Thromb Haemost 1998; 80(01): 87-91
DOI: 10.1055/s-0037-1615144
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Cloning and Characterization of a cDNA Encoding Murine Coagulation Factor X

Zhong Liang
1   Department of Chemistry and Biochemistry and the Center for Transgene Research, University of Notre Dame, Notre Dame, Indiana, USA
,
Adrian Cooper
1   Department of Chemistry and Biochemistry and the Center for Transgene Research, University of Notre Dame, Notre Dame, Indiana, USA
,
Melanie E. DeFord
1   Department of Chemistry and Biochemistry and the Center for Transgene Research, University of Notre Dame, Notre Dame, Indiana, USA
,
Peter Carmeliet
2   Center for Transgene Technology and Gene Therapy, Flanders Interuniversity Institute for Biotechnology, KU Leuven, Belgium
,
Desire Collen
2   Center for Transgene Technology and Gene Therapy, Flanders Interuniversity Institute for Biotechnology, KU Leuven, Belgium
,
Francis J. Castellino
1   Department of Chemistry and Biochemistry and the Center for Transgene Research, University of Notre Dame, Notre Dame, Indiana, USA
,
Elliot D. Rosen
1   Department of Chemistry and Biochemistry and the Center for Transgene Research, University of Notre Dame, Notre Dame, Indiana, USA
› Author Affiliations
Further Information

Publication History

Received 28 January 1998

Accepted after revision 31 March 1998

Publication Date:
08 December 2017 (online)

Summary

The cDNA encoding murine coagulation factor X (fX) was isolated and reconstructed from a λZap cDNA library generated from murine liver mRNA. The cDNA contains 1486 bases starting at the 5’-translation initiation codon. It includes an open reading frame of 1443 nucleotides, followed by an 18 residue 3’ nontranslated sequence downstream of the first stop codon, and a 3’ poly(A) tail. The translation product is composed of a 40-amino acid signal/propeptide region followed by a 441-residue mature protein. The latter is highly homologous to that of human and rat fX. All protein domains of human and rat fX are strictly conserved in mouse fX. The cDNA coding for mouse fX has been expressed in human embryonic kidney 293 cells and generates fX activity measured in a clotting assay using human fX-deficient plasma.

 
  • References

  • 1 Jackson CM, Nemerson Y. Blood coagulation. Ann Rev Biochem 1980; 49: 765-811.
  • 2 Foster WB, Nesheim ME, Mann KG. The factor Xa-catalyzed activation of factor V. J Biol Chem 1983; 258: 13970-7.
  • 3 Radcliffe R, Nemerson Y. Activation and control of factor VII by activated factor X and thrombin. Isolation and characterization of a single chain form of factor VII. J Biol Chem 1975; 250: 388-95.
  • 4 Donath MJSH, Lenting PJ, Van Mourik JA, Mertens K. Kinetics of factor VIII light-chain cleavage by thrombin and factor Xa. A regulatory role of the factor VIII heavy-chain region Lys713-Arg740. Eur J Biochem 1996; 240: 365-72.
  • 5 Haley PE, Doyle MF, Mann KG. The activation of bovine protein C by factor Xa. J Biol Chem 1989; 264: 16303-10.
  • 6 Gasic GP, Arenas CP, Gasic TB, Gasic GJ. Coagulation factors X, Xa, and protein S as potent mitogens of cultured aortic smooth muscle cells. Proc Natl Acad Sci USA 1992; 89: 2317-20.
  • 7 Ko FN, Yang YC, Huang SC, Ou JT. Coagulation factor Xa stimulates platelet-derived growth factor release and mitogenesis in cultured vascular smooth muscle cells of rat. J Clin Invest 1996; 98: 1493-501.
  • 8 Altieri DC. Xa receptor EPR-1. FASEB J 1995; 9: 860-5.
  • 9 Cirino G, Cicala C, Bucci M, Sorrentino L, Ambrosini G, DeDominicis G, Altieri DC. Factor Xa as an interface between coagulation and inflammation. Molecular mimicry of factor Xa association with effector cell protease receptor-1 induces acute inflammation in vivo. J Clin Invest 1997; 99: 2446-51.
  • 10 Foster DC, Yoshitake S, Davie EW. The nucleotide sequence of the gene for human protein C. Proc Natl Acad Sci USA 1985; 82: 4673-7.
  • 11 Jalbert LR, Rosen ED, Lissens A, Carmeliet P, Collen D, Castellino FJ. Nucleotide structure and characterization of the murine gene encoding anticoagulant protein C. Thromb Haemost 1998; 79: 310-6.
  • 12 Yoshitake S, Schach BG, Foster DC, Davie EW, Kurachi K. Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry 1985; 24: 3736-50.
  • 13 O’Hara PJ, Grant FJ, Haldeman BA, Gray CL, Insley MY, Hagen FS, Murray MJ. Nucleotide sequence of the gene coding for human factor VII, a vitamin K-dependent protein participating in blood coagulation. Proc Natl Acad Sci USA 1987; 84: 5158-62.
  • 14 Idusogie E, Rosen ED, Carmeliet P, Collen D, Castellino FJ. Nucleotide structure and characterization of the murine blood coagulation factor VII gene. Thromb Haemost 1996; 76: 957-64.
  • 15 McMullen BA, Fujikawa K, Kisiel W, Sasagawa T, Howald WN, Kwa EW, Weinstein B. Complete amino acid sequence of the light chain of human blood coagulation factor X: Evidence for identification of residue 63 as β-hydroxyaspartic acid. Biochemistry 1983; 22: 2875-84.
  • 16 Leytus SP, Chung DW, Kisiel W, Kurachi K, Davie EW. Characterization of a cDNA coding for human factor X. Proc Natl Acad Sci USA 1984; 81: 3699-702.
  • 17 Di Scipio RG, Hermodson MA, Davie EW. Activation of human factor X (Stuart factor) by a protease from Russell’s viper venom. Biochemistry 1977; 16: 5253-60.
  • 18 Hojrup P, Magnusson S. Disulphide bridges of bovine factor X. Biochem J 1987; 245: 887-91.
  • 19 Titani K, Hermodson MA, Fujikawa K, Ericsson LH, Walsh KA, Neurath H, Davie EW. Bovine factor X1a (activated Stuart factor). Evidence of homology with mammalian serine proteases. Biochemistry 1972; 11: 4899-903.
  • 20 Nemerson Y. The reaction between bovine brain tissue factor and factors VII and X. Biochemistry 1966; 5: 601-8.
  • 21 Nemerson Y. Tissue factor and hemostasis. Blood 1988; 71: 1-8.
  • 22 Rapaport SI. The extrinsic pathway inhibitor: A regulator of tissue factor-dependent blood coagulation. Thromb Haemost 1991; 66: 6-15.
  • 23 Broze GJ, Girard TJ, Novotny WF. The lipoprotein-associated coagulation inhibitor. Prog Hemost Thromb 1991; 10: 243-68.
  • 24 Fujikawa K, Coan MH, Legaz ME, Davie EW. The mechanism of activation of bovine factor X (Stuart factor) by intrinsic and extrinsic pathways. Biochemistry 1974; 13: 5290-9.
  • 25 Fujikawa K, Legaz ME, Davie EW. Bovine factor X1 (Stuart factor). Mechanism of activation by protein from Russell’s viper venom. Biochemistry 1972; 11: 4892-9.
  • 26 Boguski MS, Lowe TM, Tolstoshev CM. dbEST-database for “expressed sequence tags”. Nat Genet 1993; 4: 332-3.
  • 27 Kozak M. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucl Acids Res 1984; 12: 857-72.
  • 28 Kaul RK, Hildebrand B, Roberts S, Jagadeeswaran P. Isolation and characterization of human blood coagulation factor X cDNA. Gene 1986; 41: 311-4.
  • 29 Messier TL, Pittman DD, Long GL, Kaufman RJ, Church WR. Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X. Gene 1991; 99: 291-4.
  • 30 Murakawa M, Okamura T, Kamura T, Kuroiwa M, Harada M, Niho Y. Analysis of the partial nucleotide sequences and deduced primary structures of the protease domains of mammalian blood coagulation factors VII and X. Eur J Haematol 1994; 52: 162-8.
  • 31 James HL, Larson PJ, Chao YB, Yan SB, Kim DJ. Isolation and characterization of mouse coagulation factor X. Biophysical and enzymological properties. Thromb Haemost 1997; 78: 1049-54.