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Volumn 77, Issue 4, 1997, Pages 610-615

Compound heterozygosity for two novel missense mutations in the prothrombin gene in a patient with a severe bleeding tendency

Author keywords

[No Author keywords available]

Indexed keywords

PROTHROMBIN;

EID: 0030891620     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0038-1656020     Document Type: Article
Times cited : (16)

References (46)
  • 1
    • 0001630993 scopus 로고
    • Physiology and biochemistry of prothrombin
    • Bloom AL, Forbes CD, Thomas DP, Tuddenham EGD (eds). Edinburgh: Churchill Livingstone (3th ed)
    • Jackson CM. Physiology and biochemistry of prothrombin. In: Haemostasis and Thrombosis, vol 1. Bloom AL, Forbes CD, Thomas DP, Tuddenham EGD (eds). Edinburgh: Churchill Livingstone (3th ed) 1994: 397-438.
    • (1994) Haemostasis and Thrombosis , vol.1 , pp. 397-438
    • Jackson, C.M.1
  • 2
    • 0020584329 scopus 로고
    • Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin
    • Degen SJF, MacGillivray RTA, Davie EW. Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin. Biochem 1983; 22: 2087-97.
    • (1983) Biochem , vol.22 , pp. 2087-2097
    • Degen, S.J.F.1    MacGillivray, R.T.A.2    Davie, E.W.3
  • 3
    • 0023230641 scopus 로고
    • Nucleotide sequence of the gene for human prothrombin
    • Degen SJF, Davie EW. Nucleotide sequence of the gene for human prothrombin. Biochem 1987; 26: 6165-77.
    • (1987) Biochem , vol.26 , pp. 6165-6177
    • Degen, S.J.F.1    Davie, E.W.2
  • 6
    • 0020606807 scopus 로고
    • Determination of the amino acid substitution in human prothrombin type 3 (157 glu-to-lys) and the localization of a third thrombin cleavage site
    • Board PG, Shaw DC. Determination of the amino acid substitution in human prothrombin type 3 (157 glu-to-lys) and the localization of a third thrombin cleavage site. Brit J Haematol 1983; 54: 245-54.
    • (1983) Brit J Haematol , vol.54 , pp. 245-254
    • Board, P.G.1    Shaw, D.C.2
  • 7
    • 0022978454 scopus 로고
    • Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273
    • Rabiet MJ, Furie BC, Furie B. Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273. J Biol Chem 1986; 261: 15045-8.
    • (1986) J Biol Chem , vol.261 , pp. 15045-15048
    • Rabiet, M.J.1    Furie, B.C.2    Furie, B.3
  • 8
    • 1842323215 scopus 로고
    • Molecular defect of prothrombin Madrid. Substitution of arginine 273 by cysteine precludes activation
    • abstract
    • Rabiet MJ, Furie BC, Furie B. Molecular defect of prothrombin Madrid. Substitution of arginine 273 by cysteine precludes activation. Thromb Haemost 1987; 58: 313 (abstract).
    • (1987) Thromb Haemost , vol.58 , pp. 313
    • Rabiet, M.J.1    Furie, B.C.2    Furie, B.3
  • 9
    • 0023148572 scopus 로고
    • Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that impairs the fibrinogen clotting activity of derived thrombin Tokushima
    • Miyata T, Monta T, Inomoto T, Kawauchi A, Shirakami A, Iwanaga S. Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that impairs the fibrinogen clotting activity of derived thrombin Tokushima. Biochem 1987; 26: 1117-22.
    • (1987) Biochem , vol.26 , pp. 1117-1122
    • Miyata, T.1    Monta, T.2    Inomoto, T.3    Kawauchi, A.4    Shirakami, A.5    Iwanaga, S.6
  • 10
    • 0001820093 scopus 로고
    • Introduction to hemostasis and the vitamin K-dependent coagulation factors
    • Scriver CR, Beaudet AL, Sly WS, Valle D (eds). New York: McGraw-Hill (6th ed)
    • Hedner U, Davie EW. Introduction to hemostasis and the vitamin K-dependent coagulation factors. In: The metabolic basis of inherited disease, Vol II. Scriver CR, Beaudet AL, Sly WS, Valle D (eds). New York: McGraw-Hill (6th ed) 1989: 2107-34.
    • (1989) The Metabolic Basis of Inherited Disease , vol.2 , pp. 2107-2134
    • Hedner, U.1    Davie, E.W.2
  • 11
    • 0024232172 scopus 로고
    • Identification of the primary structural defect in the dysthrombin thrombin Quick-I. Substitution of cysteine for arginine-382
    • Henriksen RA, Mann KG. Identification of the primary structural defect in the dysthrombin thrombin Quick-I. Substitution of cysteine for arginine-382. Biochem 1988; 27: 9160-5.
    • (1988) Biochem , vol.27 , pp. 9160-9165
    • Henriksen, R.A.1    Mann, K.G.2
  • 12
    • 0024553003 scopus 로고
    • Substitution of valine for glycin-558 in the congenital dysthrombin Quick-II alters primary substrate specificity
    • Henriksen RA, Mann KG. Substitution of valine for glycin-558 in the congenital dysthrombin Quick-II alters primary substrate specificity. Biochem 1989; 28: 2078-82.
    • (1989) Biochem , vol.28 , pp. 2078-2082
    • Henriksen, R.A.1    Mann, K.G.2
  • 13
    • 0026794281 scopus 로고
    • Prothrombin Himi: A compound heterozygote for two dysfunctional prothrombin molecules (Met-337 → Thr and Arg-388 → His)
    • Morishita E, Saito M, Kumabushiri I, Asakura H, Matsuda T, Yamaguchi K. Prothrombin Himi: a compound heterozygote for two dysfunctional prothrombin molecules (Met-337 → Thr and Arg-388 → His). Blood 1992; 80: 2275-80.
    • (1992) Blood , vol.80 , pp. 2275-2280
    • Morishita, E.1    Saito, M.2    Kumabushiri, I.3    Asakura, H.4    Matsuda, T.5    Yamaguchi, K.6
  • 14
    • 0026785554 scopus 로고
    • Prothrombin Salakta. Substitution of glumatic acid -466 by alanine reduces the fibrinogen clotting activity and the esterase activity
    • Miyata T, Aruga R, Umeyama H, Bezeaud A, Guillin MC, Iwanaga S. Prothrombin Salakta. Substitution of glumatic acid -466 by alanine reduces the fibrinogen clotting activity and the esterase activity. Biochem 1992; 31: 7457-62.
    • (1992) Biochem , vol.31 , pp. 7457-7462
    • Miyata, T.1    Aruga, R.2    Umeyama, H.3    Bezeaud, A.4    Guillin, M.C.5    Iwanaga, S.6
  • 15
    • 0028984375 scopus 로고
    • Prothrombin Frankfurt: A dysfunctional prothrombin characterized by substitution of glu-466 by ala
    • Degen SJF, McDowell SA, Sparks LM, Scharrer I. Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of glu-466 by ala. Thromb Haemost 1995; 73: 203-9.
    • (1995) Thromb Haemost , vol.73 , pp. 203-209
    • Degen, S.J.F.1    McDowell, S.A.2    Sparks, L.M.3    Scharrer, I.4
  • 17
    • 0026749548 scopus 로고
    • Molecular and genetic analysis of a compound heterozygote for dysprothrombinemia of prothrombin Tokushima and hypoprothrombinemia
    • Iwahana H, Yoshimoto K, Shigekiyo T, Shirakami A, Saito S, Itakura M. Molecular and genetic analysis of a compound heterozygote for dysprothrombinemia of prothrombin Tokushima and hypoprothrombinemia. Am J Hum Genet 1992; 51: 1386-95.
    • (1992) Am J Hum Genet , vol.51 , pp. 1386-1395
    • Iwahana, H.1    Yoshimoto, K.2    Shigekiyo, T.3    Shirakami, A.4    Saito, S.5    Itakura, M.6
  • 18
    • 0028650365 scopus 로고
    • Homozygosity for a novel missense mutation in the prothrombin gene causing a severe bleeding disorder
    • Poort SR, Michiels JJ, Reitsma PH, Bertina RM. Homozygosity for a novel missense mutation in the prothrombin gene causing a severe bleeding disorder. Thromb Haemost 1994; 72: 819-24.
    • (1994) Thromb Haemost , vol.72 , pp. 819-824
    • Poort, S.R.1    Michiels, J.J.2    Reitsma, P.H.3    Bertina, R.M.4
  • 23
    • 1842321275 scopus 로고
    • Expression, isolation and characterization of biologically active γ-carboxylated recombinant human prothrombin
    • Abstr. 1637
    • Jorgensen MJ, Cantor AB, Furie BC, Furie B. Expression, isolation and characterization of biologically active γ-carboxylated recombinant human prothrombin. Circulation 1986; 74 (suppl. II): Abstr. 1637.
    • (1986) Circulation , vol.74 , Issue.2 SUPPL.
    • Jorgensen, M.J.1    Cantor, A.B.2    Furie, B.C.3    Furie, B.4
  • 25
    • 0026598028 scopus 로고
    • Highly polymorphic region of the human prothrombin (F2) gene
    • Iwahana H, Yoshimoto K, Itakura M. Highly polymorphic region of the human prothrombin (F2) gene. Hum Genet 1992; 89: 123-4.
    • (1992) Hum Genet , vol.89 , pp. 123-124
    • Iwahana, H.1    Yoshimoto, K.2    Itakura, M.3
  • 26
  • 27
    • 0010960692 scopus 로고
    • The primary structure of prothrombin, the role of vitamin K in blood coagulation and a thrombin-catalyzed "negative feedback" control mechanism for limiting the activation of prothrombin
    • Hemker HC, Veltkamp JJ (eds). Leiden University Press
    • Magnesson S, Sottrup-Jensen L, Petersen TE, Claeys H. The primary structure of prothrombin, the role of vitamin K in blood coagulation and a thrombin-catalyzed "negative feedback" control mechanism for limiting the activation of prothrombin. In: Prothrombin and related coagulation factors. Hemker HC, Veltkamp JJ (eds). Leiden University Press 1975; 25.
    • (1975) Prothrombin and Related Coagulation Factors , pp. 25
    • Magnesson, S.1    Sottrup-Jensen, L.2    Petersen, T.E.3    Claeys, H.4
  • 28
    • 0022102222 scopus 로고
    • Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules
    • Patthy L. Evolution of the proteases of blood coagulation and fibrinolysis by assembly from modules. Cell 1985; 41: 657-63.
    • (1985) Cell , vol.41 , pp. 657-663
    • Patthy, L.1
  • 32
    • 0025938869 scopus 로고
    • Characterization of the DNF15S2 locus on human chromosome 3: Identification of a gene coding for four kringle domains with homology to hepatocyte growth factor
    • Han SH, Stuart A, Degen SJF. Characterization of the DNF15S2 locus on human chromosome 3: identification of a gene coding for four kringle domains with homology to hepatocyte growth factor. Biochem 1991; 30: 9768-80.
    • (1991) Biochem , vol.30 , pp. 9768-9780
    • Han, S.H.1    Stuart, A.2    Degen, S.J.F.3
  • 33
    • 0027289115 scopus 로고
    • Molecular cloning and sequence analysis of the cDNA for a human serine protease responsible for activation of hepatocyte growth factor
    • Miyazawa K, Shimomura T, Kitamura A, Kondo J, Morimoto Y, Kitamura N. Molecular cloning and sequence analysis of the cDNA for a human serine protease responsible for activation of hepatocyte growth factor. J Biol Chem 1993; 268: 10024-8.
    • (1993) J Biol Chem , vol.268 , pp. 10024-10028
    • Miyazawa, K.1    Shimomura, T.2    Kitamura, A.3    Kondo, J.4    Morimoto, Y.5    Kitamura, N.6
  • 34
    • 0027400467 scopus 로고
    • Muscle-specific trk-related receptor with a kringle domain defines a distinct class of receptor tyrosine kinases
    • Jennings CGB, Dyer SM, Burden SJ. Muscle-specific trk-related receptor with a kringle domain defines a distinct class of receptor tyrosine kinases. Proc Natl Acad Sci USA 1993; 90: 2895-9.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2895-2899
    • Jennings, C.G.B.1    Dyer, S.M.2    Burden, S.J.3
  • 35
    • 0027205387 scopus 로고
    • Dror, a potential neurotrophic receptor gene, encodes a Drosophila homolog of the vertebrate Ror family of trk-related receptor tyrosine kinases
    • Wilson C, Goberdhan DCI, Steller H. Dror, a potential neurotrophic receptor gene, encodes a Drosophila homolog of the vertebrate Ror family of trk-related receptor tyrosine kinases. Proc Natl Acad Sci USA 1993; 90: 7109-13.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7109-7113
    • Wilson, C.1    Goberdhan, D.C.I.2    Steller, H.3
  • 36
    • 0027409404 scopus 로고
    • A player of many parts: The spotlight falls on thrombin's structure
    • Stubbs MT, Bode W. A player of many parts: the spotlight falls on thrombin's structure. Thromb Res 1993; 69: 1-58.
    • (1993) Thromb Res , vol.69 , pp. 1-58
    • Stubbs, M.T.1    Bode, W.2
  • 37
    • 0023944299 scopus 로고
    • Lysine/fibrin binding sites of kringle modeled after the structure of kringle 1 of prothrombin
    • Tulinsky A, Park CH, Mao B, Llinas M. Lysine/fibrin binding sites of kringle modeled after the structure of kringle 1 of prothrombin. Proteins 1988; 3: 85-96.
    • (1988) Proteins , vol.3 , pp. 85-96
    • Tulinsky, A.1    Park, C.H.2    Mao, B.3    Llinas, M.4
  • 38
    • 0025770980 scopus 로고
    • The structure of domains of blood proteins
    • Tulinsky A. The structure of domains of blood proteins. Thromb Haemost 1991; 66: 16-31.
    • (1991) Thromb Haemost , vol.66 , pp. 16-31
    • Tulinsky, A.1
  • 43
    • 0344908213 scopus 로고
    • Identification of a thrombin sequence with growth factor activity on macrophages
    • Bar-Shavit R, Kahn AJ, Mann KG, Wilner GD. Identification of a thrombin sequence with growth factor activity on macrophages. Proc Natl Acad Sci USA 1986; 83: 976-80.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 976-980
    • Bar-Shavit, R.1    Kahn, A.J.2    Mann, K.G.3    Wilner, G.D.4
  • 44
    • 0019967085 scopus 로고
    • Progress in laboratory control of oral anticoagulants
    • Loeliger EA, Lewis SM. Progress in laboratory control of oral anticoagulants. Lancet 1982; 2: 318-20.
    • (1982) Lancet , vol.2 , pp. 318-320
    • Loeliger, E.A.1    Lewis, S.M.2
  • 45
    • 0021923839 scopus 로고
    • Reliability and clinical impact of the normalization of the prothrombin times in oral anticoagulant control
    • Loeliger EA, van den Besselaar AMHP, Lewis SM. Reliability and clinical impact of the normalization of the prothrombin times in oral anticoagulant control. Thromb Haemost 1985; 53: 148-54.
    • (1985) Thromb Haemost , vol.53 , pp. 148-154
    • Loeliger, E.A.1    Van Den Besselaar, A.M.H.P.2    Lewis, S.M.3
  • 46
    • 0020512566 scopus 로고
    • Calibration of reference thromboplastins and standardisation of the prothrombin time ratio
    • Kirkwood TBL. Calibration of reference thromboplastins and standardisation of the prothrombin time ratio. Thromb Haemost 1983; 49: 238-44.
    • (1983) Thromb Haemost , vol.49 , pp. 238-244
    • Kirkwood, T.B.L.1


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