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      Leukocyte accumulation promoting fibrin deposition is mediated in vivo by P-selectin on adherent platelets.

      Nature

      Animals, Antibodies, Monoclonal, Arteriovenous Shunt, Surgical, Blood Platelets, physiology, Cell Adhesion Molecules, Fibrin, metabolism, Humans, Kinetics, Leukemia, Promyelocytic, Acute, Leukocytes, Mice, Mice, Inbred BALB C, immunology, Microscopy, Electron, Scanning, P-Selectin, Papio, Platelet Adhesiveness, Platelet Membrane Glycoproteins, analysis, Polyethylene Terephthalates, Tumor Cells, Cultured

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          Abstract

          The glycoprotein P-selectin is a cell adhesion molecule of stimulated platelets and endothelial cells, which mediates the interaction of these cells with neutrophils and monocytes. It is a membrane component of cell storage granules, and is a member of the selectin family which includes E-selectin and L-selectin. P-selectin recognizes both lineage-specific carbohydrate ligands on monocytes and neutrophils, including the Lewis x antigen, sialic acid, and a protein component. In inflammation and thrombosis, P-selectin may mediate the interaction of leukocytes with platelets bound in the region of tissue injury and with stimulated endothelium. To evaluate the role of P-selectin in platelet-leukocyte adhesion in vivo, the accumulation of leukocytes within an experimental thrombus was explored in an arteriovenous shunt model in baboons. A Dacron graft implanted within an arteriovenous shunt is thrombogenic, accumulating platelets and fibrin within its lumen. These bound platelets express P-selectin. Here we show that antibody inhibition of leukocyte binding to P-selectin expressed on platelets immobilized on the graft blocks leukocyte accumulation and inhibits the deposition of fibrin within the thrombus. These results indicate that P-selectin is an important adhesion molecule on platelets, mediating platelet-leukocyte binding in vivo, that the presence of leukocytes in thrombi is mediated by P-selectin, and that these leukocytes promote fibrin deposition.

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          Journal
          1279433
          10.1038/359848a0

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