Molecular heterogeneity of platelet-activating factor produced by stimulated human polymorphonuclear leukocytes.
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.
D000595:Amino Acid Sequence; D000818:Animals; D002474:Cell-Free System; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D006801:Humans; D013058:Mass Spectrometry; D009504:Neutrophils / Q000378:metabolism*; D010972:Platelet Activating Factor / Q000096:biosynthesis / Q000302:isolation & purification*; D011817:Rabbits; D013045:Species Specificity; D013329:Structure-Activity Relationship
D010972:Platelet Activating Factor