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Gene Review

F11  -  coagulation factor XI

Homo sapiens

Synonyms: Coagulation factor XI, FXI, PTA, Plasma thromboplastin antecedent
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Disease relevance of F11


Psychiatry related information on F11

  • Patients who achieved independent ambulation were significantly younger (P<.05), had better gait scores on admission (P<.05), and tended to be less severely injured-based on duration of posttraumatic amnesia (PTA; P=.058)-than those who did not ambulate independently [6].
  • CONCLUSIONS: These results should influence decision making in the management of claudication and it may be possible to prioritise PTA waiting lists to ensure patients with greatest potential benefit are treated with most urgency [7].
  • The earliest stage of recovery from moderate to severe closed head injury is a period of PTA that typically includes memory loss for events preceding and surrounding the injury and memory loss for events occurring since the injury [8].
  • In our induction and maintenance therapy group, 32 recipients (65%) underwent a simultaneous pancreas-kidney transplant (SPK), 8 (16%) a pancreas transplant alone (PTA), and 9 (19%) a pancreas after previous kidney transplant (PAK) [9].
  • GCS is used for classification by 60%, PTA 48%, retrograde amnesia by 50%, and LOC by 63% of institutions [10].

High impact information on F11

  • A neurite outgrowth-promoting activity of F11 characterized by in vitro culture of tectal cells is independent of F11-Ng-CAM and F11-RN binding [11].
  • F11 is a glycosyl phosphatidylinositol-anchored axonal surface glycoprotein belonging to a neural subgroup of the immunoglobulin superfamily [11].
  • In this report, we demonstrate that the F11 protein displays three distinguishable activities: binding to the cell recognition molecule Ng-CAM, interaction with the extracellular matrix glycoprotein restrictin (RN), and a neurite outgrowth-promoting activity [11].
  • The axonal recognition molecule F11 is a multifunctional protein: specific domains mediate interactions with Ng-CAM and restrictin [11].
  • By analyzing deletion mutants expressed in transfected COS cells, epitope mapping of monoclonal antibodies, and neurite outgrowth assays, we reveal that these activities can be localized to distinct regions within the F11 protein [11].

Chemical compound and disease context of F11


Biological context of F11

  • However, a synthetic glycoprotein Ibalpha peptide, Asp269-Asp287, containing a thrombin binding site had no effect on the binding of FXI to activated platelets [17].
  • Factor XI (FXI), the zymogen of the blood coagulation protease FXIa, and the structurally homologous protein plasma prekallikrein circulate in plasma in noncovalent complexes with H-kininogen (HK) [18].
  • Activation of factor XI (FXI) by thrombin on stimulated platelets plays a physiological role in hemostasis, providing additional thrombin generation required in cases of severe hemostatic challenge [19].
  • When normal plasma or plasma deficient in HF, PK, HMW-K or PTA was exposed to Sephadex-EA and was separated by centrifugation, each supernatant plasma except that deficient in HF shortened the prolonged partial thromboplastin time (PTT) of HF-deficient plasma [1].
  • Dinucleotide repeat polymorphism in the human coagulation factor XI gene, intron B (F11), detected using the polymerase chain reaction [20].

Anatomical context of F11

  • Thus, the inhibitor appeared to interfere with these clotting factor assays, possibly by inactivating PTA in the substrate plasmas in the test system [21].
  • By immunolocalization techniques, and using specific antibodies directed against the various contact factors, we now demonstrate that plasma prekallikrein (PK), factor XI (FXI), and factor XII (FXII) are present on the exterior face of the human neutrophil [22].
  • Single FXI mRNA species were identified by RT-PCR in platelet and bone marrow RNA, but not leukocyte RNA, that are the same size as the message from liver RNA [23].
  • Wild-type FXI mRNA was also identified in three leukemia cell lines with megakaryocyte features (MEG-01, HEL 92.1.7, and CHRF-288-11) [23].
  • Investigations determined the relative preference of prekallikrein (PK) or factor XI/XIa (FXI/FXIa) binding to endothelial cells (HUVECs) [24].

Associations of F11 with chemical compounds

  • Experiments with full-length recombinant FXI mutants show that, in the presence of Zn(2+), glycocalicin binds FXI at a heparin-binding site in A3 (Lys(252) and Lys(253)) and not by amino acids previously shown to be required for platelet binding (Ser(248), Arg(250), Lys(255), Phe(260), and Gln(263)) [25].
  • The platelet glycoprotein (GP) Ib-IX-V complex is the receptor for FXI [25].
  • Thus, we examined the effect of synthetic peptides of each of the seven leucine-rich repeats on the binding of 125I-FXI to activated platelets [17].
  • Using a collection of 53 thrombin mutants, we identified 16 mutants with <50% of the wild-type thrombin FXI-activating activity in the presence of dextran sulfate [19].
  • The FXI Apple 3 (A3) domain mediates binding to platelets in the presence of HK and zinc ions (Zn(2+)) or prothrombin and calcium ions [25].

Physical interactions of F11


Regulatory relationships of F11

  • All leucine-rich repeat (LRR) peptides derived from glycoprotein Ibalpha were able to inhibit FXI binding to activated platelets in the following order of decreasing potency: LRR7, LRR1, LRR4, LRR5, LRR6, LRR3, and LRR2 [17].
  • We have shown previously that F11 promotes neurite extension of chick tectal neurons by interaction with the tectal receptor NrCAM, a member of the L1 subgroup of the Ig superfamily [27].
  • Pituitary adenylate cyclase-activating peptide (PACAP) induces differentiation in the neuronal F11 cell line through a PKA-dependent pathway [28].
  • These results suggest that the molecular interactions of F11 might be regulated by the presence of tenascin-R and tenascin-C [29].
  • Functional interactions of the immunoglobulin superfamily member F11 are differentially regulated by the extracellular matrix proteins tenascin-R and tenascin-C [29].

Other interactions of F11


Analytical, diagnostic and therapeutic context of F11

  • Using surface plasmon resonance, we determined that FXI binds specifically to glycocalicin, the extracellular domain of GPIbalpha, in a Zn(2+)-dependent fashion (K(d) = approximately 52 nM) [25].
  • We mapped the KLK3 gene and the marker KLK3c to the long arm of human chromosome 4 between F11 and D4S426 using a radiation hybrid panel [33].
  • A good correlation (correlation coefficient 0.68) existed between the PTA procoagulant assays and radioimmunoassays among 50 normal adults (25 males and 25 females) [34].
  • Sequencing of PCR products confirmed that the FXI mRNA species in platelets is identical to the one in liver [23].
  • A sensitive ELISA failed to detect FXI antigen in the propositus [35].


  1. Interactions among Hageman factor (HG, Factor XII), plasma thromboplastin antecedent (PTA, Factor XI), plasma prekallikrein (PK, Fletcher factor) and high molecular weight kininogen (HMW-K, Fitzgerald factor) in blood coagulation. Saito, H., Ratnoff, O.D. Adv. Exp. Med. Biol. (1979) [Pubmed]
  2. Crystal structures of the FXIa catalytic domain in complex with ecotin mutants reveal substrate-like interactions. Jin, L., Pandey, P., Babine, R.E., Gorga, J.C., Seidl, K.J., Gelfand, E., Weaver, D.T., Abdel-Meguid, S.S., Strickler, J.E. J. Biol. Chem. (2005) [Pubmed]
  3. Plasma thromboplastin antecedent (Factor XI) deficiency in a black family. Niskanen, E.O., Saito, H., Cline, M.J. Arch. Intern. Med. (1981) [Pubmed]
  4. Whole blood clot formation phenotypes in hemophilia A and rare coagulation disorders. Patterns of response to recombinant factor VIIa. Sørensen, B., Ingerslev, J. J. Thromb. Haemost. (2004) [Pubmed]
  5. Real-time quantitative PCR analysis of factor XI mRNA variants in human platelets. Podmore, A., Smith, M., Savidge, G., Alhaq, A. J. Thromb. Haemost. (2004) [Pubmed]
  6. Recovery of ambulation after traumatic brain injury. Katz, D.I., White, D.K., Alexander, M.P., Klein, R.B. Archives of physical medicine and rehabilitation. (2004) [Pubmed]
  7. Percutaneous transluminal angioplasty for intermittent claudication: evidence on which to base the medicine. Chetter, I.C., Spark, J.I., Kent, P.J., Berridge, D.C., Scott, D.J., Kester, R.C. European journal of vascular and endovascular surgery : the official journal of the European Society for Vascular Surgery. (1998) [Pubmed]
  8. Cognitive impairment following closed head injury. Capruso, D.X., Levin, H.S. Neurologic clinics. (1992) [Pubmed]
  9. Use of FK 506 in pancreas transplantation. Gruessner, R.W., Sutherland, D.E., Drangstveit, M.B., Troppmann, C., Gruessner, A.C. Transpl. Int. (1996) [Pubmed]
  10. Diagnostic confusion in mild traumatic brain injury (MTBI). Lessons from clinical practice and EFNS--inquiry. European Federation of Neurological Societies. von Wild, K., Terwey, S. Brain injury : [BI]. (2001) [Pubmed]
  11. The axonal recognition molecule F11 is a multifunctional protein: specific domains mediate interactions with Ng-CAM and restrictin. Brümmendorf, T., Hubert, M., Treubert, U., Leuschner, R., Tárnok, A., Rathjen, F.G. Neuron (1993) [Pubmed]
  12. Complexes between C1-inhibitor, kallikrein, high molecular weight kininogen, plasma thromboplastin antecedent, and plasmin in normal human plasma and hereditary angioneurotic edema plasmas containing dysmorphic C1-inhibitors: role of cold activation. Donaldson, V.H., Harrison, R.A. Blood (1982) [Pubmed]
  13. Neural cell recognition molecule F11: homology with fibronectin type III and immunoglobulin type C domains. Brümmendorf, T., Wolff, J.M., Frank, R., Rathjen, F.G. Neuron (1989) [Pubmed]
  14. Fimbrial serotypes of Escherichia coli strains isolated from extra-intestinal infections. De Ree, J.M., Van den Bosch, J.F. J. Med. Microbiol. (1989) [Pubmed]
  15. Effects of synergists on toxicity of six insecticides in parasitoid Diaeretiella rapae (Hymenoptera: Aphidiidae). Wu, G., Jiang, S., Miyata, T. J. Econ. Entomol. (2004) [Pubmed]
  16. Faecal Escherichia coli mediating transferable multi-antibiotic resistance and undesirable extra-chromosomal genes. Obaseiki-Ebor, E.E., Abiodun, P.O., Emina, P.A. Annals of tropical paediatrics. (1986) [Pubmed]
  17. Factor XI interacts with the leucine-rich repeats of glycoprotein Ibalpha on the activated platelet. Baglia, F.A., Shrimpton, C.N., Emsley, J., Kitagawa, K., Ruggeri, Z.M., López, J.A., Walsh, P.N. J. Biol. Chem. (2004) [Pubmed]
  18. 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]
  19. Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib alpha with thrombin anion-binding exosites I and II, respectively. Yun, T.H., Baglia, F.A., Myles, T., Navaneetham, D., López, J.A., Walsh, P.N., Leung, L.L. J. Biol. Chem. (2003) [Pubmed]
  20. Dinucleotide repeat polymorphism in the human coagulation factor XI gene, intron B (F11), detected using the polymerase chain reaction. Bodfish, P., Warne, D., Watkins, C., Nyberg, K., Spurr, N.K. Nucleic Acids Res. (1991) [Pubmed]
  21. A unique precipitating autoantibody against plasma thromboplastin antecedent associated with multiple apparent plasma clotting factor deficiencies in a patient with systemic lupus erythematosus. Poon, M.C., Saito, H., Koopman, W.J. Blood (1984) [Pubmed]
  22. Assembly of contact-phase factors on the surface of the human neutrophil membrane. Henderson, L.M., Figueroa, C.D., Müller-Esterl, W., Bhoola, K.D. Blood (1994) [Pubmed]
  23. Factor XI messenger RNA in human platelets. Martincic, D., Kravtsov, V., Gailani, D. Blood (1999) [Pubmed]
  24. The relative priority of prekallikrein and factors XI/XIa assembly on cultured endothelial cells. Mahdi, F., Shariat-Madar, Z., Schmaier, A.H. J. Biol. Chem. (2003) [Pubmed]
  25. Identification of a binding site for glycoprotein Ibalpha in the Apple 3 domain of factor XI. Baglia, F.A., Gailani, D., López, J.A., Walsh, P.N. J. Biol. Chem. (2004) [Pubmed]
  26. Nr-CAM: a cell adhesion molecule with ligand and receptor functions. Grumet, M. Cell Tissue Res. (1997) [Pubmed]
  27. Functional cooperation of beta1-integrins and members of the Ig superfamily in neurite outgrowth induction. Treubert, U., Brümmendorf, T. J. Neurosci. (1998) [Pubmed]
  28. Pituitary adenylate cyclase-activating peptide (PACAP) induces differentiation in the neuronal F11 cell line through a PKA-dependent pathway. McIlvain, H.B., Baudy, A., Sullivan, K., Liu, D., Pong, K., Fennell, M., Dunlop, J. Brain Res. (2006) [Pubmed]
  29. Functional interactions of the immunoglobulin superfamily member F11 are differentially regulated by the extracellular matrix proteins tenascin-R and tenascin-C. Zacharias, U., Nörenberg, U., Rathjen, F.G. J. Biol. Chem. (1999) [Pubmed]
  30. 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]
  31. Studies on the blood clotting and fibrinolytic system in the plasma from a sei (baleen) whale. Saito, H., Poon, M., Goldsmith, G.H., Ratnoff, O.D., Arnason, U. Proc. Soc. Exp. Biol. Med. (1976) [Pubmed]
  32. The role of prekallikrein and high-molecular-weight kininogen in the contact activation of Hageman factor (factor XII) by sulfatides and other agents. España, F., Ratnoff, O.D. J. Lab. Clin. Med. (1983) [Pubmed]
  33. Identification of human plasma kallikrein gene polymorphisms and evaluation of their role in end-stage renal disease. Yu, H., Bowden, D.W., Spray, B.J., Rich, S.S., Freedman, B.I. Hypertension (1998) [Pubmed]
  34. Plasma thromboplastin antecedent (PTA, factor XI): a specific and sensitive radioimmunoassay. Saito, H., Goldsmith, G.H. Blood (1977) [Pubmed]
  35. Identification of a novel mutation in a non-Jewish factor XI deficient kindred. Alhaq, A., Mitchell, M., Sethi, M., Rahman, S., Flynn, G., Boulton, P., Caeno, G., Smith, M., Savidge, G. Br. J. Haematol. (1999) [Pubmed]
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