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- W2003972235 abstract "P-selectin (CD62P, previously also known as GMP140 and PADGEM) is, alongside E-selectin (CD62E) and L-selectin (CD62L), a member of the selectin family of adhesion molecules, sharing common structural features but having different tissue distributions. It has a mass of approximately 140 kDa and is a protein rich in cysteine, containing several complex N-linked oligosaccharides chains. The extracellular domain is arranged as a lectin region (the amino-terminal of 120 amino acid residues), an epidermal growth factor-like region and nine discrete complement regulatory-like regions (each about 60 amino acid residues in length). In addition, there is a cross-membrane segment and an intracytoplasmic tail (Fig. 1). P-selectin is so named because it is a component of the cell membrane of the a granules of platelets, the organelle which stores coagulation-related substances such as b thromboglobulin and platelet factor 4. It is also a component of the membrane of the Weibel-Palade body (the endothelial cell specific organelle which stores von Willebrand factor) and is rapidly mobilised to the cell surface by various stimuli including inflammatory mediators [1–3]. The mucin-like glycoprotein ligand for P-selectin (PSGL-1) bears Oand N-linked carbohydrates, and is found on neutrophils, natural killer cells, monocytes and T-lymphocytes, giving rise to the hypothesis that it is involved in an interaction between these leukocytes and the endothelium, (possibly as part of the rolling/ binding/activation sequence), between platelets and neutrophils, and between platelets and the endothelium [4–8]." @default.
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- W2003972235 date "1997-02-01" @default.
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- W2003972235 title "Hypothesis: is soluble P-selectin a new marker of platelet activation?" @default.
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- W2003972235 doi "https://doi.org/10.1016/s0021-9150(96)05980-1" @default.
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