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A more recent version of this article appeared on November 1, 2004

Papers In Press, published online ahead of print August 16, 2004
J. Lipid Res., doi:10.1194/jlr.D400010-JLR200
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Submitted on June 14, 2004
Revised on August 3, 2004
Accepted on August 7, 2004

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

Tamotsu Tanaka, Hideki Tsutsui, Kaoru Hirano, Tohru Koike, Akira Tokumura, and Kiyoshi Satouchi

Applied Biological Science, Fukuyama University, Fukuyama, Hiroshima 729-0292

Corresponding Author: tamot{at}fubac.fukuyama-u.ac.jp

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 (MALDI-TOF MS). The method is based on 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 positive mode, where 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 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 amounts of LPA homologues in an egg white by this method, and found that results obtained were in good agreement with those by gas-liquid chromatography. This sensitive and convenient procedure for LPA-specific detection is useful for quantification of LPA homologues occurring in biological materials.


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This article has been cited by other articles:


Home page
 Mol. Cell. ProteomicsHome page
E. Kinoshita, E. Kinoshita-Kikuta, K. Takiyama, and T. Koike
Phosphate-binding Tag, a New Tool to Visualize Phosphorylated Proteins
Mol. Cell. Proteomics, April 1, 2006; 5(4): 749 - 757.
[Abstract] [Full Text] [PDF]


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