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P-selectin: Wikis

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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 OMIM173610 MGI98280 HomoloGene2260 GeneCards: SELP Gene
RNA expression pattern
PBB GE SELP 206049 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 6403 20344
Ensembl ENSG00000174175 ENSMUSG00000026580
UniProt P16109 Q32MF1
RefSeq (mRNA) NM_003005 XM_982736
RefSeq (protein) NP_002996 XP_987830
Location (UCSC) 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.

Contents

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

Footnotes

Further reading

  • Ryan US, Worthington RE (1992). "Cell-cell contact mechanisms.". Curr. Opin. Immunol. 4 (1): 33–7. doi:10.1016/0952-7915(92)90120-4. PMID 1375831.  
  • Bajorath J, Stenkamp R, Aruffo A (1994). "Knowledge-based model building of proteins: concepts and examples.". Protein Sci. 2 (11): 1798–810. doi:10.1002/pro.5560021103. PMID 7505680.  
  • Varki NM, Varki A (2002). "Heparin inhibition of selectin-mediated interactions during the hematogenous phase of carcinoma metastasis: rationale for clinical studies in humans.". Semin. Thromb. Hemost. 28 (1): 53–66. doi:10.1055/s-2002-20564. PMID 11885026.  
  • Furie B, Furie BC (2004). "Role of platelet P-selectin and microparticle PSGL-1 in thrombus formation.". Trends in molecular medicine 10 (4): 171–8. doi:10.1016/j.molmed.2004.02.008. PMID 15059608.  
  • Cambien B, Wagner DD (2004). "A new role in hemostasis for the adhesion receptor P-selectin.". Trends in molecular medicine 10 (4): 179–86. doi:10.1016/j.molmed.2004.02.007. PMID 15059609.  
  • Chen M, Geng JG (2006). "P-selectin mediates adhesion of leukocytes, platelets, and cancer cells in inflammation, thrombosis, and cancer growth and metastasis.". Arch. Immunol. Ther. Exp. (Warsz.) 54 (2): 75–84. doi:10.1007/s00005-006-0010-6. PMID 16648968.  

External links

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