Abstract
PHOSPHOCHOLINE-containing phospholipids, particularly phosphatidylcholine (lecithin), lysophosphatidylcholine and sphingomyelin, have integral roles in the structure and function of mammalian cell membranes1. Enzymatic digestion of platelet choline phosphatides, particularly of phosphatidylcholine which is the most abundant of the platelet phospholipids2,3, has been shown to induce platelet release reactions4. We have demonstrated that C-reactive protein (CRP), an acute phase reactant with binding specificities for phosphocholine, choline phosphatides and polycations generally5–8, can inhibit multiple platelet reactivities9,10. These considerations have raised the possibility that molecules generally with binding specificities for choline phosphatides can influence platelet responsiveness. We report here an investigation of the ability of the T-15 anti-phosphocholine mouse IgA myeloma protein to inhibit the aggregating response of human platelets.
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FIEDEL, B., OSMAND, A. & GEWURZ, H. Inhibition of platelet aggregation by a myeloma protein with anti-phosphocholine specificity. Nature 263, 687–689 (1976). https://doi.org/10.1038/263687a0
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DOI: https://doi.org/10.1038/263687a0
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