Quantitative analysis of lysophosphatidic acid by time-of-flight mass spectrometry using a phosphate-capture molecule

Lysophosphatidic acid (LPA) is a lipid mediator that may play an important role in wound healing, embryonic development, and progression of cancer. Here, we report a procedure for the quantification of LPA by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The method is...

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Bibliographic Details
Main Authors: Tamotsu Tanaka, Hideki Tsutsui, Kaoru Hirano, Tohru Koike, Akira Tokumura, Kiyoshi Satouchi
Format: Article
Language:English
Published: Elsevier 2004-11-01
Series:Journal of Lipid Research
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Online Access:http://www.sciencedirect.com/science/article/pii/S0022227520341468
Description
Summary:Lysophosphatidic acid (LPA) is a lipid mediator that may play an important role in wound healing, embryonic development, and progression of cancer. Here, we report a procedure for the quantification of LPA by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The method is based on a characteristic mass shift with total charge change (from –2 to +1) of the phosphate species due to 1:1 complexation of LPA2− with a dinuclear zinc (II) complex {1,3-bis[bis(pyridin-2-ylmethyl)amino]propan-2-olato dizinc(II) complex; Zn2L3+} at physiological pH. The monocationic complex [LPA2−-Zn2L3+]+ was detected in the positive mode, in which no other signal of cation adducts of LPA2− was observed. The detection limit of 18:1 LPA by this method was 0.1 pmol on a sample plate. The intensity ratio of [LPA2−-Zn2L3+]+ against an internal standard [17:0 LPA2−-Zn2L3+]+ increased linearly with their molar ratio. Based on the relative intensities of complex ions, we determined the amounts of LPA homologs in an egg white by this method; the results obtained were in good agreement with those by gas liquid chromatography.This sensitive and convenient procedure for LPA-specific detection is useful for the quantification of LPA homologs occurring in biological materials.
ISSN:0022-2275