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Gene Review

F12  -  coagulation factor XII (Hageman factor)

Homo sapiens

Synonyms: Coagulation factor XII, HAE3, HAEX, HAF, Hageman factor
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Disease relevance of F12

  • Association after linkage analysis indicates that homozygosity for the 46C-->T polymorphism in the F12 gene is a genetic risk factor for venous thrombosis [1].
  • In a family-based study called GAIT (Genetic Analysis of Idiopathic Thrombophilia) that included a genome-wide scan we demonstrated that a polymorphism (46C-->T) in the F12 locus jointly influences variability of plasma (Factor XII) FXII levels and susceptibility to thrombotic disease [1].
  • Additionally, the proband and two of his children had decreased Hageman factor (factor XII) levels consistent with those of heterozygous carriers of Hageman trait [2].
  • Normal plasma arginine esterase and the Hageman factor (factor XII) -prekallikrein-kininogen system in cystic fibrosis [3].
  • From the viewpoint of fetal distress related disseminated intravascular coagulation (DIC), the Hageman Factor, kinin-kallikrein system were investigated and on the other hand the adaptation of the normal newborn to extrauterine life was also evaluated [4].
  • Homozygosity for the C46T polymorphism of the F12 gene is associated with venous thrombosis during the first pregnancy/puerperium in previously asymptomatic women [5].

Psychiatry related information on F12


High impact information on F12

  • The cysts were loaded with natural cyst fluid or with a combination of Dulbecco's modified Eagle's medium and Ham's F12 medium (DME-F12) and incubated in DME-F12 for 24 hours [7].
  • These data suggest that Hageman-factor fragments are potent hypotensive agents, presumably because they trigger the generation of bradykinin in recipients [8].
  • Hypotension associated with prekallikrein activator (Hageman-factor fragments) in plasma protein fraction [8].
  • A fragment of activated Hageman factor (HFf) has been demonstrated to activate the classical pathway of complement in a manner that is analogous to complement activation by antigen-antibody complexes or aggregated IgG [9].
  • By contrast, kinin generation and fibrinolysis resulting from the formation of kallikrein can be initiated either at the site of contact activation, by alpha-HFa action, or throughout the plasma, by beta-HFa; further dissemination of these activities is assured by the rapid dissociation of kallikrein itself from the surface [10].

Chemical compound and disease context of F12


Biological context of F12


Anatomical context of F12

  • Morphology in mixture of Ham's F12 and Dulbecco's modified Eagle's medium was slightly hyperplastic, and keratins 1 and 10 synthesis less co-ordinated than in supplemented keratinocyte defined medium, but a consistently inverted sequence of expression of keratins 1 and 10 was found in either medium [21].
  • Transmission electron microscopy showed that cultures of HUC grown entirely in serum-free F12 on collagen gel substrates morphologically differentiate postconfluence to resemble in some respects the stratified uroepithelium in vivo, although neither a basal lamina nor an asymmetric unit membrane develop [22].
  • Strain F12 was significantly more adherent to HeLa cells in a quantitative adherence assay than was its E. coli O157:H7 parent, but they did not differ in other phenotypes [23].
  • This serum-free medium, which was developed for the long-term cultivation of protease-dissociated HBE cells, consists of Ham's F12 nutrient medium supplemented with insulin, transferrin, epidermal growth factor, hydrocortisone, cholera toxin, and bovine hypothalamus extract [24].
  • An HUT-78 cell clone (F12) chronically infected by a nonproducer HIV-1 variant (Federico et al., (1989) AIDS Res. Hum. Retroviruses 5, 385-396) is fully resistant to superinfection with HIV-1 or HIV-2 [25].

Associations of F12 with chemical compounds

  • To investigate the earliest steps of the intrinsic clotting pathway, Hageman factor (Factor XII) was exposed to Sephadex gels to which ellagic acid had been adsorbed; Hageman factor was then separated from the gels and studied in the fluid phase [26].
  • The effect of C1 inhibitor upon Hageman factor autoactivation [27].
  • When Hageman factor was exposed to a negatively charged surface, provided by either a glass cuvette or dextran sulfate, the addition of C1 INH gave a dose-dependent inhibition of the activity observed [27].
  • Further, beta 2-glycoprotein inhibited the generation of amidolytic activity against H-D-prolyl-L-phenylalanyl-L-arginine p-nitroanilide dihydrochloride in mixtures of Hageman factor and ellagic acid [28].
  • The culture medium used (F12) was the standard Ham's F12 medium (0.3 mM calcium) supplemented with 1 microgram/ml hydrocortisone, 5 micrograms/ml transferrin, 10 micrograms/ml insulin, 0.1 mM nonessential amino acids, 2.0 mM L-glutamine, 2.7 mg/ml D-glucose, 10(-4) M ethanolamine or 10(-4) M phosphoethanolamine, and 5 X 10(-8) M selenium [22].

Physical interactions of F12


Regulatory relationships of F12


Other interactions of F12


Analytical, diagnostic and therapeutic context of F12


  1. Association after linkage analysis indicates that homozygosity for the 46C-->T polymorphism in the F12 gene is a genetic risk factor for venous thrombosis. Tirado, I., Soria, J.M., Mateo, J., Oliver, A., Souto, J.C., Santamaria, A., Felices, R., Borrell, M., Fontcuberta, J. Thromb. Haemost. (2004) [Pubmed]
  2. Plasma thromboplastin antecedent (Factor XI) deficiency in a black family. Niskanen, E.O., Saito, H., Cline, M.J. Arch. Intern. Med. (1981) [Pubmed]
  3. Normal plasma arginine esterase and the Hageman factor (factor XII) -prekallikrein-kininogen system in cystic fibrosis. Goldsmith, G.H., Stern, R.C., Saito, H., Ratnoff, O.D. J. Lab. Clin. Med. (1977) [Pubmed]
  4. A biochemical study on the kinetics of kininogen in asphyxiated newborn. Suzuki, S. Nippon Sanka Fujinka Gakkai Zasshi (1982) [Pubmed]
  5. Homozygosity for the C46T polymorphism of the F12 gene is a risk factor for venous thrombosis during the first pregnancy. Cochery-Nouvellon, E., Mercier, E., Lissalde-Lavigne, G., Daurès, J.P., Quéré, I., Dauzat, M., Marès, P., Gris, J.C. J. Thromb. Haemost. (2007) [Pubmed]
  6. Hageman factor and its binding sites are present in senile plaques of Alzheimer's disease. Yasuhara, O., Walker, D.G., McGeer, P.L. Brain Res. (1994) [Pubmed]
  7. The secretion of fluid by renal cysts from patients with autosomal dominant polycystic kidney disease. Ye, M., Grantham, J.J. N. Engl. J. Med. (1993) [Pubmed]
  8. Hypotension associated with prekallikrein activator (Hageman-factor fragments) in plasma protein fraction. Alving, B.M., Hojima, Y., Pisano, J.J., Mason, B.L., Buckingham, R.E., Mozen, M.M., Finlayson, J.S. N. Engl. J. Med. (1978) [Pubmed]
  9. Activation of the classical pathway of complement by Hageman factor fragment. Ghebrehiwet, B., Silverberg, M., Kaplan, A.P. J. Exp. Med. (1981) [Pubmed]
  10. Surface and fluid phase activities of two forms of activated Hageman factor produced during contact activation of plasma. Revak, S.D., Cochrane, C.G., Bouma, B.N., Griffin, J.H. J. Exp. Med. (1978) [Pubmed]
  11. Studies of C1 inactivator-plasma kallikrein complexes in purified systems and in plasma. Lewin, M.F., Kaplan, A.P., Harpel, P.C. J. Biol. Chem. (1983) [Pubmed]
  12. Bradykinin generation by dialysis membranes: possible role in anaphylactic reaction. Schulman, G., Hakim, R., Arias, R., Silverberg, M., Kaplan, A.P., Arbeit, L. J. Am. Soc. Nephrol. (1993) [Pubmed]
  13. Hyperprolactinemia and reduction in plasma titers of Hageman factor, prekallikrein, and high molecular weight kininogen in patients with acute myocardial infarction. La Follette, L., Gordon, E.M., Mazur, C.A., Ratnoff, O.D., Yamashita, T.S. J. Lab. Clin. Med. (1987) [Pubmed]
  14. Identification and purification of truncated insulin-like growth factor I from porcine uterus. Evidence for high biological potency. Ogasawara, M., Karey, K.P., Marquardt, H., Sirbasku, D.A. Biochemistry (1989) [Pubmed]
  15. A recombinant retrovirus carrying a non-producer human immunodeficiency virus (HIV) type 1 variant induces resistance to superinfecting HIV. Federico, M., Taddeo, B., Carlini, F., Nappi, F., Verani, P., Rossi, G.B. J. Gen. Virol. (1993) [Pubmed]
  16. Williams trait. Human kininogen deficiency with diminished levels of plasminogen proactivator and prekallikrein associated with abnormalities of the Hageman factor-dependent pathways. Colman, R.W., Bagdasarian, A., Talamo, R.C., Scott, C.F., Seavey, M., Guimaraes, J.A., Pierce, J.V., Kaplan, A.P. J. Clin. Invest. (1975) [Pubmed]
  17. Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor). McMullen, B.A., Fujikawa, K. J. Biol. Chem. (1985) [Pubmed]
  18. Kinin-generating cascade in advanced cancer patients and in vitro study. Matsumura, Y., Maruo, K., Kimura, M., Yamamoto, T., Konno, T., Maeda, H. Jpn. J. Cancer Res. (1991) [Pubmed]
  19. Severe Fletcher factor (plasma prekallikrein) deficiency with partial deficiency of Hageman factor (factor XII): report of a case with observation on in vivo and in vitro leukocyte chemotaxis. Poon, M.C., Moore, M.R., Castleberry, R.P., Lurie, A., Huang, S.T., Lehmeyer, J. Am. J. Hematol. (1982) [Pubmed]
  20. gag, vif, and nef genes contribute to the homologous viral interference induced by a nonproducer human immunodeficiency virus type 1 (HIV-1) variant: identification of novel HIV-1-inhibiting viral protein mutants. D'Aloja, P., Olivetta, E., Bona, R., Nappi, F., Pedacchia, D., Pugliese, K., Ferrari, G., Verani, P., Federico, M. J. Virol. (1998) [Pubmed]
  21. Organotypic keratinocyte cocultures in defined medium with regular epidermal morphogenesis and differentiation. Stark, H.J., Baur, M., Breitkreutz, D., Mirancea, N., Fusenig, N.E. J. Invest. Dermatol. (1999) [Pubmed]
  22. Growth kinetics and differentiation in vitro of normal human uroepithelial cells on collagen gel substrates in defined medium. Reznikoff, C.A., Loretz, L.J., Pesciotta, D.M., Oberley, T.D., Ignjatovic, M.M. J. Cell. Physiol. (1987) [Pubmed]
  23. Role of the Escherichia coli O157:H7 O side chain in adherence and analysis of an rfb locus. Bilge, S.S., Vary, J.C., Dowell, S.F., Tarr, P.I. Infect. Immun. (1996) [Pubmed]
  24. Effects of retinoids on human bronchial epithelial cells: differential regulation of hyaluronate synthesis and keratin protein synthesis. Wu, R., Wu, M.M. J. Cell. Physiol. (1986) [Pubmed]
  25. Homologous superinfection of both producer and nonproducer HIV-infected cells is blocked at a late retrotranscription step. Taddeo, B., Federico, M., Titti, F., Rossi, G.B., Verani, P. Virology (1993) [Pubmed]
  26. Interactions among Hageman factor, plasma prekallikrein, high molecular weight kininogen, and plasma thromboplastin antecedent. Ratnoff, O.D., Saito, H. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  27. The effect of C1 inhibitor upon Hageman factor autoactivation. Weiss, R., Silverberg, M., Kaplan, A.P. Blood (1986) [Pubmed]
  28. Inhibition of the activation of Hageman factor (factor XII) by beta 2-glycoprotein I. Henry, M.L., Everson, B., Ratnoff, O.D. J. Lab. Clin. Med. (1988) [Pubmed]
  29. Studies of binding of prekallikrein and Factor XI to high molecular weight kininogen and its light chain. Thompson, R.E., Mandle, R., Kaplan, A.P. Proc. Natl. Acad. Sci. U.S.A. (1979) [Pubmed]
  30. Immunofluorescence and immunoelectron microscopy analyses of a human monoclonal anti-epithelial cell surface antibody that recognizes a 185-kD polypeptide: a component of the paraneoplastic pemphigus antigen complex? Joly, P., Gilbert, D., Thomine, E., Delpech, A., Verdier, S., Lauret, P., Tron, F. J. Invest. Dermatol. (1993) [Pubmed]
  31. Activation and function of human Hageman factor. The role of high molecular weight kininogen and prekallikrein. Meier, H.L., Pierce, J.V., Colman, R.W., Kaplan, A.P. J. Clin. Invest. (1977) [Pubmed]
  32. Detection of activation of the contact system of coagulation in vitro and in vivo: quantitation of activated Hageman factor-C-1-inhibitor and kallikrein-C-1-inhibitor complexes by specific radioimmunoassays. Nuijens, J.H., Huijbregts, C.C., Cohen, M., Navis, G.O., de Vries, A., Eerenberg, A.J., Bakker, J.C., Hack, C.E. Thromb. Haemost. (1987) [Pubmed]
  33. Human epidermis reconstructed on synthetic membrane: influence of experimental conditions on terminal differentiation. Noël-Hudson, M.S., Dusser, I., Collober, I., Muriel, M.P., Bonté, F., Meybeck, A., Font, J., Wepierre, J. In Vitro Cell. Dev. Biol. Anim. (1995) [Pubmed]
  34. Inhibitory action of amyloid precursor protein against human Hageman factor (factor XII). Niwano, H., Embury, P.B., Greenberg, B.D., Ratnoff, O.D. J. Lab. Clin. Med. (1995) [Pubmed]
  35. Plasma prekallikrein: quantitative determination by direct activation with Hageman factor fragment (beta-XIIa). Alving, B.M., Tankersley, D.L., Mason, B.L. J. Lab. Clin. Med. (1983) [Pubmed]
  36. Rapid fibrinolysis, augmented Hageman factor (factor XII) titers, and decreased C1 esterase inhibitor titers in women taking oral contraceptives. Gordon, E.M., Ratnoff, O.D., Saito, H., Donaldson, V.H., Pensky, J., Jones, P.K. J. Lab. Clin. Med. (1980) [Pubmed]
  37. Activation of human plasma prekallikrein by Pseudomonas aeruginosa elastase in vitro. Shibuya, Y., Tanaka, H., Nishino, N., Okabe, H., Kambara, T., Yamamoto, T. Biochim. Biophys. Acta (1991) [Pubmed]
  38. Isolation and cultivation of human iris pigment epithelium. Hu, D.N., Ritch, R., McCormick, S.A., Pelton-Henrion, K. Invest. Ophthalmol. Vis. Sci. (1992) [Pubmed]
  39. 2,3,7,8-Tetrachlorodibenzo-p-dioxin alters embryonic palatal medial epithelial cell differentiation in vitro. Abbott, B.D., Diliberto, J.J., Birnbaum, L.S. Toxicol. Appl. Pharmacol. (1989) [Pubmed]
  40. Establishment and characterization of a cholangiocarcinoma cell line from a Thai patient with intrahepatic bile duct cancer. Sirisinha, S., Tengchaisri, T., Boonpucknavig, S., Prempracha, N., Ratanarapee, S., Pausawasdi, A. Asian Pac. J. Allergy Immunol. (1991) [Pubmed]
  41. Urinary excretion of Hageman factor (factor XII) and the presence of nonfunctional Hageman factor in the nephrotic syndrome. Saito, H., Goodnough, L.T., Makker, S.P., Kallen, R.J. Am. J. Med. (1981) [Pubmed]
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