D008049:Lipase