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Thromb Haemost 1996; 75(03): 481-487
DOI: 10.1055/s-0038-1650301
Original Article
Schattauer GmbH Stuttgart

Characterization of a cDNA Encoding Murine Coagulation Factor VII

Esohe Idusogie
1   The Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA
,
Elliot Rosen
1   The Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA
2   The Center for Transgene Technology and Gene Therapy, Flanders Interuniversity Institute for Biotechnology, KU Leuven, Belgium
,
Jie-Ping Geng
1   The Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA
,
Peter Carmeliet
2   The Center for Transgene Technology and Gene Therapy, Flanders Interuniversity Institute for Biotechnology, KU Leuven, Belgium
,
Desirá Collen
2   The Center for Transgene Technology and Gene Therapy, Flanders Interuniversity Institute for Biotechnology, KU Leuven, Belgium
,
Francis J Castellino
1   The Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, USA
› Institutsangaben
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Publikationsverlauf

Received 31. August 1995

Accepted after revision 13. Dezember 1995

Publikationsdatum:
27. Juli 2018 (online)

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Summary

The cDNA encoding murine coagulation factor VII (mfVII) was isolated and reconstructed from a Λ Zap cDNA library generated from murine liver mRNA. The cDNA contains 1903 nucleotides spanning 15 bases upstream of the 5’-translation initiation codon, an open reading frame of 1338 nucleotides, 550 nucleotides downstream of the first stop codon and a 3’ poly(A) tail. The translation product is composed of a 41-amino acid signal/propeptide region followed by a 405-residue mature protein. The latter is highly homologous to that of human, rabbit, bovine, Rhesus monkey, and canine fVII. All protein domains of hfVII are strictly conserved in mfVII.

 

  • References

  • 1 Kisiel W, Davie E. Isolation and characterization of bovine factor VII. Biochemistry 1975; 14: 4928-4934
    CrossrefPubMedGoogle Scholar
  • 2 Hagen FS, Gray CL, O’Hara P, Grant FJ, Saari GC, Woodbury RG, Hart CE, Insley M, Kisiel W, Kurachi K, Davie EW. Characterization of a cDNA coding for human factor VII. Proc Natl Acad Sci USA 1986; 83: 2412-2416
    CrossrefPubMedGoogle Scholar
  • 3 Pedersen AH, Nordfang O, Norris F, Wiberg FC, Christensen PM, Moeller KB, Midahl-Pedersen J, Beck TC, Norris K, Hedner U, Kisiel W. Recombinant human extrinsic pathway inhibitor. Production, isolation and characterization of its inhibitory activity on tissue factor-initiated coagulation reactions. J Biol Chem 1990; 265: 16786-16793
    PubMedGoogle Scholar
  • 4 Komiyama Y, Pedersen AH, Kisiel W. Proteolytic activation of human factors IX and X by recombinant human factor Vila: Effects of calcium, phospholipid and tissue factor. Biochemistry 1990; 29: 9418-9425
    CrossrefPubMedGoogle Scholar
  • 5 tenCate H, Bauer KA, Levi M, Edgington TS, Sublett RD, Barzegar S, Kass BL, Rosenberg RD. The activation of factor X and prothrombin by recombinant factor Vila in vivo is mediated by tissue factor. J Clin Invest 1993; 92: 1207-1212
    CrossrefPubMedGoogle Scholar
  • 6 Teglt DSC, Macik BG, McCord DM, Monroe D, Roberts HR. Mechanism by which recombinant factor Vila shortens the aPTT: Activation of factor X in the absence of tissue factor. Thromb Res 1989; 56: 603-609
    CrossrefPubMedGoogle Scholar
  • 7 Seligsohn U, Osterud B, Brown SF, Griffin JH, Rapaport SI. Activation of human factor VII in plasma and in purified systems. Roles of activated factor IX, kallikrein, and activated factor XII. J Clin Invest 1979; 64: 1056-1065
    CrossrefPubMedGoogle Scholar
  • 8 Broze GJ, Majerus PJ. Human factor VII. Methods Enzymol 1981; 80: 228-237
    PubMedGoogle Scholar
  • 9 Pedersen AH, Lund-Hansen D, Bisgaard-Frantzen H, Olsen F, Petersen LC. Autoactivation of human recombinant factor VII. Biochemistry 1989; 28: 9331-9336
    CrossrefPubMedGoogle Scholar
  • 10 Nakagaki T, Foster DC, Berkner KL, Kisiel W. Initiation of the extrinsic pathway of blood coagulation: Evidence for the tissue factor dependent autoactivation of human coagulation factor VII. Biochemistry 1991; 30: 10819-10824
    CrossrefPubMedGoogle Scholar
  • 11 Neuenschwander PF, Fiore MM, Morrissey JH. Factor VII autoactivation proceeds via interaction of distinct protease-cofactor and zymogen-cofactor complexes. Implications of a 2-dimensional enzyme kinetic mechanism. J Biol Chem 1993; 268: 21489-21492
    PubMedGoogle Scholar
  • 12 Thim L, Bjoem S, Christensen M, Nicolaisen EM, Lund-Hansen T, Pedersen AH, Hedner U. Amino acid sequence and posttranslational modifications of human factor Vila from plasma and transfected baby hamster kidney cells. Biochemistry 1988; 27: 7785-7793
    CrossrefPubMedGoogle Scholar
  • 13 McMullen BA, Fujikawa K, Kisiel W. The occurrence of Β-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens. Biochem BiophysRes Comm 1983; 115: 8-14
    PubMedGoogle Scholar
  • 14 Nishimura H, Kawabata S-i, Kisiel W, Hase S, Ikenaka T, Takao T, Shimonishi Y, Iwanaga S. Identification of a disaccharide (xyl-glc) and a trisaccharide (xyl2-glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z. J Biol Chem 1989; 264: 20320-20325
    PubMedGoogle Scholar
  • 15 Bjoem S, Foster DC, Thim L, Wiberg FC, Christensen M, Komiyama Y, Pedersen AH, Kisiel W. Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine. J Biol Chem 1991; 266: 11051-11057
    PubMedGoogle Scholar
  • 16 Foster DC, Yoshitake S, Davie EW. The nucleotide sequence of the gene for human protein C. Proc Natl Acad Sci USA 1985; 82: 4673-4677
    CrossrefPubMedGoogle Scholar
  • 17 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: 3736-3750
    CrossrefPubMedGoogle Scholar
  • 18 Leytus SP, Foster DC, Kurachi K, Davie EW. Gene for human factor X: A blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. Biochemistry 1986; 25: 5098-5102
    CrossrefPubMedGoogle Scholar
  • 19 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: 5158-5162
    CrossrefPubMedGoogle Scholar
  • 20 Matsushita T, Kojima T, Emi N, Takahashi I, Satio H. Impaired human tissue factor-mediated activity in blood clotting factor VII (Nagoya) (ARG(304)-<trp). Evidence that a region in the catalytic domain of factor VII is important for the association with tissue factor. J Biol Chem 1994; 269: 7355-7363
    PubMedGoogle Scholar
  • 21 Ohiwa M, Hayashi T, Wada H, Minamikawa K, Shirakawa S, Suzuki K. Factor VII MIE. Homozygous asymptomatic type-I deficiency caused by an amino acid substitution of His (CAC) for ARG(247)(CGC) in the catalytic domain. Thromb Haemost 1994; 71: 773-777
    Artikel in Thieme ConnectPubMedGoogle Scholar
  • 22 Mariani G, Iacopino G, Pasqualilasagni R. Evidence that factor VII lev( correlate strongly with fibrinopeptide A release. Evaluation by an ex vivo method. Int J Clin Lab Res 1992; 22: 111-114
    CrossrefPubMedGoogle Scholar
  • 23 Meade TW, Mellows S, Brozovic M, Miller GJ, Chakrabarti RR, North WRS, Haines AP, Stirling Y, Imeson JD, Thompson SG. Haemostatic function and ischaemic heart disease: principal results of the Northwick Park Heart Study. Lancet 1986; 2: 533-537
    PubMedGoogle Scholar
  • 24 Heinrich J, Balleisen L, Schulte H, Assmann G, van de Loo J. Fibrinogen and factor VII in the prediction of coronary risk. Results from the PROCAM study in healthy men. Arterioscler Thromb 1994; 14: 54-59
    CrossrefPubMedGoogle Scholar
  • 25 Green F, Kelleher C, Wilkes H, Temple A, Meade T, Humphries SA. A common genetic polymorphism associated with lower coagulation factor VII levels in healthy individuals. Arterioscler Thromb 1991; 11: 540-546
    CrossrefPubMedGoogle Scholar
  • 26 Lane A, Cruickshank JK, Mitchell J, Henderson A, Humphries S, Green F. Genetic and environmental determinants of factor VII coagulant activity in ethnic groups at differing risk of coronary heat disease. Atherosclerosis 1992; 94: 43-50
    CrossrefPubMedGoogle Scholar
  • 27 Kario K, Matsuo T, Yamada T, Nakao K, Shimano C, Matsuo M. Factor VII hyperactivity in chronic dialysis patients. Thromb Res 1992; 67: 105-113
    CrossrefPubMedGoogle Scholar
  • 28 Kario K, Matsuo T, Matsuo M, Koide M, Yamada T, Nakamura S, Sakata T, Kato H, Miyata T. Marked increase of activated factor VII in uremic patients. Thromb Haemost 1995; 73: 763-767
    Artikel in Thieme ConnectPubMedGoogle Scholar
  • 29 Pearson WR, Lipman DJ. Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 1988; 85: 2444-2448
    CrossrefPubMedGoogle Scholar
  • 30 Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J Mol Biol 1990; 215: 403-410
    CrossrefPubMedGoogle Scholar
  • 31 Zhang L, Castellino FJ. A Γ-carboxyglutamic acid variant (Γ6D, Γ7D) of human activated protein C displays greatly reduced activity as an anticoagulant. Biochemistry 1990; 29: 10828-10834
    CrossrefPubMedGoogle Scholar
  • 32 Israel DI. A PCR-based method for high stringency screening of DNA libraries. Nucl Acids Res 1993; 21: 2627-2631
    CrossrefPubMedGoogle Scholar
  • 33 Menhart N, Sehl LC, Kelley RF, Castellino FJ. Construction, expression and purification of recombinant kringle 1 of human plasminogen and analysis of its interaction with co-amino acids. Biochemistry 1991; 30: 1948-1957
    CrossrefPubMedGoogle Scholar
  • 34 De Serrano VS, Menhart N, Castellino FJ. The expression, purification and characterization of the recombinant kringle 1 domain from tissue-type plasminogen activator. Arch Biochem Biophys 1992; 294: 282-290
    CrossrefPubMedGoogle Scholar
  • 35 De Serrano VS, Castellino FJ. The role of tryptophan-74 of the recombinant kringel 2 domain of tissue-type plasminogen activator in its co-amino acid binding properties. Biochemistry 1992; 31: 3326-3335
    CrossrefPubMedGoogle Scholar
  • 36 Sanger F, Nicklen S, Coulson AR. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 1977; 74: 5463-5467
    CrossrefPubMedGoogle Scholar
  • 37 Staden E. A new computer method for the storage and manipulation of DNA gel reading data. Nucl Acids Res 1980; 8: 3673-3694
    CrossrefPubMedGoogle Scholar
  • 38 Takeya H, Kawabata S-i, Nakagawa K, Yamamichi Y, Miyata T, Iwanaga S, Takao T, Shimonishi Y. Bovine factor VII. Its purification and complete amino acid sequence. J Biol Chem 1988; 262: 14868-14877
    PubMedGoogle Scholar
  • 39 Brothers AB, Clarke BJ, Sheffield WP, Blajchman MA. Complete nucleotide sequence of the cDNA encoding rabbit coagulation factor VII. Thromb Res 1993; 69: 231-238
    CrossrefPubMedGoogle Scholar
  • 40 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: 162-168
    PubMedGoogle Scholar
  • 41 Huber P, Schmitz T, Griffin J, Jacobs M, Walsh C, Furie B, Furie BC. Identification of amino acids in the Γ-carboxylation recognition site of the propeptide of prothrombin. J Biol Chem 1990; 265: 12467-12473
    PubMedGoogle Scholar
  • 42 Zhang L, Castellino FJ. The binding energy of human coagulation protein C to acidic phospholipid vesicles contains a major contribution from leucine-5 in the gamma-carboxyglutamic acid domain. J Biol Chem 1994; 269: 3590-3595
    PubMedGoogle Scholar
  • 43 Soriano-Garcia M, Padmanabhan K, de Vos AM, Tulinsky A. The Ca2+ ion and membrane binding structure of the gla-domain of Ca-prothrombin fragment 1. Biochemistry 1992; 31: 2554-2566
    CrossrefPubMedGoogle Scholar
  • 44 Zhang L, Jhingan A, Castellino FJ. Role of individual gamma-carboxyglutamic acid residues of activated human protein C in defining its in vitro anticoagulant activitiy. Blood 1992; 80: 942-952
    PubMedGoogle Scholar
  • 45 Zhang L, Castellino FJ. Role of the hexapeptide disulfide loop present in the y-carboxyglutamic acid domain of protein C in its activation properties and in the in vitro anticoagulant activity of activated protein C. Biochemistry 1991; 30: 6696-6704
    CrossrefPubMedGoogle Scholar
  • 46 Christiansen WT, Geng J-P, Castellino FJ. Structure-function assessment of the role of the helical stack domain in the properties of human recombinant protein C and activated protein C. Biochemistry 1995; 34: 8082-8090
    CrossrefPubMedGoogle Scholar
  • 47 Colpitts TL, Castellino FJ. Calcium and phospholipid binding properties of synthetic gamma-carboxyglutamic acid-containing peptides with sequence counterparts in human protein C. Biochemistry 1994; 33: 3501-3508
    CrossrefPubMedGoogle Scholar
  • 48 Valcarce C, Holmgren A, Stenflo J. Calcium-dependent interaction between gamma-carboxyglutamic acid-containing and N-terminal epidermal growth factor-like modules in factor X. J Biol Chem 1994; 269: 26011-26016
    PubMedGoogle Scholar
  • 49 Handford PA, Mayhew M, Baron M, Winship PR, Campbell ID, Brownlee GG. Key residues involved in calcium-binding motifs in EGF-like proteins. Nature 1991; 351: 164-167
    CrossrefPubMedGoogle Scholar
  • 50 Selander-Sunnerhagen M, Ullner M, Persson E, Teleman O, Stenflo J, Drakenberg T. How an epidermal growth factor (EGF)-like domain binds calcium. High resolution nmr structure of the calcium form of the NH2-ter-minal EGF-like domain in coagulation factor X. J Biol Chem 1992; 267:: 19642-19649
    PubMedGoogle Scholar
  • 51 Mayhew M, Handford P, Baron M, Tse AGD, Campbell ID, Brownlee GG. Ligand requirements for Ca2+ binding of EGF-like domains. Protein Eng 1992; 5: 489-494
    CrossrefPubMedGoogle Scholar
  • 52 Hughes PE, Handford PA, Austen DEG, Brownlee GG. Protein engineering of the hydrophobic domain of human factor IX. Protein Eng 1994; 7: 1121-1127
    CrossrefPubMedGoogle Scholar
  • 53 Sridhara S, Clarke BJ, Blajchman MA. Arginine 79 in the 1st epidermal growth factor domain of factor VII is essential for the interaction with tissue factor. Blood Coag Fibrinol 1993; 4: 505-506
    CrossrefPubMedGoogle Scholar
  • 54 Takamiya O, Abe S, Yoshioka A, Nakajima K, McVey JH, Tuddenham EGD. Factor VUShinjo: a dysfunctional factor VII variant homozygous for the substitution gin for arg at position 79. Haemostasis 1995; 25: 89-97
    PubMedGoogle Scholar
  • 55 Ruf W. Factor Vila residue arg(290) is required for efficient activation of the macromolecular substrate factor X. Biochemistry 1994; 33: 11631-11636
    CrossrefPubMedGoogle Scholar
  • 56 Bemardi F, Castaman G, Redaelli R, Pinotti M, Lunghi B, Rodeghiero F, Marchetti G. Topologically equivalent mutations causing dysfunctional coagulation factors VII ((294)Ala-<Val) and X ((334)Ser-<Pro). Hum Mol Genet 1994; 3: 1175-1177
    CrossrefPubMedGoogle Scholar
  • 57 Bemardi F, Liney DL, Patracchini P, Gemmati D, Legnani C, Arcieri P, Pinotti M, Redaelli R, Ballerini G, Pemberton S, Wacey AI, Mariani G, Tuddenham EGD, Marchetti G. Molecular defects in CRM+ factor VII deficiencies. Modeling of missense mutations in the catalytic domain of fVII. Br J Haematol 1994; 86: 610-618
    CrossrefPubMedGoogle Scholar
  • 58 Wildgoose P, Kazim AL, Kisiel W. The importance of residues 195-206 of human blood clotting factor VII in the interaction of factor VII with tissue factor. Proc Natl Acad Sci USA 1990; 87: 7290-7294
    CrossrefPubMedGoogle Scholar