Phospholipid methylation in myogenic cells

Thomas K. Koch; Adrienne S. Gordon; Ivan Diamond

doi:10.1016/0006-291X(83)91633-9

Phospholipid methylation in myogenic cells

Thomas K. Koch, Adrienne S. Gordon, Ivan Diamond

Research output: Contribution to journal › Article › peer-review

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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 β -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 β -adrenergic simulation of adenylate cyclase no alteration in the transmethylation pathway could be demonstrated.

Original language	English (US)
Pages (from-to)	339-347
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	114
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(83)91633-9
State	Published - Jul 18 1983
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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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 β -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 β -adrenergic simulation of adenylate cyclase no alteration in the transmethylation pathway could be demonstrated.",

author = "Koch, {Thomas K.} and Gordon, {Adrienne S.} and Ivan Diamond",

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AU - Gordon, Adrienne S.

AU - Diamond, Ivan

PY - 1983/7/18

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N2 - 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 β -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 β -adrenergic simulation of adenylate cyclase no alteration in the transmethylation pathway could be demonstrated.

AB - 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 β -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 β -adrenergic simulation of adenylate cyclase no alteration in the transmethylation pathway could be demonstrated.

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Phospholipid methylation in myogenic cells

Abstract

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