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Blood Coagulation Factor IX/Factor X-Binding Protein

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Abstract

C-type lectin-like proteins of snake have a variety of biological properties, acting for example as an anticoagulant, procoagulant, and agonist/antagonist of platelet activation. Dimerization or oligomer formation of carbohydrate recognition domain (CRD) in C-type lectin by 3D domain swapping generates novel proteins with new functions such as coagulant-, anticoagulant-, and platelet-modulating activities. The structural and functional studies of the first identified C-type lectin-like proteins, IX/X-bp, have been instrumental in defining how new functionally heterodimeric C-type lectin-like proteins are generated from monomeric CRD (carbohydrate recognition domain) in C-type lectin by 3D domain swapping. The crystal structure of IX/X-bp revealed that the two subunits associated by 3 D-domain swapping, and this dimerization resulted in the creation of a concave surface serving as a binding site of Gla domain, the functionally important domain of blood coagulation factors. The strong activities by snaclecs such as IX/X-bp and X-bp are caused by the binding at the Gla domain of factors IX and X. C-type lectin-like proteins of snake venom such as IX/X-bp and its structurally-related proteins recognize various ligands by the higher frequency of mutation in the open reading frames than in the non-coding regions after duplication of a gene.

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References

  • Atoda, H., Hyuga, M., Morita, T., 1991. The primary structure of coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Homology with asialoglycoprotein receptors, proteoglycan core protein, tetranectin, and lymphocyte Fcɛ receptor for immunoglobulin E. J. Biol. Chem. 266, 14903–14911.

    PubMed  CAS  Google Scholar 

  • Atoda, H., Ishikawa, M., Mizuno, H., Morita, T., 1998. Coagulation factor X-binding protein from Deinagkistrodon acutus venom is a Gla domain-binding protein. Biochemistry 37, 17361–17370.

    Article  PubMed  CAS  Google Scholar 

  • Atoda, H., Ishikawa, M., Yoshihara, E., Sekiya, F., Morita, T., 1995. Blood coagulation factor IX-binding protein from the venom of Trimeresurus flavoviridis: purification and characterization. J. Biochem. (Tokyo) 118, 965–973.

    Article  CAS  Google Scholar 

  • Atoda, H., Kaneko, H., Mizuno, H., Morita, T., 2002. Calcium-binding analysis and molecular modeling reveal echis coagulation factor IX/factor X-binding protein has the Ca-binding properties and Ca ion-independent folding of other C-type lectin-like proteins. FEBS Lett. 531, 229–234.

    Article  PubMed  CAS  Google Scholar 

  • Atoda, H., Morita, T., 1989. A novel blood coagulation factor IX/factor X-binding protein with anticoagulant activity from the venom of Trimeresurus flavoviridis (Habu snake): isolation and characterization. J. Biochem. (Tokyo) 106, 808–813.

    CAS  Google Scholar 

  • Atoda, H., Morita, T., 1993. Arrangement of the disulfide bridges in a blood coagulation factor IX/factor X-binding protein from the venom of Trimeresurus flavoviridis. J. Biochem. (Tokyo) 113, 159–163.

    CAS  Google Scholar 

  • Atoda, H., Yoshida, N., Ishikawa, M., Morita, T., 1994. Binding properties of the coagulation factor IX/factor X-binding protein isolated from the venom of Trimeresurus flavoviridis. Eur. J. Biochem. 224, 703–708.

    Article  PubMed  CAS  Google Scholar 

  • Batuwangala, T., Leduc, M., Gibbins, J.M., Bon, C., Jones, E.Y., 2004. Structure of the snake-venom toxin convulxin. Acta Crystallogr. D Biol. Crystallogr. 60(Pt 1), 46–53.

    Article  PubMed  Google Scholar 

  • Clemetson, J.M., Polgar, J., Magnenat, E., Wells, T.N., Clemetson, K.J., 1999. The platelet collagen receptor glycoprotein VI is a member of the immunoglobulin superfamily closely related to FcalphaR and the natural killer receptors. J. Biol. Chem. 274, 29019–29024.

    Article  PubMed  CAS  Google Scholar 

  • Bennett, M.J., Schluneggar, M.P., Eisenberg, D., 1995, 3 D domain swapping: mechanism for oligomer assembly. Protein Sci. 4, 2455–2468.

    Article  PubMed  CAS  Google Scholar 

  • Clemetson, K.J., Morita, T., Kini, R.M., 2009a, Classification and nomenclature of snake venom C-type lectins and related proteins. Toxicon 54, 83.

    Article  PubMed  CAS  Google Scholar 

  • Clemetson, K.J., Morita, T, Kini, M.R., 2009b. Registry of exogenous hemostatic factors of SSC of the ISTH. Scientific and standardization committee communications: classification and nomenclature of snake venom C-type lectins and related proteins. J. Thromb. Haemost. 7, 360.

    Article  PubMed  CAS  Google Scholar 

  • Fujimura, Y., Kawasaki, T., Titani, K., 1996. Snake venom proteins modulating the interaction between von Willebrand factor and platelet glycoprotein Ib. Thromb. Haemost. 76, 633–639.

    PubMed  CAS  Google Scholar 

  • Fukuda, K., Mizuno, H., Atoda, H., Morita, T., 2000. Crystal structure of flavocetin-A, a platelet glycoprotein Ib-binding protein, reveals a novel cyclic tetramer of C-type lectin-like heterodimers. Biochemistry 39, 1915–1923.

    Article  PubMed  CAS  Google Scholar 

  • Hirotsu, S., Mizuno, H., Fukuda, K., Ma, C.Q., Matsui, T., Hamako, J., Morita, T., Titani, K., 2001. Crystal structure of bitiscetin, a von Willebrand factor-dependent platelet aggregation inducer. Biochemistry 40, 13592–13597.

    Article  PubMed  CAS  Google Scholar 

  • Horii, K., Okuda, D., Morita, T., Mizuno, H., 2003. Structural characterization of EMS16, an antagonist of collagen receptor (GPIa/IIa) from the venom of Echis multisquamatus. Biochemistry 42, 12497–12502.

    Article  PubMed  CAS  Google Scholar 

  • Iwahashi, H., Kimura, M., Nakajima, K., Yamada, D., Morita, T., 2001. Determination of plasma prothrombin level by Ca2+-dependent prothrombin activator (CA-1) during warfarin anticoagulation. J. Heart Valve Dis. 10, 388–392.

    PubMed  CAS  Google Scholar 

  • Jasti, J., Paramasivam, M., Srinivasan, A., Singh, T.P., 2004. Crystal structure of echicetin from Echis carinatus (Indian saw-scaled viper) at 2.4A resolution. J. Mol. Biol. 335, 167–176.

    Article  PubMed  CAS  Google Scholar 

  • Lee, W.H., Zhuang, Q.Y., Zhang, Y., 2003. Cloning and characterization of a blood coagulation factor IX-binding protein from the venom of Trimeresurus stejnegeri. Toxicon 41, 765–772.

    Article  PubMed  CAS  Google Scholar 

  • Liu, Y., Eisenberg, D., 2002. 3D domain swapping: as domains continue to swap. Protein Sci. 11, 1285–1299.

    Article  PubMed  CAS  Google Scholar 

  • Matsuzaki, R., Yoshihara, E., Yamada, M., Shima, K., Atoda, H., Morita, T., 1996. cDNA cloning of IX/X-BP, a heterogeneous two-chain anticoagulant protein from snake venom. Biochem. Biophys. Res. Commun. 220, 382–387.

    Article  PubMed  CAS  Google Scholar 

  • Mizuno, H., Fujimoto, Z., Atoda, H., Morita, T., 2001. Crystal structure of an anticoagulant protein in complex with the Gla domain of factor X. Proc. Natl. Acad. Sci. U.S.A. 98, 7230–7234.

    Article  PubMed  CAS  Google Scholar 

  • Mizuno, H., Fujimoto, Z., Koizumi, M., Kano, H., Atoda, H., Morita, T., 1997. Structure of coagulation factors IX/X-binding protein, a heterodimer of C-type lectin domains. Nat. Struct. Biol. 4, 438–441.

    Article  PubMed  CAS  Google Scholar 

  • Mizuno, H., Fujimoto, Z., Koizumi, M., Kano, H., Atoda, H., Morita, T., 1999. Crystal structure of coagulation factor IX-binding protein from habu snake venom at 2.6 A: implication of central loop swapping based on deletion in the linker region. J. Mol. Biol. 289, 103–112.

    Article  PubMed  CAS  Google Scholar 

  • Morita, T., 1998. Proteases which activate factor X, in: Bailey, G.S. (Ed.), Snake Venom Enzymes. Alaken, Inc., Colorado, pp. 179–208.

    Google Scholar 

  • Morita, T., 2004a. C-type lectin-related proteins from snake venoms. Curr. Drug Targets-Cardiovasc. Haematol Disorders 4, 357–373.

    Article  CAS  Google Scholar 

  • Morita, T., 2004b. Use of snake venom inhibitors in studies of the function and tertiary structure of coagulation factors. Int. J. Hematol. 79, 123–129.

    Article  PubMed  CAS  Google Scholar 

  • Nakashima, K., Ogawa, T., Oda, N., Hattori, M., Sakaki, Y., Kihara, H., Ohno, M., 1993. Accelerated evolution of Trimeresurus flavoviridis venom gland phospholipase A2 isozymes. Proc. Natl. Acad. Sci. U.S.A. 90, 5964–5968.

    Article  PubMed  CAS  Google Scholar 

  • Ogawa, T., Oda, N., Nakashima, K., Sasaki, H., Hattori, M., Sakaki, Y., Kihara, H., Ohno, M., 1992. Unusually high conservation of untranslated sequences in cDNAs for Trimeresurus flavoviridis phospholipase A2 isozymes. Proc. Natl. Acad. Sci. U.S.A. 89, 8557–8561.

    Article  PubMed  CAS  Google Scholar 

  • Ohno, M., Chijiwa, T., Oda-Ueda, N., Ogawa, T., Hattori, S., 2003. Molecular evolution of myotoxic phospholipases A2 from snake venom. Toxicon 42, 841–854.

    Article  PubMed  CAS  Google Scholar 

  • Peng, M., Lu, W., Beviglia, L., Niewiarowski, S., Kirby, E.P., 1993. Echicetin: a snake venom protein that inhibits binding of von Willebrand factor and alboaggregins to platelet glycoprotein Ib. Blood 81, 2321–2328.

    PubMed  CAS  Google Scholar 

  • Peng, M., Lu, W., Kirby, E.P., 1991. Alboaggregin-B: a new platelet agonist that binds to platelet membrane glycoprotein Ib. Biochemistry 30, 11529–11536.

    Article  PubMed  CAS  Google Scholar 

  • Sekiya, F., Atoda, H., Morita, T., 1993. Isolation and characterization of an anticoagulant protein homologous to botrocetin from the venom of Bothrops jararaca. Biochemistry 32, 6892–6897.

    Article  PubMed  CAS  Google Scholar 

  • Sekiya, F., Yamashita, T., Atoda, H., Komiyama, Y., Morita, T., 1995. Regulation of the tertiary structure and function of coagulation factor IX by magnesium (II) ions. J. Biol. Chem. 270, 14325–14331.

    Article  PubMed  CAS  Google Scholar 

  • Sekiya, F., Yoshida, M., Yamashita, T., Morita, T., 1996a. Localization of the specific binding site for magnesium (II) ions in factor IX. FEBS Lett. 392, 205–208.

    Article  PubMed  CAS  Google Scholar 

  • Sekiya, F., Yoshida, M., Yamashita, T., Morita, T., 1996b. Magnesium (II) is a crucial constituent of the blood coagulation cascade. Potentiation of coagulant activities of factor IX by Mg2+ ions. J. Biol. Chem. 271, 8541–8544.

    Article  PubMed  CAS  Google Scholar 

  • Shikamoto, Y., Morita, T., Fujimoto, Z., Mizuno, H., 2003. Crystal structure of Mg2+- and Ca2+-bound Gla domain of factor IX complexed with binding protein. J. Biol. Chem. 278, 24090–24094.

    Article  PubMed  CAS  Google Scholar 

  • Shin, Y., Okuyama, I., Hasegawa, J., Morita, T., 2000. Molecular cloning of glycoprotein Ib-binding protein, flavocetin-A, which inhibits platelet aggregation. Thromb. Res. 99(3), 239–247.

    Article  PubMed  CAS  Google Scholar 

  • Takeda, S., Igarashi, T., Mori, H., 2007. Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases. FEBS Lett. 581, 5859–5864

    Article  PubMed  CAS  Google Scholar 

  • Takeya, H., Nishida, S., Miyata, T., Kawada, S., Saisaka, Y., Morita, T., Iwanaga, S., 1992. Coagulation factor X activating enzyme from Russell’s viper venom (RVV-X). A novel metalloproteinase with disintegrin (platelet aggregation inhibitor)-like and C-type lectin-like domains. J. Biol. Chem. 267, 14109–14117.

    PubMed  CAS  Google Scholar 

  • Tani, A., Ogawa, T., Nose, T., Nikandrov, N.N., Deshimaru, M., Chijiwa, T., Chang, C.C., Fukumaki, Y., Ohno, M., 2002. Characterization, primary structure and molecular evolution of anticoagulant protein from Agkistrodon actus venom. Toxicon 40, 803–813.

    Article  PubMed  CAS  Google Scholar 

  • Taniuchi, Y., Kawasaki, T., Fujimura, Y., Suzuki, M., Titani, K., Sakai, Y., Kaku, S., Hisamichi, N., Satoh, N., Takenaka, T., et al., 1995. Flavocetin-A and -B, two high molecular mass glycoprotein Ib binding proteins with high affinity purified from Trimeresurus flavoviridis venom, inhibit platelet aggregation at high shear stress. Biochim. Biophys. Acta 1244, 331–338.

    Article  PubMed  Google Scholar 

  • Whisstock, J.C., Bottomley, S.P., 2008. Serpins’ mystery solved. Nature 455, 1189–1190.

    Article  PubMed  CAS  Google Scholar 

  • Yamada, D., Morita, T., 1999. CA-1 method, a novel assay for quantification of normal prothrombin using a Ca2+ -dependent prothrombin activator, carinactivase-1. Thromb. Res. 94, 221–226.

    Article  PubMed  CAS  Google Scholar 

  • Yamada, D., Sekiya, F., Morita, T., 1996. Isolation and characterization of carinactivase, a novel prothrombin activator in Echis carinatus venom with a unique catalytic mechanism. J. Biol. Chem. 271, 5200–5207.

    Article  PubMed  CAS  Google Scholar 

  • Yamasaki, M., Li, W., Johnson, D.J.D., Huntington, J.A., 2008. Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. Nature 455, 1255–1259

    Article  PubMed  CAS  Google Scholar 

  • Yoshida, E., Fujimura, Y., Miura, S., Sugimoto, M., Fukui, H., Narita, N., Usami, Y., Suzuki, M., Titani, K., 1993. Alboaggregin-B and botrocetin, two snake venom proteins with highly homologous amino acid sequences but totally distinct functions on von Willebrand factor binding to platelets. Biochem. Biophys. Res. Commun. 191, 1386–1392.

    Article  PubMed  CAS  Google Scholar 

  • Zingali, R.B., Jandrot-Perrus, M., Guillin, M.C., Bon, C., 1993. Bothrojaracin, a new thrombin inhibitor isolated from Bothrops jararaca venom: characterization and mechanism of thrombin inhibition. Biochemistry 32, 10794–10802.

    Article  PubMed  CAS  Google Scholar 

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Correspondence to Takashi Morita .

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Morita, T. (2010). Blood Coagulation Factor IX/Factor X-Binding Protein. In: Kini, R., Clemetson, K., Markland, F., McLane, M., Morita, T. (eds) Toxins and Hemostasis. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-9295-3_11

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