메뉴 건너뛰기




Volumn 75, Issue 3, 1996, Pages 481-487

Characterization of a cDNA encoding murine coagulation factor VII

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 7; COMPLEMENTARY DNA; MESSENGER RNA; NUCLEOTIDE; POLYADENYLATED RNA;

EID: 0029914396     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0038-1650301     Document Type: Article
Times cited : (20)

References (58)
  • 1
    • 0016703356 scopus 로고
    • Isolation and characterization of bovine factor VII
    • Kisiel W, Davie E. Isolation and characterization of bovine factor VII. Biochemistry 1975; 14: 4928-34.
    • (1975) Biochemistry , vol.14 , pp. 4928-4934
    • Kisiel, W.1    Davie, E.2
  • 4
    • 0025010978 scopus 로고
    • Proteolytic activation of human factors IX and X by recombinant human factor VIIa: Effects of calcium, phospholipid and tissue factor
    • Komiyama Y, Pedersen AH, Kisiel W. Proteolytic activation of human factors IX and X by recombinant human factor VIIa: Effects of calcium, phospholipid and tissue factor. Biochemistry 1990; 29: 9418-25.
    • (1990) Biochemistry , vol.29 , pp. 9418-9425
    • Komiyama, Y.1    Pedersen, A.H.2    Kisiel, W.3
  • 6
    • 0024834211 scopus 로고
    • Mechanism by which recombinant factor VIIa shortens the aPTT: Activation of factor X in the absence of tissue factor
    • Teglt DSC, Macik BG, McCord DM, Monroe D, Roberts HR. Mechanism by which recombinant factor VIIa shortens the aPTT: Activation of factor X in the absence of tissue factor. Thromb Res 1989; 56: 603-9.
    • (1989) Thromb Res , vol.56 , pp. 603-609
    • Teglt, D.S.C.1    Macik, B.G.2    McCord, D.M.3    Monroe, D.4    Roberts, H.R.5
  • 7
    • 0018731365 scopus 로고
    • Activation of human factor VII in plasma and in purified systems. Roles of activated factor IX, kallikrein, and activated factor XII
    • 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: 1056-65.
    • (1979) J Clin Invest , vol.64 , pp. 1056-1065
    • Seligsohn, U.1    Osterud, B.2    Brown, S.F.3    Griffin, J.H.4    Rapaport, S.I.5
  • 10
    • 0026355315 scopus 로고
    • Initiation of the extrinsic pathway of blood coagulation: Evidence for the tissue factor dependent autoactivation of human coagulation factor VII
    • 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: 10819-24.
    • (1991) Biochemistry , vol.30 , pp. 10819-10824
    • Nakagaki, T.1    Foster, D.C.2    Berkner, K.L.3    Kisiel, W.4
  • 11
    • 0027494426 scopus 로고
    • Factor VII autoactivation proceeds via interaction of distinct protease-cofactor and zymogen-cofactor complexes. Implications of a 2-dimensional enzyme kinetic mechanism
    • 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: 21489-92.
    • (1993) J Biol Chem , vol.268 , pp. 21489-21492
    • Neuenschwander, P.F.1    Fiore, M.M.2    Morrissey, J.H.3
  • 12
    • 0023784390 scopus 로고
    • Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells
    • Thim L, Bjoern S, Christensen M, Nicolaisen EM, Lund-Hansen T, Pedersen AH, Hedner U. Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells. Biochemistry 1988; 27: 7785-93.
    • (1988) Biochemistry , vol.27 , pp. 7785-7793
    • Thim, L.1    Bjoern, S.2    Christensen, M.3    Nicolaisen, E.M.4    Lund-Hansen, T.5    Pedersen, A.H.6    Hedner, U.7
  • 13
    • 0020515543 scopus 로고
    • The occurrence of β-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens
    • McMullen BA, Fujikawa K, Kisiel W. The occurrence of β-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens. Biochem Biophys Res Comm 1983; 115: 8-14.
    • (1983) Biochem Biophys Res Comm , vol.115 , pp. 8-14
    • McMullen, B.A.1    Fujikawa, K.2    Kisiel, W.3
  • 14
    • 0024377258 scopus 로고
    • 2-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
    • 2-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: 20320-5.
    • (1989) J Biol Chem , vol.264 , pp. 20320-20325
    • Nishimura, H.1    Kawabata, S.-I.2    Kisiel, W.3    Hase, S.4    Ikenaka, T.5    Takao, T.6    Shimonishi, Y.7    Iwanaga, S.8
  • 15
    • 0025764566 scopus 로고
    • 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
    • Bjoern 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. 11051-7.
    • (1991) J Biol Chem , vol.266 , pp. 11051-11057
    • Bjoern, S.1    Foster, D.C.2    Thim, L.3    Wiberg, F.C.4    Christensen, M.5    Komiyama, Y.6    Pedersen, A.H.7    Kisiel, W.8
  • 16
  • 17
    • 0022257323 scopus 로고
    • Nucleotide sequence of the gene for human factor IX (antihemophilic factor B)
    • 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.
    • (1985) Biochemistry , vol.24 , pp. 3736-3750
    • Yoshitake, S.1    Schach, B.G.2    Foster, D.C.3    Davie, E.W.4    Kurachi, K.5
  • 18
    • 0022871419 scopus 로고
    • Gene for human factor X: A blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C
    • 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: 5098-102.
    • (1986) Biochemistry , vol.25 , pp. 5098-5102
    • Leytus, S.P.1    Foster, D.C.2    Kurachi, K.3    Davie, E.W.4
  • 19
    • 0004330552 scopus 로고
    • Nucleotide sequence of the gene coding for human factor VII, a vitamin K-dependent protein participating in blood coagulation
    • 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.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 5158-5162
    • O'Hara, P.J.1    Grant, F.J.2    Haldeman, B.A.3    Gray, C.L.4    Insley, M.Y.5    Hagen, F.S.6    Murray, M.J.7
  • 20
    • 0028340150 scopus 로고
    • 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
    • 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: 7355-63.
    • (1994) J Biol Chem , vol.269 , pp. 7355-7363
    • Matsushita, T.1    Kojima, T.2    Emi, N.3    Takahashi, I.4    Satio, H.5
  • 21
    • 0028175691 scopus 로고
    • 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
    • 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: 773-7.
    • (1994) Thromb Haemost , vol.71 , pp. 773-777
    • Ohiwa, M.1    Hayashi, T.2    Wada, H.3    Minamikawa, K.4    Shirakawa, S.5    Suzuki, K.6
  • 22
    • 0026472867 scopus 로고
    • Evidence that factor VII levels correlate strongly with fibrinopeptide A release. Evaluation by an ex vivo method
    • Mariani G, Iacopino G, Pasqualilasagni 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: 111-4.
    • (1992) Int J Clin Lab Res , vol.22 , pp. 111-114
    • Mariani, G.1    Iacopino, G.2    Pasqualilasagni, R.3
  • 24
    • 0028127942 scopus 로고
    • Fibrinogen and factor VII in the prediction of coronary risk. Results from the PROCAM study in healthy men
    • 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: 54-9.
    • (1994) Arterioscler Thromb , vol.14 , pp. 54-59
    • Heinrich, J.1    Balleisen, L.2    Schulte, H.3    Assmann, G.4    Van De Loo, J.5
  • 25
    • 0025860324 scopus 로고
    • A common genetic polymorphism associated with lower coagulation factor VII levels in healthy individuals
    • 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: 540-6.
    • (1991) Arterioscler Thromb , vol.11 , pp. 540-546
    • Green, F.1    Kelleher, C.2    Wilkes, H.3    Temple, A.4    Meade, T.5    Humphries, S.A.6
  • 26
    • 0026716531 scopus 로고
    • Genetic and environmental determinants of factor VII coagulant activity in ethnic groups at differing risk of coronary heat disease
    • 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.
    • (1992) Atherosclerosis , vol.94 , pp. 43-50
    • Lane, A.1    Cruickshank, J.K.2    Mitchell, J.3    Henderson, A.4    Humphries, S.5    Green, F.6
  • 29
    • 0023989064 scopus 로고
    • Improved tools for biological sequence comparison
    • Pearson WR, Lipman DJ. Improved tools for biological sequence comparison Proc Natl Acad Sci USA 1988; 85: 2444-8.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 2444-2448
    • Pearson, W.R.1    Lipman, D.J.2
  • 31
    • 0025598301 scopus 로고
    • 7D) of human activated protein C displays greatly reduced activity as an anticoagulant
    • 7D) of human activated protein C displays greatly reduced activity as an anticoagulant. Biochemistry 1990; 29: 10828-34.
    • (1990) Biochemistry , vol.29 , pp. 10828-10834
    • Zhang, L.1    Castellino, F.J.2
  • 32
    • 0027303971 scopus 로고
    • A PCR-based method for high stringency screening of DNA libraries
    • Israel DI. A PCR-based method for high stringency screening of DNA libraries. Nucl Acids Res 1993; 21: 2627-31.
    • (1993) Nucl Acids Res , vol.21 , pp. 2627-2631
    • Israel, D.I.1
  • 33
    • 0025774601 scopus 로고
    • Construction, expression and purification of recombinant kringle 1 of human plasminogen and analysis of its interaction with ω-amino acids
    • 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 ω-amino acids. Biochemistry 1991; 30: 1948-57.
    • (1991) Biochemistry , vol.30 , pp. 1948-1957
    • Menhart, N.1    Sehl, L.C.2    Kelley, R.F.3    Castellino, F.J.4
  • 34
    • 0026566331 scopus 로고
    • The expression, purification and characterization of the recombinant kringle 1 domain from tissue-type plasminogen activator
    • 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: 282-90.
    • (1992) Arch Biochem Biophys , vol.294 , pp. 282-290
    • De Serrano, V.S.1    Menhart, N.2    Castellino, F.J.3
  • 35
    • 0026606375 scopus 로고
    • The role of tryptophan-74 of the recombinant kringel 2 domain of tissue-type plasminogen activator in its ω-amino acid binding properties
    • De Serrano VS, Castellino FJ. The role of tryptophan-74 of the recombinant kringel 2 domain of tissue-type plasminogen activator in its ω-amino acid binding properties. Biochemistry 1992; 31: 3326-35.
    • (1992) Biochemistry , vol.31 , pp. 3326-3335
    • De Serrano, V.S.1    Castellino, F.J.2
  • 37
    • 0019193278 scopus 로고
    • A new computer method for the storage and manipulation of DNA gel reading data
    • Staden E. A new computer method for the storage and manipulation of DNA gel reading data. Nucl Acids Res 1980; 8: 3673-94.
    • (1980) Nucl Acids Res , vol.8 , pp. 3673-3694
    • Staden, E.1
  • 39
    • 0027400886 scopus 로고
    • Complete nucleotide sequence of the cDNA encoding rabbit coagulation factor VII
    • Brothers AB, Clarke BJ, Sheffield WP, Blajchman MA. Complete nucleotide sequence of the cDNA encoding rabbit coagulation factor VII. Thromb Res 1993; 69: 231-8.
    • (1993) Thromb Res , vol.69 , pp. 231-238
    • Brothers, A.B.1    Clarke, B.J.2    Sheffield, W.P.3    Blajchman, M.A.4
  • 40
    • 0028357936 scopus 로고
    • Analysis of the partial nucleotide sequences and deduced primary structures of the protease domains of mammalian blood coagulation factors VII and X
    • 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.
    • (1994) Eur J Haematol , vol.52 , pp. 162-168
    • Murakawa, M.1    Okamura, T.2    Kamura, T.3    Kuroiwa, M.4    Harada, M.5    Niho, Y.6
  • 41
    • 0025370072 scopus 로고
    • Identification of amino acids in the γ-carboxylation recognition site of the propeptide of prothrombin
    • 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: 12467-73.
    • (1990) J Biol Chem , vol.265 , pp. 12467-12473
    • Huber, P.1    Schmitz, T.2    Griffin, J.3    Jacobs, M.4    Walsh, C.5    Furie, B.6    Furie, B.C.7
  • 42
    • 0027968913 scopus 로고
    • 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
    • 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: 3590-5.
    • (1994) J Biol Chem , vol.269 , pp. 3590-3595
    • Zhang, L.1    Castellino, F.J.2
  • 44
    • 0026687609 scopus 로고
    • Role of individual gamma-carboxyglulamic acid residues of activated human protein C in defining its in vitro anticoagulant activitiy
    • Zhang L, Jhingan A, Castellino FJ. Role of individual gamma-carboxyglulamic acid residues of activated human protein C in defining its in vitro anticoagulant activitiy. Blood 1992; 80: 942-52.
    • (1992) Blood , vol.80 , pp. 942-952
    • Zhang, L.1    Jhingan, A.2    Castellino, F.J.3
  • 45
    • 0025881214 scopus 로고
    • Role of the hexapeptide disulfide loop present in the γ-carboxyglutamic acid domain of protein C in its activation properties and in the in vitro anticoagulant activity of activated protein C
    • Zhang L, Castellino FJ. Role of the hexapeptide disulfide loop present in the γ-carboxyglutamic acid domain of protein C in its activation properties and in the in vitro anticoagulant activity of activated protein C. Biochemistry 1991; 30: 6696-704.
    • (1991) Biochemistry , vol.30 , pp. 6696-6704
    • Zhang, L.1    Castellino, F.J.2
  • 46
    • 0029031301 scopus 로고
    • Structure-function assessment of the role of the helical stack domain in the properties of human recombinant protein C and activated protein C
    • 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: 8082-90.
    • (1995) Biochemistry , vol.34 , pp. 8082-8090
    • Christiansen, W.T.1    Geng, J.-P.2    Castellino, F.J.3
  • 47
    • 0028267187 scopus 로고
    • Calcium and phospholipid binding properties of synthetic gamma-carboxyglutamic acid-containing peptides with sequence counterparts in human protein C
    • 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: 3501-8.
    • (1994) Biochemistry , vol.33 , pp. 3501-3508
    • Colpitts, T.L.1    Castellino, F.J.2
  • 48
    • 0028172935 scopus 로고
    • Calcium-dependent interaction between gamma-carboxyglutamic acid-containing and N-terminal epidermal growth factor-like modules in factor X
    • 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: 26011-6.
    • (1994) J Biol Chem , vol.269 , pp. 26011-26016
    • Valcarce, C.1    Holmgren, A.2    Stenflo, J.3
  • 53
    • 0027298331 scopus 로고
    • Arginine 79 in the 1st epidermal growth factor domain of factor VII is essential for the interaction with tissue factor
    • 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: 505-6.
    • (1993) Blood Coag Fibrinol , vol.4 , pp. 505-506
    • Sridhara, S.1    Clarke, B.J.2    Blajchman, M.A.3
  • 54
    • 0028988004 scopus 로고
    • Factor VIIShinjo: A dysfunctional factor VII variant homozygous for the substitution gln for arg at position 79
    • Takamiya O, Abe S, Yoshioka A, Nakajima K, McVey JH, Tuddenham EGD. Factor VIIShinjo: a dysfunctional factor VII variant homozygous for the substitution gln for arg at position 79. Haemostasia 1995; 25: 89-97.
    • (1995) Haemostasia , vol.25 , pp. 89-97
    • Takamiya, O.1    Abe, S.2    Yoshioka, A.3    Nakajima, K.4    McVey, J.H.5    Tuddenham, E.G.D.6
  • 55
    • 0028007436 scopus 로고
    • Factor VIIa residue arg(290) is required for efficient activation of the macromolecular substrate factor X
    • Ruf W. Factor VIIa residue arg(290) is required for efficient activation of the macromolecular substrate factor X Biochemistry 1994; 33: 11631-6.
    • (1994) Biochemistry , vol.33 , pp. 11631-11636
    • Ruf, W.1
  • 56
    • 0028260648 scopus 로고
    • Topologically equivalent mutations causing dysfunctional coagulation factors VII ((294)Ala->Val) and X ((334)Ser->Pro)
    • Bernardi 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: 1175-7
    • (1994) Hum Mol Genet , vol.3 , pp. 1175-1177
    • Bernardi, F.1    Castaman, G.2    Redaelli, R.3    Pinotti, M.4    Lunghi, B.5    Rodeghiero, F.6    Marchetti, G.7
  • 58
    • 0025162863 scopus 로고
    • The importance of residues 195-206 of human blood clotting factor VII in the interaction of factor VII with tissue factor
    • 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: 7290-4.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7290-7294
    • Wildgoose, P.1    Kazim, A.L.2    Kisiel, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.