Phospholipid methylation in myogenic cells

Biochem Biophys Res Commun. 1983 Jul 18;114(1):339-47. doi: 10.1016/0006-291x(83)91633-9.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenylyl Cyclases / metabolism
  • Animals
  • Cell Line
  • Clone Cells
  • Isoproterenol / pharmacology
  • Kinetics
  • Membrane Lipids / metabolism*
  • Mice
  • Muscles / drug effects
  • Muscles / metabolism*
  • Phospholipids / metabolism*
  • S-Adenosylmethionine / metabolism

Substances

  • Membrane Lipids
  • Phospholipids
  • S-Adenosylmethionine
  • Adenylyl Cyclases
  • Isoproterenol