P-selectin is a type-1 transmembrane protein that in humans is encoded by the SELP gene.[5]
P-selectin functions as a cell adhesion molecule (CAM) on the surfaces of activated endothelial cells, which line the inner surface of blood vessels, and activated platelets. In unactivated endothelial cells, it is stored in granules called Weibel-Palade bodies. In unactivated platelets P-selectin is stored in α-granules.
Other names for P-selectin include CD62P, Granule Membrane Protein 140 (GMP-140), and Platelet Activation-Dependent Granule to External Membrane Protein (PADGEM). It was first identified in endothelial cells in 1989.[6]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000174175 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026580 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Ryan US, Worthington RE (February 1992). "Cell-cell contact mechanisms". Current Opinion in Immunology. 4 (1): 33–37. doi:10.1016/0952-7915(92)90120-4. PMID 1375831.
- ^ McEver RP, Beckstead JH, Moore KL, Marshall-Carlson L, Bainton DF (July 1989). "GMP-140, a platelet alpha-granule membrane protein, is also synthesized by vascular endothelial cells and is localized in Weibel-Palade bodies". The Journal of Clinical Investigation. 84 (1): 92–99. doi:10.1172/JCI114175. PMC 303957. PMID 2472431.