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Open Access Articles- Top Results for Coagulation factor II receptor

Coagulation factor II receptor

Template:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/rowTemplate:Infobox3cols/row
Identifiers
SymbolsF2R ; CF2R; HTR; PAR-1; PAR1; TR
External IDsOMIM187930 MGI101802 HomoloGene1510 IUPHAR: 347 ChEMBL: 3974 GeneCards: F2R Gene
RNA expression pattern
File:PBB GE F2R 203989 x at tn.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez214914062
EnsemblENSG00000181104ENSMUSG00000048376
UniProtP25116P30558
RefSeq (mRNA)NM_001992NM_010169
RefSeq (protein)NP_001983NP_034299
Location (UCSC)Chr 5:
76.01 – 76.03 Mb
Chr 13:
95.6 – 95.62 Mb
PubMed search[1][2]
"F2R" redirects here. For the Navy fighter, see Ryan XF2R Dark Shark.

Proteinase-activated receptor 1 (PAR1) also known as the coagulation factor II (thrombin) receptor is a protein that in humans is encoded by the F2R gene.[1] PAR1 is a G protein-coupled receptor involved in the regulation of thrombotic response. Proteolytic cleavage leads to the activation of the receptor.[2]

Ligands

Several selective antagonists for the PAR1 receptor have been developed, for use as anti-clotting agents for the treatment of heart disease.

See also

References

  1. ^ Bahou WF, Nierman WC, Durkin AS, Potter CL, Demetrick DJ (September 1993). "Chromosomal assignment of the human thrombin receptor gene: localization to region q13 of chromosome 5". Blood 82 (5): 1532–7. PMID 8395910. 
  2. ^ "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. PMC 442859. PMID 1310691. doi:10.1172/JCI115592. 
  • Wu H, Zhang Z, Li Y, Zhao R, Li H, Song Y, Qi J, Wang J. (2010). "Time course of upregulation of inflammatory mediators in the hemorrhagic brain in rats: correlation with brain edema". Neurochem Int. 57 (3): 248–53. PMID 20541575. doi:10.1016/j.neuint.2010.06.002. 
  • 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. PMID 12023853. doi:10.1042/BST0300211. 
  • Tellez C, Bar-Eli M (2003). "Role and regulation of the thrombin receptor (PAR-1) in human melanoma". Oncogene 22 (20): 3130–7. PMID 12789289. doi:10.1038/sj.onc.1206453. 
  • 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. PMID 15821019. doi:10.1152/ajplung.00016.2005. 
  • Leger AJ, Covic L, Kuliopulos A (2006). "Protease-activated receptors in cardiovascular diseases". Circulation 114 (10): 1070–7. PMID 16952995. doi:10.1161/CIRCULATIONAHA.105.574830. 
  • Traynelis SF, Trejo J (2007). "Protease-activated receptor signaling: new roles and regulatory mechanisms". Curr. Opin. Hematol. 14 (3): 230–5. PMID 17414212. doi:10.1097/MOH.0b013e3280dce568. 
  • 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. doi:10.1016/0092-8674(91)90261-V. 
  • 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. doi:10.1021/bi00177a018. 
  • 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. PMC 42977. PMID 8290554. doi:10.1073/pnas.91.2.504. 
  • Hoffman M, Church FC (1993). "Response of blood leukocytes to thrombin receptor peptides". J. Leukoc. Biol. 54 (2): 145–51. PMID 8395550. 
  • 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. doi:10.1074/jbc.271.16.9809. 
  • 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. doi:10.1074/jbc.271.42.26320. 
  • 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. doi:10.1074/jbc.271.51.32874. 
  • 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. doi:10.1016/S0014-2999(96)00653-X. 
  • 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. doi:10.1074/jbc.272.9.6011. 
  • 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. 
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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