P-selectin

Selectin P (granule membrane protein 140kDa, antigen CD62)
PDB rendering based on pdb 1gsr.
Available structures: 1fsb, 1g1q, 1g1r, 1g1s
Identifiers
Symbols	SELP; CD62; CD62P; FLJ45155; GMP140; GRMP; PADGEM; PSEL
External IDs	OMIM: 173610 MGI: 98280 HomoloGene: 2260
Gene ontology Molecular function: • protein binding • sugar binding Cellular component: • membrane fraction • soluble fraction • plasma membrane • integral to plasma membrane • membrane • integral to membrane • platelet alpha granule membrane Biological process: • inflammatory response • cell adhesion
RNA expression pattern
More reference expression data
Orthologs
	Human	Mouse
Entrez	6403	20344
Ensembl	ENSG00000174175	ENSMUSG00000026580
Uniprot	P16109	Q32MF1
Refseq	NM_003005 (mRNA) NP_002996 (protein)	XM_982736 (mRNA) XP_987830 (protein)
Location	Chr 1: 167.82 - 167.87 Mb	Chr 1: 165.96 - 165.99 Mb
Pubmed search	[1]	[2]

P-selectin is 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 Weibel-Palade bodies, and α-granules in unactivated platelets.

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 shown to be found in endothelial cells in 1989.

Function

P-selectin plays an essential role in the initial recruitment of leukocytes (white blood cells) to the site of injury during inflammation. When endothelial cells are activated by molecules such as histamine or thrombin during inflammation, P-selectin moves from an internal cell location to the endothelial cell surface.

Thrombin is one trigger which can stimulate endothelial-cell release of P-selectin and recent studies suggest an additional Ca2+-independent pathway involved in release of P-selectin. ^[1]

Ligands for P-selectin on eosinophils and neutrophils are similar sialylated, protease-sensitive, endo-beta-galactosidase-resistant structures, clearly different than those reported for E-selectin, and suggest disparate roles for P-selectin and E-selectin during recruitment during inflammatory responses. ^[2]

P-selectin attaches to the actin cytoskeleton through anchor proteins that are still poorly characterized.

See also

• Selectin

Footnotes

Further reading

v • d • e PDB Gallery 1fsb: STRUCTURE OF THE EGF DOMAIN OF P-SELECTIN, NMR, 19 STRUCTURES   1g1q: Crystal structure of P-selectin lectin/EGF domains   1g1r: Crystal structure of P-selectin lectin/EGF domains complexed with SLeX   1g1s: P-SELECTIN LECTIN/EGF DOMAINS COMPLEXED WITH PSGL-1 PEPTIDE

External links

• MeSH P-Selectin