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Gene Review

F2  -  coagulation factor II (thrombin)

Homo sapiens

Synonyms: Coagulation factor II, PT, Prothrombin, RPRGL2, THPH1
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Disease relevance of F2


High impact information on F2

  • Enhanced mRNA 3' end formation efficiency emerges as a novel principle causing a genetic disorder and explains the role of the F2 20210 G-->A mutation in the pathogenesis of thrombophilia [6].
  • gamma-Carboxyglutamic acid residues on prothrombin are synthesized from glutamic acid on a prothrombin precursor in the liver through a vitamin K-dependent carboxylase [7].
  • There were higher levels of F2 mRNA (encoding prothrombin) as well as prothrombin and thrombin protein in liver of C3-/- mice compared to C3+/+ mice [8].
  • Prostaglandins A1, A2, B1, B2, E2, F2 alpha, 6-keto-prostaglandin F1 alpha, and thromboxane B2, which do not affect platelet cyclic AMP level, did not stimulate the protease [9].
  • These data suggest that reduced synthesis as well as impaired carboxylation of prothrombin precursor protein are factors contributing to the coagulopathy in patients with moderate to severe liver disease and that measurement of circulating levels of II-Ag may provide an excellent indication of hepatic synthetic capacity [10].

Biological context of F2

  • F2 20221(*)T thus represents the first example of a likely pathologically relevant mutation of the putative CstF binding site in the 3'flanking sequence of a human gene [11].
  • Kringle F2 binds to thrombin at the heparin binding site through charge complementarity; a conformational change appears to occur on binding [12].
  • In addition, the cDNA probe for F2 recognizes a homologous sequence which has been tentatively mapped to the X chromosome [13].
  • Knocking out the PB1-F2 protein had no effect on viral replication in tissue culture but diminished virus pathogenicity and mortality in mice [1].
  • The influenza virus PB1-F2 protein is a novel protein previously shown to be involved in induction of cell death [1].

Anatomical context of F2


Associations of F2 with chemical compounds

  • Finally, we show that the low-efficiency F2 cleavage and CstF binding sites are balanced by a stimulatory upstream uridine-rich element in the 3'UTR [11].
  • PA (after stimulation with ADP), P-selectin expression and fibrinogen binding to glycoprotein (GP) IIb/IIIa (determined by flow cytometry with and without stimulation with ADP), and levels of soluble P-selectin, prothrombin fragments F1 and F2, thrombin-antithrombin complexes (TAT), and antithrombin III (ATIII) were determined [18].
  • This serine protease was detected by measuring the concentrations of activation fragments (F2/F1+2) cleaved from prothrombin [19].
  • The immunologic expression of this area is unaffected by denaturation or reduction-alkylation of F2 as well as by attachment of polypeptide to the NH2-terminal of this component [20].
  • Acclimation of wild type and the chlorina F2 mutant of barley to either high light or low temperature results in a 2- to 3-fold increase in non-photochemical quenching which occurred independently of either energy-dependent quenching (qE), xanthophyll cycle-mediated antenna quenching or state transitions [21].

Physical interactions of F2

  • Monoclonal antibodies against F2 are superior to F4 or F1 antibodies as inhibitors of HK binding to FXI [22].

Other interactions of F2

  • A chimeric FXI molecule in which F2 is replaced by P2 is cleaved within P2 during activation by factor XIIa, resulting in greatly reduced HK binding capacity [22].
  • The order of affinity from highest to lowest is F2 F4 > F1 F3 [22].
  • We successfully applied SNPicker in designing endonuclease restriction assays for 14 SNPs for the MTHFR gene, the Coagulation Factor II gene and the Coagulation Factor V gene [23].
  • FMF (MEFV), factor V (F5), and factor II (F2) genotypes identified using this improved system were totally concordant with results of other genotyping methods (denaturing gradient gel electrophoresis [DGGE], SSCP, and RFLP analysis) [24].
  • Fifteen men undergoing extracorporeal circulation for aorta-coronary bypass grafting were investigated for alterations of the plasma levels of cross-linked fibrin degradation products, protein C, free protein S, coagulation factor II, immunoglobulin G, and albumin [25].

Analytical, diagnostic and therapeutic context of F2


  1. Influenza A virus PB1-F2 protein contributes to viral pathogenesis in mice. Zamarin, D., Ortigoza, M.B., Palese, P. J. Virol. (2006) [Pubmed]
  2. Factor II G20210A and factor V G1691A gene mutations and peripheral arterial occlusive disease. Renner, W., Köppel, H., Brodmann, M., Pabst, E., Schallmoser, K., Toplak, H., Wascher, T.C., Pilger, E. Thromb. Haemost. (2000) [Pubmed]
  3. Prothrombin A19911G polymorphism and the risk of venous thromboembolism. Martinelli, I., Battaglioli, T., Tosetto, A., Legnani, C., Sottile, L., Ghiotto, R., Mannucci, P.M. J. Thromb. Haemost. (2006) [Pubmed]
  4. The association of prothrombin A19911G polymorphism with plasma prothrombin activity and venous thrombosis: results of the MEGA study, a large population-based case-control study. Chinthammitr, Y., Vos, H.L., Rosendaal, F.R., Doggen, C.J. J. Thromb. Haemost. (2006) [Pubmed]
  5. Type and location of venous thromboembolism in patients with factor V Leiden or prothrombin G20210A and in those with no thrombophilia. Martinelli, I., Battaglioli, T., Razzari, C., Mannucci, P.M. J. Thromb. Haemost. (2007) [Pubmed]
  6. Increased efficiency of mRNA 3' end formation: a new genetic mechanism contributing to hereditary thrombophilia. Gehring, N.H., Frede, U., Neu-Yilik, G., Hundsdoerfer, P., Vetter, B., Hentze, M.W., Kulozik, A.E. Nat. Genet. (2001) [Pubmed]
  7. Acquired vitamin K-dependent carboxylation deficiency in liver disease. Blanchard, R.A., Furie, B.C., Jorgensen, M., Kruger, S.F., Furie, B. N. Engl. J. Med. (1981) [Pubmed]
  8. Generation of C5a in the absence of C3: a new complement activation pathway. Huber-Lang, M., Sarma, J.V., Zetoune, F.S., Rittirsch, D., Neff, T.A., McGuire, S.R., Lambris, J.D., Warner, R.L., Flierl, M.A., Hoesel, L.M., Gebhard, F., Younger, J.G., Drouin, S.M., Wetsel, R.A., Ward, P.A. Nat. Med. (2006) [Pubmed]
  9. Prostacyclin stimulation of the activation of blood coagulation factor X by platelets. Dutta-Roy, A.K., Ray, T.K., Sinha, A.K. Science (1986) [Pubmed]
  10. Prothrombin antigen and coagulant activity in patients with liver disease. Corrigan, J.J., Jeter, M., Earnest, D.L. JAMA (1982) [Pubmed]
  11. The prothrombin 3'end formation signal reveals a unique architecture that is sensitive to thrombophilic gain-of-function mutations. Danckwardt, S., Gehring, N.H., Neu-Yilik, G., Hundsdoerfer, P., Pforsich, M., Frede, U., Hentze, M.W., Kulozik, A.E. Blood (2004) [Pubmed]
  12. A player of many parts: the spotlight falls on thrombin's structure. Stubbs, M.T., Bode, W. Thromb. Res. (1993) [Pubmed]
  13. Human genes encoding prothrombin and ceruloplasmin map to 11p11-q12 and 3q21-24, respectively. Royle, N.J., Irwin, D.M., Koschinsky, M.L., MacGillivray, R.T., Hamerton, J.L. Somat. Cell Mol. Genet. (1987) [Pubmed]
  14. Pericardial fluid from patients with unstable angina induces vascular endothelial cell apoptosis. Iwakura, A., Fujita, M., Hasegawa, K., Sawamura, T., Nohara, R., Sasayama, S., Komeda, M. J. Am. Coll. Cardiol. (2000) [Pubmed]
  15. Decreased protein C levels in patients with insulin-dependent type I diabetes mellitus. Vukovich, T.C., Schernthaner, G. Diabetes (1986) [Pubmed]
  16. Characterization of immobilized hepatocytes as liver support. Miura, Y., Akimoto, T., Yoshikawa, N., Yagi, K. Biomaterials, artificial cells, and artificial organs. (1990) [Pubmed]
  17. The PB1-F2 protein of Influenza A virus: increasing pathogenicity by disrupting alveolar macrophages. Coleman, J.R. Virol. J. (2007) [Pubmed]
  18. Platelet function during and after thrombolytic therapy for acute myocardial infarction with reteplase, alteplase, or streptokinase. Moser, M., Nordt, T., Peter, K., Ruef, J., Kohler, B., Schmittner, M., Smalling, R., Kübler, W., Bode, C. Circulation (1999) [Pubmed]
  19. Protection of factor Xa from neutralization by the heparin-antithrombin complex. Teitel, J.M., Rosenberg, R.D. J. Clin. Invest. (1983) [Pubmed]
  20. The isolation and characterization of a specific antibody population directed against the prothrombin activation fragments F2 and F1 + 2. Lau, H.K., Rosenberg, J.S., Beeler, D.L., Rosenberg, R.D. J. Biol. Chem. (1979) [Pubmed]
  21. Acclimation to temperature and irradiance modulates PSII charge recombination. Ivanov, A.G., Sane, P.V., Krol, M., Gray, G.R., Balseris, A., Savitch, L.V., Oquist, G., Hüner, N.P. FEBS Lett. (2006) [Pubmed]
  22. Characterization of the H-kininogen-binding site on factor XI: a comparison of factor XI and plasma prekallikrein. Renné, T., Gailani, D., Meijers, J.C., Müller-Esterl, W. J. Biol. Chem. (2002) [Pubmed]
  23. SNPicker: a graphical tool for primer picking in designing mutagenic endonuclease restriction assays. Niu, T., Hu, Z. Bioinformatics (2004) [Pubmed]
  24. An improved electronic microarray-based diagnostic assay for identification of MEFV mutations. Moutereau, S., Narwa, R., Matheron, C., Vongmany, N., Simon, E., Goossens, M. Hum. Mutat. (2004) [Pubmed]
  25. The protein C system in patients undergoing cardiopulmonary bypass. Knöbl, P.N., Zilla, P., Fasol, R., Müller, M.M., Vukovich, T.C. J. Thorac. Cardiovasc. Surg. (1987) [Pubmed]
  26. Guidance of anticoagulation after intracoronary implantation of Palmaz-Schatz stents by monitoring prothrombin and prothrombin fragment 1 + 2. Haude, M., Hafner, G., Jablonka, A., Rupprecht, H.J., Prellwitz, W., Meyer, J., Erbel, R. Am. Heart J. (1995) [Pubmed]
  27. Four-color multiplex 5' nuclease assay for the simultaneous detection of the factor V Leiden and the prothrombin G20210A mutations. Ugozzoli, L.A., Hamby, K. Mol. Cell. Probes (2004) [Pubmed]
  28. Measurement of immunoreactive prothrombin precursor and vitamin-K-dependent gamma-carboxylation in human hepatocellular carcinoma tissues: decreased carboxylation of prothrombin precursor as a cause of des-gamma-carboxyprothrombin synthesis. Ono, M., Ohta, H., Ohhira, M., Sekiya, C., Namiki, M. Tumour Biol. (1990) [Pubmed]
  29. Polymorphisms in the genes for coagulation factor II, V, VII in patients undergoing coronary angiography. Geng, X., Jin, G.D., Fu, G.S., Ji, M.A., Shan, J., Wang, J.A. J. Zhejiang Univ. Sci. (2003) [Pubmed]
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