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Receptor koagulacionog faktora II‎‎
Identifikatori
Simboli	F2R; CF2R; HTR; PAR1; TR
Vanjski ID	OMIM: 187930 MGI: 101802 HomoloGene: 1510 IUPHAR: PAR1 GeneCards: F2R Gene
Ontologija gena
Molekularna funkcija	• rodopsinu-slična receptorska aktivnost; • receptorska aktivnost; • receptorsko vezivanje; • aktivnost trombinskog receptora;
Celularna komponenta	• Goldžijev aparat; • membrana plazme; • integralno sa membranom plazme;
Biološki proces	• regulacija progresa ćelijskog ciklusa; • apoptoza; • aktivacija kaspaze; • ćelijska motilnost; • prenos signala; • signalni put G-protein spregnutog receptora; • tirozinska fosforilacija STAT proteina; • STAT proteinska jezgrena translokacija; • razvoj multićelijskih organizama; • koagulacija krvi; • respons na ranjavanje; • anatomska strukturna morfogeneza; • pozitivna regulacija I-kapaB kinaze/NF-kapaB kaskade;
Pregled RNK izražavanja
	podaci
Ortolozi

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Receptor koagulacionog faktora II, ili proteazom-aktivirani receptor‎‎ 1 (PAR1), je protein koji kod ljudi kodira F2R gen.^[1] PAR1 je G protein-spregnuti receptor koji učestvuje u regulaciji trombotskog responsa. Proteolitičko odsecanje dovodi do aktivacije receptora.^[2]

Ligandi

Nekoliko selektivnih antagonista PAR1 receptora je poznato. Oni se koriste kao antizgrušavajuća sredstva u lečenju bolesti srca.

SCH-530348

Povezano

Proteazom-aktivirani receptor‎‎

Literatura

↑ 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.
↑ „Entrez Gene: F2R coagulation factor II (thrombin) receptor”.

Dodatna literatura

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. DOI:10.1172/JCI115592. PMC 442859. 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/BST0300211. 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. DOI:10.1016/0092-8674(91)90261-V. 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. DOI:10.1021/bi00177a018. 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. DOI:10.1073/pnas.91.2.504. PMC 42977. PMID 8290554.
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. DOI:10.1074/jbc.271.16.9809. 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. DOI:10.1074/jbc.271.42.26320. 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. DOI:10.1074/jbc.271.51.32874. 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. DOI:10.1016/S0014-2999(96)00653-X. 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. DOI:10.1074/jbc.272.9.6011. 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.

[pmid8395910-1] 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.

[entrez-2] „Entrez Gene: F2R coagulation factor II (thrombin) receptor”.

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