PDF herunterladen
Thromb Haemost 1996; 76(06): 0957-0964
DOI: 10.1055/s-0038-1650692
Original Article
Schattauer GmbH Stuttgart

Nucleotide Structure and Characterization of the Murine Blood Coagulation Factor VII Gene

Esohe Idusogie
1   The Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, USA
2   The Center for Transgene Research, University of Notre Dame, Notre Dame, IN, USA
,
Elliot D Rosen
1   The Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN, USA
2   The Center for Transgene Research, University of Notre Dame, Notre Dame, IN, USA
,
Peter Carmeliet
3   The Center for Transgene Technology and Gene Therapy, Flanders Interuniversity Institute for Biotechnology, KU Leuven, Belgium
,
Desire Collen
3   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, IN, USA
2   The Center for Transgene Research, University of Notre Dame, Notre Dame, IN, USA
› Institutsangaben
Weitere Informationen

Publikationsverlauf

Received 04. Juni 1996

Accepted after revision 23. August 1996

Publikationsdatum:
11. Juli 2018 (online)

Auch verfügbar auf
  als PDF herunterladen  Lizenzen und Reprints

Summary

The gene encoding murine coagulation factor VII (fVII) has been cloned. Seven introns and eight exons are present, with the introns positioned as splice junctions between the major domain units of the protein. A total of 11,748 bp of the gene was sequenced, and included 1,077 bp of a 5’-flanking region, in which several high probability binding sites for liver transcription factors were present, as well as a CCAAT sequence and possible GC boxes. Primer extension analysis revealed that the major transcription start site was positioned only 9 residues upstream of the ATG initiation codon, thus providing a very short 5’-untranslated region of the gene. The sequence of the CAP site in the murine fVII gene matched exactly the consensus eukaryotic sequence. A total of 1,484 bp of 3’-flanking nucleotides included a probable polyadenylation site (ATTAAA) and an appropriately positioned downstream consensus sequence (AGTGTTTC) for the efficient formation of a 3’ terminus of mRNA. These results indicate that all elements are present for liver-based transcription of the gene for murine factor VII. The sequence and restriction endonuclease map of this gene will facilitate construction of fVII deficient mice and mice containing mutant fVII genes.

 

  • References

  • 1 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
    CrossrefPubMedSuche in Google Scholar
  • 2 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
    CrossrefPubMedSuche in Google Scholar
  • 3 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
    CrossrefPubMedSuche in Google Scholar
  • 4 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
    CrossrefPubMedSuche in Google Scholar
  • 5 Chang JY, Stafford DW, Straight DL. The roles of factor VII’s structural domains in tissue factor binding. Biochemistry 1995; 34: 12227-12232
    CrossrefPubMedSuche in Google Scholar
  • 6 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
    PubMedSuche in Google Scholar
  • 7 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
    CrossrefPubMedSuche in Google Scholar
  • 8 Idusogie E, Rosen E, Geng J-P, Carmeliet P, Collen D, Castellino FJ. Characterization of a cDNA encoding murine coagulation factor VII. Thromb Haemost 1996; 75: 481-487
    Thieme ConnectPubMedSuche in Google Scholar
  • 9 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
    CrossrefPubMedSuche in Google Scholar
  • 10 Chaing S, Clarke B, Sridhara S, Chu K, Friedman P, Van Dusen W, Roberts HR, Blajchman M, Monroe DM, High KA. Severe factor VII deficiency caused by mutations abolishing the cleavage site for activation and altering binding to tissue factor. Blood 1994; 83: 3524-3535
    PubMedSuche in Google Scholar
  • 11 O’Brien DP, Gale KM, Anderson JS, McVey JA, Miller GJ, Meade TW, Tuddenham EGD. Purification and characterization of factor VII304 Glu: a variant molecule with reduced activity isolated from a clinically unaffected male. Blood 1991; 78: 132-140
    PubMedSuche in Google Scholar
  • 12 Ohiwa M, Hayashi T, Wada H, Minamikawa K, Shirakawa S, Suzuki K. Factor VIIMIE. 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
    PubMedSuche in Google Scholar
  • 13 Mariani G, Iacopino G, Pasquali-Lasagni R. Evidence that factor VII levels correlate strongly with fibrinopeptide A release. Evaluation by an ex vivo method. Int J Clin Lab Res 1992; 22: 111-114
    PubMedSuche in Google Scholar
  • 14 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
    PubMedSuche in Google Scholar
  • 15 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
    PubMedSuche in Google Scholar
  • 16 Kario K, Miyata T, Sakata T, Matsuo T, Kato H. Fluorogenic assay of activated factor VII. Plasma factor Vila levels in relation to arterial cardiovascular diseases in Japanese. Arterioscler Thromb 1994; 14: 265-274
    PubMedSuche in Google Scholar
  • 17 Kario K, Narita N, Matsuo T, Kayaba K, Tsutsumi A, Matsuo M, Miyata T, Shimada K. Genetic determinants of plasma factor VII activity in the Japanese. Thromb Haemost 1995; 73: 617-622
    Thieme ConnectPubMedSuche in Google Scholar
  • 18 Green F, Kelleher C, Wilkes H, Temple A, Meade T, Humphries S. A common genetic polymorphism associated with lower coagulation factor VII levels in healthy individuals. Arterioscler Thromb 1991; 11: 540-546
    CrossrefPubMedSuche in Google Scholar
  • 19 Lane A, Cruickshank JK, Mitchell J, Henderson A, Humphries S, Green F. Genetic and developmental determinants of factor VII coagulant activity in ethnic groups at differing risk of coronary heart disease. Atherosclerosis 1992; 94: 43-50
    CrossrefPubMedSuche in Google Scholar
  • 20 Humphries SE, Lane A, Green FR, Cooper J, Miller GJ. Factor VII coagulant activity and antigen levels in healthy men are determined by interaction between factor VII genotype and plasma triglyceride concentration. Arteriosclerosis and Thrombosis 1994; 14: 193-198
    CrossrefPubMedSuche in Google Scholar
  • 21 Zitoun D, Bara L, Basdevant A, Samama MM. Levels of factor VIIc associated with decreased tissue factor pathway inhibitor and increased plasminogen activator inhibitor-1 in dyslipidemias. Arterioscler Thromb Vase Biol 1996; 16: 77-81
    CrossrefPubMedSuche in Google Scholar
  • 22 Benton WD, Davis RW. Screening lgt recombinant clones by hybridization to single plaques in situ. Science 1977; 196: 180-182
    CrossrefPubMedSuche in Google Scholar
  • 23 Chirgwin JJ, Przbyla AE, MacDonald RJ, Rutter WJ. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 1979; 18: 5294-5299
    CrossrefPubMedSuche in Google Scholar
  • 24 Chomczynski P, Sacchi N. Single-step method for RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987; 162: 156-159
    PubMedSuche in Google Scholar
  • 25 Quandt K, Freeh K, Karas H, Wingender E, Werner T. Matlnd and Matln-spector: new fast versatile tools for detection of consensus matches in nucleotide sequence data. Nucl Acids Res 1995; 23: 4878-4884
    CrossrefPubMedSuche in Google Scholar
  • 26 Pearson WR, Lipman DJ. Improved tools for biological sequence comparison. Proc Natl Acad Sci USA 1988; 85: 2444-2448
    CrossrefPubMedSuche in Google Scholar
  • 27 Needleman SB, Wunsch CD. A general method applicable to the search for similarities in the amino acid sequence of two proteins. J Mol Biol 1970; 48: 443-453
    CrossrefPubMedSuche in Google Scholar
  • 28 Kozak M. Compilation and analysis of sequences upstream from the translational start site in eukaryotic mRNAs. Nucl Acids Res 1984; 12: 857-872
    CrossrefPubMedSuche in Google Scholar
  • 29 Bucher P. Weight matrix descriptions of four eukaryotic RNA polymerase II elements derived from 502 unrelated promoter sequences. J Mol Biol 1990; 212: 563-578
    CrossrefPubMedSuche in Google Scholar
  • 30 Javahery R, Khacki A, Lo K, Zenzie-Gregory B, Smale ST. DNA sequence requirements for transcriptional initiator activity in mammalian cells. Mol Cell Biol 1994; 14: 116-127
    CrossrefPubMedSuche in Google Scholar
  • 31 Poliak ES, Hung HL, Godin W, Overton GC, High KA. Functional characterization of the human factor VII 5’-flanking region. J Bio Chem 1996; 271: 1738-1747
    CrossrefPubMedSuche in Google Scholar
  • 32 Miao CH, Leytus SP, Chung DW, Davie EW. Liver-specific expression of the gene coding for human factor X, a blood coagulation factor. J Biol Chem 1992; 267: 7395-7401
    PubMedSuche in Google Scholar
  • 33 Salier J-P, Hirosawa S, Kurachi K. Functional characterization of the 5’-regulatory region of human factor IX gene. J Biol Chem 1990; 265: 7062-7068
    PubMedSuche in Google Scholar
  • 34 Swick AG, Blake MC, Kahn JW, Azizkhan JC. Functional analysis of GC element binding and transcription in the hamster dihydrofolate reductase gene promoter. Nucl Acids Res 1989; 17: 9291-9304
    CrossrefPubMedSuche in Google Scholar
  • 35 Kadonaga JT, Jones KA, Tijan R. Promoter-specific activation of RNA polymerase II transcription by SP1. Trends Biochem Sci 1986; 11: 20-23
    CrossrefPubMedSuche in Google Scholar
  • 36 Huang N-M, Hung H-L, Stanfield-Oakley SA, High KA. Characterization of the human blood coagulation factor X promoter. J Biol Chem 1992; 267: 15440-15448
    PubMedSuche in Google Scholar
  • 37 Erdmann D, Heim J. Orphan nuclear receptor HNF-4 binds to the human factor VII promoter. J Biol Chem 1995; 270: 22988-22996
    CrossrefPubMedSuche in Google Scholar
  • 38 Greenberg D, Miao CH, Ho WT, Chung DW, Davie EW. Liver-specific expression of the human factor VII gene. Proc Natl Acad Sci USA 1995; 92: 12347-12351
    CrossrefPubMedSuche in Google Scholar
  • 39 McPherson CE, Shim E-Y, Friedman DS, Zaret KS. An active tissue-specific enhancer and bound transcription factors existing in a precisely positioned nucleosomal array. Cell 1993; 75: 387-398
    CrossrefPubMedSuche in Google Scholar
  • 40 Hardon EM, Frain M, Paonessa G, Cortese R. Two distinct factors interact with the promoter regions of several liver-specific genes. EMBO J 1988; 7: 1711-1719
    PubMedSuche in Google Scholar
  • 41 Chow BK-C, Ting V, Tufaro F, MacGillivray RTA. Characterization of a novel liver-specific enhancer in the human prothrombin gene. J Biol Chem 1991; 266: 18927-18933
    PubMedSuche in Google Scholar
  • 42 Ullrich A, Gray A, Goeddel DV, Dull TJ. Nucleotide sequence of a portion of human chromosome 9 containing aleukocyte interferon gene cluster. J Mol Biol 1982; 156: 467-486
    CrossrefPubMedSuche in Google Scholar
  • 43 McLauchlan J, Gaffney D, Whitton JL, Clements JB. The consensus sequence YGTGTTYY located downstream from the AATAAA signal is required for efficient formation of mRNA 3’ termini. Nucl Acids Res 1985; 13: 1347-1368
    CrossrefPubMedSuche in Google Scholar
  • 44 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
    CrossrefPubMedSuche in Google Scholar
  • 45 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
    CrossrefPubMedSuche in Google Scholar
  • 46 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
    CrossrefPubMedSuche in Google Scholar