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A more recent version of this article appeared on May 1, 2005

Papers In Press, published online ahead of print February 16, 2005
J. Lipid Res., doi:10.1194/jlr.M500014-JLR200
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Submitted on January 12, 2005
Revised on February 14, 2005
Accepted on February 14, 2005

Analysis of cell membrane aminophospholipids as isotope-tagged derivatives

Karin A. Zemski Berry and Robert C. Murphy

Department of Pharmacology, University of Colorado Health Sciences Center, Aurora, CO 80045-0511

Corresponding Author: robert.murphy{at}uchsc.edu

Glycerophosphoethanolamine (GPEtn) and glycerophosphoserine (GPSer) lipids were reacted with a multiplexed set of differentially isotopically enriched N-methylpiperazine acetic acid NHS (N-hydroxysuccinimide) ester reagents, which place isobaric mass labels at a primary amino group. The resulting derivatized aminophospholipids were isobaric and chromatographically indistinguishable, but yielded positive reporter ions (m/z 114 or 117) after collisional activation that could be used to identify and quantify individual members of the multiplex set. The chromatographic and mass spectrometric response of N-methylpiperazine amide tagged aminophospholipids was probed using phosphoethanolamine and phosphoserine standards. The [M+H]+ of each tagged aminophospholipid shifted 144 Da and during collision-induced dissociation the major fragmentation ion was either m/z 114 or 117. This mode of detecting aminophospholipids was useful for an unbiased analysis of plasmalogen GPEtn lipids. Molecular species information as to the esterified fatty acyl substituents was obtained by collisional activation of the [M-H]¯ ions. The isotope tagged reagents were used to assess the changes in the distribution of GPEtn lipids after exposure of liposomes made from phospholipids extracted from RAW 264.7 cells to Cu2+/H2O2 in order to illustrate the ability of these reagents to aid in the mass spectrometric identification of aminophospholipid changes that occur during biological stimuli.


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