A simple and highly sensitive radioenzymatic assay for lysophosphatidic acid quantification

• Main Authors: Jean Sébastien Saulnier-Blache, Alexia Girard, Marie-Françoise Simon, Max Lafontan, Philippe Valet
• Format: Article
• Language: English
• Published: Elsevier 2000-12-01
• Series: Journal of Lipid Research
• Subjects: radioenzymatic detection; lysophosphatidic acid acyltransferase; phosphatidic acid; serum; plasma; [14C]oleoyl-CoA
• Online Access: http://www.sciencedirect.com/science/article/pii/S0022227520323555
• ISSN: 0022-2275

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.