Phospholipid methylation in myogenic cells.
The biosynthesis of phosphatidylcholine from successive N-methylation of phosphatidylethanolamine has been implicated as a major mechanism for the transduction of several receptor-mediated signals including beta-adrenergic coupling to adenylate cyclase. In this report we demonstrate L-isoproterenol stimulation of adenylate cyclase activity in two myogenic cell lines, L8 and BC3H-1. Using a sensitive high performance liquid chromatography method for qualitative and quantitative determination of phospholipids we found an active membrane phospholipid methylation pathway in these cells. Despite beta-adrenergic simulation of adenylate cyclase no alteration in the transmethylation pathway could be demonstrated.
D000262:Adenylyl Cyclases / Q000378:metabolism; D000818:Animals; D002460:Cell Line; D002999:Clone Cells; D007545:Isoproterenol / Q000494:pharmacology; D007700:Kinetics; D008563:Membrane Lipids / Q000378:metabolism*; D051379:Mice; D009132:Muscles / Q000187:drug effects / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism*; D012436:S-Adenosylmethionine / Q000378:metabolism
D008563:Membrane Lipids; D010743:Phospholipids; D012436:S-Adenosylmethionine; D000262:Adenylyl Cyclases; D007545:Isoproterenol