Coagulation factor II receptor

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Coagulation factor II (thrombin) receptor
Identifiers
Symbols F2R ; CF2R; HTR; PAR1; TR
External IDs Template:OMIM5 Template:MGI HomoloGene1510
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Coagulation factor II (thrombin) receptor, also known as F2R or protease activated receptor 1 (PAR1) is a human gene.

Coagulation factor II receptor is a 7-transmembrane receptor involved in the regulation of thrombotic response. Proteolytic cleavage leads to the activation of the receptor. F2R is a G-protein coupled receptor family member.[1]

See also

References

  1. "Entrez Gene: F2R coagulation factor II (thrombin) receptor".

Further reading

  • Coughlin SR, Vu TK, Hung DT, Wheaton VI (1992). "Characterization of a functional thrombin receptor. Issues and opportunities". J. Clin. Invest. 89 (2): 351–5. PMID 1310691.
  • Howell DC, Laurent GJ, Chambers RC (2002). "Role of thrombin and its major cellular receptor, protease-activated receptor-1, in pulmonary fibrosis". Biochem. Soc. Trans. 30 (2): 211–6. doi:10.1042/ Check |doi= value (help). PMID 12023853.
  • Tellez C, Bar-Eli M (2003). "Role and regulation of the thrombin receptor (PAR-1) in human melanoma". Oncogene. 22 (20): 3130–7. doi:10.1038/sj.onc.1206453. PMID 12789289.
  • Remillard CV, Yuan JX (2005). "PGE2 and PAR-1 in pulmonary fibrosis: a case of biting the hand that feeds you?". Am. J. Physiol. Lung Cell Mol. Physiol. 288 (5): L789–92. doi:10.1152/ajplung.00016.2005. PMID 15821019.
  • Leger AJ, Covic L, Kuliopulos A (2006). "Protease-activated receptors in cardiovascular diseases". Circulation. 114 (10): 1070–7. doi:10.1161/CIRCULATIONAHA.105.574830. PMID 16952995.
  • Traynelis SF, Trejo J (2007). "Protease-activated receptor signaling: new roles and regulatory mechanisms". Curr. Opin. Hematol. 14 (3): 230–5. doi:10.1097/MOH.0b013e3280dce568. PMID 17414212.
  • Vu TK, Hung DT, Wheaton VI, Coughlin SR (1991). "Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation". Cell. 64 (6): 1057–68. PMID 1672265.
  • Wojtukiewicz MZ, Tang DG, Ben-Josef E; et al. (1995). "Solid tumor cells express functional "tethered ligand" thrombin receptor". Cancer Res. 55 (3): 698–704. PMID 7834643.
  • Hein L, Ishii K, Coughlin SR, Kobilka BK (1994). "Intracellular targeting and trafficking of thrombin receptors. A novel mechanism for resensitization of a G protein-coupled receptor". J. Biol. Chem. 269 (44): 27719–26. PMID 7961693.
  • Mathews II, Padmanabhan KP, Ganesh V; et al. (1994). "Crystallographic structures of thrombin complexed with thrombin receptor peptides: existence of expected and novel binding modes". Biochemistry. 33 (11): 3266–79. PMID 8136362.
  • Offermanns S, Laugwitz KL, Spicher K, Schultz G (1994). "G proteins of the G12 family are activated via thromboxane A2 and thrombin receptors in human platelets". Proc. Natl. Acad. Sci. U.S.A. 91 (2): 504–8. PMID 8290554.
  • Hoffman M, Church FC (1993). "Response of blood leukocytes to thrombin receptor peptides". J. Leukoc. Biol. 54 (2): 145–51. PMID 8395550.
  • Bahou WF, Nierman WC, Durkin AS; et al. (1993). "Chromosomal assignment of the human thrombin receptor gene: localization to region q13 of chromosome 5". Blood. 82 (5): 1532–7. PMID 8395910.
  • Schmidt VA, Vitale E, Bahou WF (1996). "Genomic cloning and characterization of the human thrombin receptor gene. Structural similarity to the proteinase activated receptor-2 gene". J. Biol. Chem. 271 (16): 9307–12. PMID 8621593.
  • Li F, Baykal D, Horaist C; et al. (1996). "Cloning and identification of regulatory sequences of the human thrombin receptor gene". J. Biol. Chem. 271 (42): 26320–8. PMID 8824285.
  • Shapiro MJ, Trejo J, Zeng D, Coughlin SR (1997). "Role of the thrombin receptor's cytoplasmic tail in intracellular trafficking. Distinct determinants for agonist-triggered versus tonic internalization and intracellular localization". J. Biol. Chem. 271 (51): 32874–80. PMID 8955127.
  • Ogino Y, Tanaka K, Shimizu N (1997). "Direct evidence for two distinct G proteins coupling with thrombin receptors in human neuroblastoma SH-EP cells". Eur. J. Pharmacol. 316 (1): 105–9. PMID 8982657.
  • Molino M, Bainton DF, Hoxie JA; et al. (1997). "Thrombin receptors on human platelets. Initial localization and subsequent redistribution during platelet activation". J. Biol. Chem. 272 (9): 6011–7. PMID 9038223.
  • Renesto P, Si-Tahar M, Moniatte M; et al. (1997). "Specific inhibition of thrombin-induced cell activation by the neutrophil proteinases elastase, cathepsin G, and proteinase 3: evidence for distinct cleavage sites within the aminoterminal domain of the thrombin receptor". Blood. 89 (6): 1944–53. PMID 9058715.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.