Modulation of acylglycerol synthetase activities of rat intestinal mucosa by homogenization and sonication.
Diacylglycerol and triacylglycerol synthesis was compared in intact villus cells and in their homogenates and sonicates using 2-monoacylglycerols and free fatty acids as substrates along with appropriate cofactors. It was found that simple pestle homogenization of cells led to an apparent loss of 80-90% in the triacylglycerol and 40-fold increase in the diacylglycerol synthetase activity. Sonication of the homogenate resulted in reestablishing the normal activity of cellular triacylglycerol synthesis (12 +/- 1 nmol . mg protein-1 . h-1) but the diacylglycerol biosynthesis further increased (to a maximum of 70 +/- 5 nmol . mg protein-1 . h-1). Preincubation with trypsin and postincubation treatment with pancreatic lipase indicated that different enzymes are involved in diacylglycerol and triacylglycerol biosynthesis from 2-monoacylglycerols and that these enzymes become segregated during homogenization. It is concluded that a triacylglycerol synthetase system utilizing 2-monoacylglycerols can be reassembled upon sonication.
D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D051048:Diacylglycerol O-Acyltransferase; D004075:Diglycerides / Q000096:biosynthesis; D005989:Glycerides / Q000378:metabolism; D007413:Intestinal Mucosa / Q000201:enzymology*; D008049:Lipase; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D013010:Sonication; D014280:Triglycerides / Q000096:biosynthesis; D014357:Trypsin
D004075:Diglycerides; D005989:Glycerides; D014280:Triglycerides; D000217:Acyltransferases; D051048:Diacylglycerol O-Acyltransferase; C021802:2-acylglycerol O-acyltransferase; D008049:Lipase; D014357:Trypsin