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Gene Review

LOC407212  -  prothrombin

Bos taurus

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Disease relevance of LOC407212

  • Staphylocoagulase (SC) is a protein secreted by the human pathogen, Staphylococcus aureus, that activates human prothrombin (ProT) by inducing a conformational change [1].
  • To characterize the gene more thoroughly, two bovine genomic phage libraries were screened by using prothrombin cDNAs as hybridization probes [2].
  • We have studied PT synthesis by Reuber H-35 rat hepatoma cells exposed to vitamin K and [3H]leucine in serum-free cultures [3].
  • Mechanism and effects of the binding of lupus anticoagulant IgG and prothrombin to surface phospholipid [4].
  • These data may have implications for understanding the mechanisms of the abnormalities in serum prothrombin times reported in Bernard-Soulier syndrome, hemorrhage in von Willebrand disease (vWD), and the increased risk of thrombosis associated with elevated vWF levels [5].

Psychiatry related information on LOC407212

  • To determine whether cleavage was necessary for function, prothrombin conversion reaction mixtures were monitored for thrombin formation and Factor Va cleavage with time in a defined phospholipid vesicle model system [6].

High impact information on LOC407212


Chemical compound and disease context of LOC407212

  • Quantification of the total virion and DB phospholipid, and comparison of prothrombin conversion rates to experiments conducted using known concentrations of PS-containing vesicles showed that 8.5% and 7.2% of the CMV and DB phospholipid, respectively is procoagulant [11].
  • This response has now been studied in rat hepatoma (H-35) cells in which prothrombin secretion is decreased 90% by incubation in the presence of warfarin [12].
  • In a previous study, we prepared a monoclonal antibody (MoAb) to coagulation factor IX (FIX), designated 65-10, which interfered with the activation of FIX by the activated factor XI/Ca(2+) and neutralized the prolonged ox brain prothrombin time of hemophilia B(M) [11,12] [13].
  • The apparent Km value toward prothrombin was relatively low (2.3 microM), suggesting that tryptase contributes to blood coagulation or the process of fibrosis in tissues [14].
  • The 65-10 MoAb antibody neutralized the prolonged ox brain prothrombin time of hemophilia B(M) Nagoya 2 ((180)Arg -->Trp) and Kashihara ((181)Val --> Phe) as well as B(M) Kiryu ((313)Val --> Asp) and Niigata ((390)Ala --> Val) [13].

Biological context of LOC407212

  • SC-bound ProT efficiently clots fibrinogen, thus bypassing the physiological blood coagulation pathway [1].
  • These results suggest that the catalytic site in the SC-(1-325).bovine ProT complex is incompletely formed [1].
  • Comparison of human and bovine fibrinogen as substrates of human and bovine thrombin and the SC-(1-325).(pro)thrombin complexes indicates that the species specificity of SC-(1-325) cofactor activity is determined primarily by differences in conformational activation of bound ProT [1].
  • These analyses suggested that the bovine genome contains a single prothrombin gene that is at least 10 kilobase pairs (kbp) in size [2].
  • Heteroduplex analysis of the cloned genomic DNA and cDNA showed that the prothrombin gene is 14.9 kbp in size and contains at least 14 exons interrupted by 13 introns [2].

Anatomical context of LOC407212


Associations of LOC407212 with chemical compounds


Regulatory relationships of LOC407212


Other interactions of LOC407212


Analytical, diagnostic and therapeutic context of LOC407212


  1. Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation. Friedrich, R., Panizzi, P., Kawabata, S., Bode, W., Bock, P.E., Fuentes-Prior, P. J. Biol. Chem. (2006) [Pubmed]
  2. Characterization of the bovine prothrombin gene. Irwin, D.M., Ahern, K.G., Pearson, G.D., MacGillivray, R.T. Biochemistry (1985) [Pubmed]
  3. Induction of prothrombin synthesis by prothrombin fragments. Graves, C.B., Munns, T.W., Carlisle, T.L., Grant, G.A., Strauss, A.W. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  4. Mechanism and effects of the binding of lupus anticoagulant IgG and prothrombin to surface phospholipid. Rao, L.V., Hoang, A.D., Rapaport, S.I. Blood (1996) [Pubmed]
  5. Fibrin-dependent platelet procoagulant activity requires GPIb receptors and von Willebrand factor. Béguin, S., Kumar, R., Keularts, I., Seligsohn, U., Coller, B.S., Hemker, H.C. Blood (1999) [Pubmed]
  6. Proteolytic alterations of factor Va bound to platelets. Tracy, P.B., Nesheim, M.E., Mann, K.G. J. Biol. Chem. (1983) [Pubmed]
  7. Vitamin K, prothrombin and gamma-carboxyglutamic acid. Stenflo, J. N. Engl. J. Med. (1977) [Pubmed]
  8. Studies of thrombin-induced proteoglycan release in the degradation of human and bovine cartilage. Furmaniak-Kazmierczak, E., Cooke, T.D., Manuel, R., Scudamore, A., Hoogendorn, H., Giles, A.R., Nesheim, M. J. Clin. Invest. (1994) [Pubmed]
  9. Activation of endogenous factor V by a homocysteine-induced vascular endothelial cell activator. Rodgers, G.M., Kane, W.H. J. Clin. Invest. (1986) [Pubmed]
  10. A coagulation pathway on bovine aortic segments leading to generation of Factor Xa and thrombin. Stern, D.M., Nawroth, P.P., Kisiel, W., Handley, D., Drillings, M., Bartos, J. J. Clin. Invest. (1984) [Pubmed]
  11. Prothrombinase assembly on an enveloped virus: evidence that the cytomegalovirus surface contains procoagulant phospholipid. Pryzdial, E.L., Wright, J.F. Blood (1994) [Pubmed]
  12. Prothrombin synthesis and degradation in rat hepatoma (H-35) cells: effects of warfarin. Zhang, P., Suttie, J.W. Blood (1994) [Pubmed]
  13. Detailed characterization of an anti-factor IX monoclonal antibody that neutralizes the prolonged ox brain prothrombin time of hemophilia B(M) by synthetic peptides. Takahashi, I., Kojima, T., Sano, M., Watanabe, T., Kamiya, T., Saito, H. Peptides (2000) [Pubmed]
  14. Biological functions of serine proteases in the granules of rat mast cells. Katunuma, N., Fukusen, N., Kido, H. Adv. Enzyme Regul. (1986) [Pubmed]
  15. Prothrombin is activated on vascular endothelial cells by factor Xa and calcium. Rodgers, G.M., Shuman, M.A. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  16. Cloning and analysis of a cDNA coding for bovine prothrombin. MacGillivray, R.T., Degen, S.J., Chandra, T., Woo, S.L., Davie, E.W. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  17. A new carboxylation reaction. The vitamin K-dependent incorporation of H-14-CO3- into prothrombin. Esmon, C.T., Sadowski, J.A., Suttie, J.W. J. Biol. Chem. (1975) [Pubmed]
  18. Plasma abnormal prothrombin and microsomal prothrombin precursor in various species (38492). Carlisle, T.L., Shah, D.V., Schlegel, R., Suttie, J.W. Proc. Soc. Exp. Biol. Med. (1975) [Pubmed]
  19. A factor IX mutation, verified by direct genomic sequencing, causes haemophilia B by a novel mechanism. Tsang, T.C., Bentley, D.R., Mibashan, R.S., Giannelli, F. EMBO J. (1988) [Pubmed]
  20. The effect of prothrombin fragment 2 on the inhibition of thrombin by antithrombin III. Walker, F.J., Esmon, C.T. J. Biol. Chem. (1979) [Pubmed]
  21. A caesarean section model to characterize coagulation in the fetal and uterine circulation during late gestation in dairy cattle. Heuwieser, W., Grunert, E. Zentralblatt für Veterinärmedizin. Reihe A. (1993) [Pubmed]
  22. Deriving the generic structure of the fibronectin type II domain from the prothrombin Kringle 1 crystal structure. Holland, S.K., Harlos, K., Blake, C.C. EMBO J. (1987) [Pubmed]
  23. Complete primary structure for the zymogen of human complement factor B. Mole, J.E., Anderson, J.K., Davison, E.A., Woods, D.E. J. Biol. Chem. (1984) [Pubmed]
  24. The gamma-carboxyglutamic acid and epidermal growth factor-like domains of factor X. Effect of isolated domains on prothrombin activation and endothelial cell binding of factor X. Persson, E., Valcarce, C., Stenflo, J. J. Biol. Chem. (1991) [Pubmed]
  25. Purification and properties of an abnormal blood coagulation factor IX (factor IXBm)/kinetics of its inhibition of factor X activation by factor VII and bovine tissue factor. Osterud, B., Kasper, C.K., Lavine, K.K., Prodanos, C., Rapaport, S.I. Thromb. Haemost. (1981) [Pubmed]
  26. Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins. Huang, M., Rigby, A.C., Morelli, X., Grant, M.A., Huang, G., Furie, B., Seaton, B., Furie, B.C. Nat. Struct. Biol. (2003) [Pubmed]
  27. Structural features of the kringle domain determine the intracellular degradation of under-gamma-carboxylated prothrombin: studies of chimeric rat/human prothrombin. Wu, W., Bancroft, J.D., Suttie, J.W. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
  28. Magnesium and calcium ion binding to bovine prothrombin fragment 1. A circular dichroism, fluorescence, and 43Ca2+ and 25Mg2+ nuclear magnetic resonance study. Marsh, H.C., Robertson, P., Scott, M.E., Koehler, K.A., Hiskey, R.G. J. Biol. Chem. (1979) [Pubmed]
  29. Prothrombin activation by an activator from the venom of Oxyuranus scutellatus (Taipan snake). Speijer, H., Govers-Riemslag, J.W., Zwaal, R.F., Rosing, J. J. Biol. Chem. (1986) [Pubmed]
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