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Correspondence to:
Jean Sébastien Saulnier-Blache
The objective of the present work was to develop a simple and sensitive radioenzymatic assay to quantify lysophosphatidic acid (LPA). For that, a recombinant rat LPA acid acyltransferase (LPAAT) produced in Escherichia coli was used. In the presence of [14C]oleoyl-CoA, LPAAT selectively catalyzes the transformation of LPA and alkyl-LPA into [14C]phosphatidic acid. Acylation of LPA was complete and linear from 0 to 200 pmol with a minimal detection of 0.2 pmol. This method was used to quantify LPA in butanol-extracted lipids from bovine sera, as well as from human and mouse plasma.
This radioenzymatic assay represents a new, simple, and highly sensitive method to quantify LPA in various biological fluids. — Saulnier-Blache, J. S., A. Girard, M-F. Simon, M. Lafontan, and P. Valet. A simple and highly sensitive radioenzymatic assay for lysophosphatidic acid quantification. J. Lipid Res. 2000. 41: 1947;–1951.
Supplementary key words:
radioenzymatic detection, lysophosphatidic acid acyltransferase, phosphatidic acid, serum, plasma, [14C]oleoyl-CoA, butanol, recombinant protein, Escherichia coli, bioactive phospholipid, thin-layer chromatography
Copyright © 2000 by Lipid Research, Inc.
Original Article
A simple and highly sensitive radioenzymatic assay for lysophosphatidic acid quantification
Jean Sébastien Saulnier-Blachea,
Alexia Girarda,
Marie-Françoise Simona,
Max Lafontana, and
Philippe Valeta
a INSERM U317, Institut Louis Bugnard, Université Paul Sabatier, CHU Rangueil, 31403 Toulouse, Cedex 04, France
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