Molecular heterogeneity of platelet-activating factor produced by stimulated human polymorphonuclear leukocytes

R. Neal Pinckard; Evelyn M. Jackson; Carol Hoppens; Susan T. Weintraub; Janet C. Ludwig; Linda M. McManus; Glen E. Mott

doi:10.1016/0006-291X(84)90478-9

Molecular heterogeneity of platelet-activating factor produced by stimulated human polymorphonuclear leukocytes

R. Neal Pinckard, Evelyn M. Jackson, Carol Hoppens, Susan T. Weintraub, Janet C. Ludwig, Linda M. McManus, Glen E. Mott

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Abstract

The molecular heterogeneity of platelet-activating factor (PAF) produced by stimulated human neutrophilic polymorphonuclear leukocytes (PMN) was assessed by both normal and reverse phase high performance liquid chromatography (HPLC). As detected by rabbit platelet stimulation, at least 5 PAF molecules were separated by HPLC. Fast atom bombardment (FAB) mass spectrometry revealed one of these PAFs was acetyl glyceryl ether phosphorylcholine (AGEPC) with a C_16:0 alkyl chain in the sn-1 position. Although the structures of the remaining PAFs are unknown, two of the peaks of PAF activity had the same retention times on reverse phase HPLC as the C₁₅- and C₁₈-saturated alkyl chain AGEPC homologues. These studies indicate that the human PMN produces multiple molecular species of PAF.

Original language	English (US)
Pages (from-to)	325-332
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	122
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(84)90478-9
State	Published - Jul 18 1984

ASJC Scopus subject areas

Molecular Biology
Biophysics
Biochemistry
Cell Biology

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title = "Molecular heterogeneity of platelet-activating factor produced by stimulated human polymorphonuclear leukocytes",

abstract = "The molecular heterogeneity of platelet-activating factor (PAF) produced by stimulated human neutrophilic polymorphonuclear leukocytes (PMN) was assessed by both normal and reverse phase high performance liquid chromatography (HPLC). As detected by rabbit platelet stimulation, at least 5 PAF molecules were separated by HPLC. Fast atom bombardment (FAB) mass spectrometry revealed one of these PAFs was acetyl glyceryl ether phosphorylcholine (AGEPC) with a C16:0 alkyl chain in the sn-1 position. Although the structures of the remaining PAFs are unknown, two of the peaks of PAF activity had the same retention times on reverse phase HPLC as the C15- and C18-saturated alkyl chain AGEPC homologues. These studies indicate that the human PMN produces multiple molecular species of PAF.",

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T1 - Molecular heterogeneity of platelet-activating factor produced by stimulated human polymorphonuclear leukocytes

AU - Pinckard, R. Neal

AU - Jackson, Evelyn M.

AU - Hoppens, Carol

AU - Weintraub, Susan T.

AU - Ludwig, Janet C.

AU - McManus, Linda M.

AU - Mott, Glen E.

N1 - Funding Information: Castillo, Pat Padilla, and Laida Garcia part by USPHS Grant

PY - 1984/7/18

Y1 - 1984/7/18

N2 - The molecular heterogeneity of platelet-activating factor (PAF) produced by stimulated human neutrophilic polymorphonuclear leukocytes (PMN) was assessed by both normal and reverse phase high performance liquid chromatography (HPLC). As detected by rabbit platelet stimulation, at least 5 PAF molecules were separated by HPLC. Fast atom bombardment (FAB) mass spectrometry revealed one of these PAFs was acetyl glyceryl ether phosphorylcholine (AGEPC) with a C16:0 alkyl chain in the sn-1 position. Although the structures of the remaining PAFs are unknown, two of the peaks of PAF activity had the same retention times on reverse phase HPLC as the C15- and C18-saturated alkyl chain AGEPC homologues. These studies indicate that the human PMN produces multiple molecular species of PAF.

AB - The molecular heterogeneity of platelet-activating factor (PAF) produced by stimulated human neutrophilic polymorphonuclear leukocytes (PMN) was assessed by both normal and reverse phase high performance liquid chromatography (HPLC). As detected by rabbit platelet stimulation, at least 5 PAF molecules were separated by HPLC. Fast atom bombardment (FAB) mass spectrometry revealed one of these PAFs was acetyl glyceryl ether phosphorylcholine (AGEPC) with a C16:0 alkyl chain in the sn-1 position. Although the structures of the remaining PAFs are unknown, two of the peaks of PAF activity had the same retention times on reverse phase HPLC as the C15- and C18-saturated alkyl chain AGEPC homologues. These studies indicate that the human PMN produces multiple molecular species of PAF.

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Molecular heterogeneity of platelet-activating factor produced by stimulated human polymorphonuclear leukocytes

Abstract

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