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Volumn 87, Issue 3, 1996, Pages 1006-1012

Molecular and cellular basis for type I heparin cofactor II deficiency (heparin cofactor II Awaji)

Author keywords

[No Author keywords available]

Indexed keywords

HEPARIN COFACTOR II; MUTANT PROTEIN;

EID: 0030062348     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v87.3.1006.bloodjournal8731006     Document Type: Article
Times cited : (22)

References (29)
  • 1
    • 0019362162 scopus 로고
    • Detection of a new heparin-dependent inhibitor of thrombin in human plasma
    • Tollefsen DM, Blank MK: Detection of a new heparin-dependent inhibitor of thrombin in human plasma. J Clin Invest 68:589, 1981
    • (1981) J Clin Invest , vol.68 , pp. 589
    • Tollefsen, D.M.1    Blank, M.K.2
  • 2
    • 0002061080 scopus 로고
    • Antithrombin and related inhibitors of coagulation proteinases
    • Barrett AJ, Salvesen G (eds): Amsterdam, The Netherlands, Elsevier
    • Björk I, Danielsson Å: Antithrombin and related inhibitors of coagulation proteinases, in Barrett AJ, Salvesen G (eds): Proteinase Inhibitors. Amsterdam, The Netherlands, Elsevier, 1986, p 489
    • (1986) Proteinase Inhibitors , pp. 489
    • Björk, I.1    Danielsson, Å.2
  • 3
    • 0020617887 scopus 로고
    • Activation of heparin cofactor II by dermatan sulfate
    • Tollefsen DM, Pestka CA, Monafo WJ: Activation of heparin cofactor II by dermatan sulfate. J Biol Chem 258:6713, 1983
    • (1983) J Biol Chem , vol.258 , pp. 6713
    • Tollefsen, D.M.1    Pestka, C.A.2    Monafo, W.J.3
  • 4
    • 0022639105 scopus 로고
    • A new member of the plasma protease inhibitor gene family
    • Ragg H: A new member of the plasma protease inhibitor gene family. Nucleic Acids Res 14:1073, 1986
    • (1986) Nucleic Acids Res , vol.14 , pp. 1073
    • Ragg, H.1
  • 5
    • 0024297509 scopus 로고
    • Heparin cofactor II: CDNA sequence, chromosome localization, restriction length polymorphism, and expression in Escherichia coli
    • Blinder MA, Marasa JC, Reynolds CH, Deaven LL, Tollefsen DM: Heparin cofactor II: cDNA sequence, chromosome localization, restriction length polymorphism, and expression in Escherichia coli. Biochemistry 27:752, 1988
    • (1988) Biochemistry , vol.27 , pp. 752
    • Blinder, M.A.1    Marasa, J.C.2    Reynolds, C.H.3    Deaven, L.L.4    Tollefsen, D.M.5
  • 6
    • 0022998259 scopus 로고
    • Identification of two sites of sulfation of human heparin cofactor II
    • Hortin G, Tollefsen DM, Strauss AW: Identification of two sites of sulfation of human heparin cofactor II. J Biol Chem 261:15827, 1986
    • (1986) J Biol Chem , vol.261 , pp. 15827
    • Hortin, G.1    Tollefsen, D.M.2    Strauss, A.W.3
  • 7
    • 0023723149 scopus 로고
    • Structure and expression of the gene coding for the human serpin hLS2
    • Ragg H, Preibisch G: Structure and expression of the gene coding for the human serpin hLS2. J Biol Chem 263:12129, 1988
    • (1988) J Biol Chem , vol.263 , pp. 12129
    • Ragg, H.1    Preibisch, G.2
  • 8
    • 0025891865 scopus 로고
    • Complete nucleotide sequence of the gene for human heparin cofactor II and mapping to chromosomal band 22q11
    • Herzog R, Lutz S, Blin N, Marasa JC, Blinder MA, Tollefsen DM: Complete nucleotide sequence of the gene for human heparin cofactor II and mapping to chromosomal band 22q11. Biochemistry 30:1350, 1991
    • (1991) Biochemistry , vol.30 , pp. 1350
    • Herzog, R.1    Lutz, S.2    Blin, N.3    Marasa, J.C.4    Blinder, M.A.5    Tollefsen, D.M.6
  • 10
    • 0024478248 scopus 로고
    • Heparin cofactor II Oslo: Mutation of Arg-189 to His decreases the affinity for dermatan sulfate
    • Blinder MA, Andersson TR, Ablidgaard U, Tollefsen DM: Heparin cofactor II Oslo: Mutation of Arg-189 to His decreases the affinity for dermatan sulfate. J Biol Chem 264:5128, 1989
    • (1989) J Biol Chem , vol.264 , pp. 5128
    • Blinder, M.A.1    Andersson, T.R.2    Ablidgaard, U.3    Tollefsen, D.M.4
  • 12
    • 0021995981 scopus 로고
    • Association of hereditary heparin co-factor II deficiency with thrombosis
    • Tran TH, Marbert GA, Duckert F: Association of hereditary heparin co-factor II deficiency with thrombosis. Lancet 2:413, 1985
    • (1985) Lancet , vol.2 , pp. 413
    • Tran, T.H.1    Marbert, G.A.2    Duckert, F.3
  • 13
    • 0021995982 scopus 로고
    • Constitutional heparin co-factor II deficiency associated with recurrent thrombosis
    • Sie P, Dupouy D, Pichon J, Boneu B: Constitutional heparin co-factor II deficiency associated with recurrent thrombosis. Lancet 2:414, 1985
    • (1985) Lancet , vol.2 , pp. 414
    • Sie, P.1    Dupouy, D.2    Pichon, J.3    Boneu, B.4
  • 14
    • 0025979231 scopus 로고
    • Recurrent venous thrombosis associated with inherited deficiency of heparin cofactor II
    • Weisdorf DJ, Edson JR: Recurrent venous thrombosis associated with inherited deficiency of heparin cofactor II. Br J Haematol 77:125, 1991
    • (1991) Br J Haematol , vol.77 , pp. 125
    • Weisdorf, D.J.1    Edson, J.R.2
  • 16
    • 0021688518 scopus 로고
    • Purification and biological property of heparin cofactor II: Activation of heparin cofactor II and antithrombin III by dextran sulfate and various glycosaminoglycans
    • Yamagishi R, Niwa M, Kondo S, Sakuragawa N, Koide T: Purification and biological property of heparin cofactor II: Activation of heparin cofactor II and antithrombin III by dextran sulfate and various glycosaminoglycans. Thromb Res 36:633, 1984
    • (1984) Thromb Res , vol.36 , pp. 633
    • Yamagishi, R.1    Niwa, M.2    Kondo, S.3    Sakuragawa, N.4    Koide, T.5
  • 17
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C, Okayama H: High-efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol 7:2745, 1987
    • (1987) Mol Cell Biol , vol.7 , pp. 2745
    • Chen, C.1    Okayama, H.2
  • 18
    • 0023850352 scopus 로고
    • SRα promoter: An efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and R-U5 segment of human T-cell leukemia virus type 1 long terminal repeat
    • Takebe Y, Seiki M, Fujikawa J, Hoy P, Yokota K, Arai K, Yoshida M, Arai N: SRα promoter: An efficient and versatile mammalian cDNA expression system composed of the simian virus 40 early promoter and R-U5 segment of human T-cell leukemia virus type 1 long terminal repeat. Mol Cell Biol 8:466, 1988
    • (1988) Mol Cell Biol , vol.8 , pp. 466
    • Takebe, Y.1    Seiki, M.2    Fujikawa, J.3    Hoy, P.4    Yokota, K.5    Arai, K.6    Yoshida, M.7    Arai, N.8
  • 19
    • 0028908684 scopus 로고
    • Warfarin causes the degradation of protein C precursor in the endoplasmic reticulum
    • Tokunaga F, Wakabayashi S, Koide T: Warfarin causes the degradation of protein C precursor in the endoplasmic reticulum. Biochemistry 34:1163, 1995
    • (1995) Biochemistry , vol.34 , pp. 1163
    • Tokunaga, F.1    Wakabayashi, S.2    Koide, T.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680, 1970
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 21
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G: Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368, 1987
    • (1987) Anal Biochem , vol.166 , pp. 368
    • Schägger, H.1    Von Jagow, G.2
  • 22
    • 0023278398 scopus 로고
    • The use of biotinylated monoclonal antibodies and streptoavidin affinity chromatography to isolate herpesvirus hydrophobic proteins or glycoproteins
    • Gretch DR, Suter M, Stinski MF: The use of biotinylated monoclonal antibodies and streptoavidin affinity chromatography to isolate herpesvirus hydrophobic proteins or glycoproteins. Anal Biochem 163:270, 1987
    • (1987) Anal Biochem , vol.163 , pp. 270
    • Gretch, D.R.1    Suter, M.2    Stinski, M.F.3
  • 23
    • 0026088567 scopus 로고
    • Chromogenic substrates for horse-radish peroxidase
    • Conyers SM, Kidwell DA: Chromogenic substrates for horse-radish peroxidase. Anal Biochem 192:207, 1991
    • (1991) Anal Biochem , vol.192 , pp. 207
    • Conyers, S.M.1    Kidwell, D.A.2
  • 24
    • 0011858261 scopus 로고
    • The molecular basis of quantitative antithrombin deficiency in 8 unrelated families
    • abstr
    • Daly DM, Perry DJ, Harper PL, Carrell RW: The molecular basis of quantitative antithrombin deficiency in 8 unrelated families. Br J Haematol 80:15, 1992 (abstr)
    • (1992) Br J Haematol , vol.80 , pp. 15
    • Daly, D.M.1    Perry, D.J.2    Harper, P.L.3    Carrell, R.W.4
  • 25
    • 0025789987 scopus 로고
    • The N-terminal acidic domain of heparin cofactor II mediates the inhibition of α-thrombin in the presence of glycosaminoglycans
    • Van Deerlin VMD, Tollefsen DM: The N-terminal acidic domain of heparin cofactor II mediates the inhibition of α-thrombin in the presence of glycosaminoglycans. J Biol Chem 266:20223, 1991
    • (1991) J Biol Chem , vol.266 , pp. 20223
    • Van Deerlin, V.M.D.1    Tollefsen, D.M.2
  • 26
    • 0025294486 scopus 로고
    • Mechanism of the lack of induction of UDP-glucuronosyltransferase activity in Gunn rats by 3-methylcholanthrene: Identification of a truncated enzyme
    • ElAwady M, Chowdhury JR, Kesari K, van Es H, Jansen PLM, Lederstein M, Arias IM, Chowdhury NR: Mechanism of the lack of induction of UDP-glucuronosyltransferase activity in Gunn rats by 3-methylcholanthrene: Identification of a truncated enzyme. J Biol Chem 265:10752, 1990
    • (1990) J Biol Chem , vol.265 , pp. 10752
    • Elawady, M.1    Chowdhury, J.R.2    Kesari, K.3    Van Es, H.4    Jansen, P.L.M.5    Lederstein, M.6    Arias, I.M.7    Chowdhury, N.R.8
  • 27
    • 0024517692 scopus 로고
    • 2-plasmin inhibitor: A frameshift mutation leading to elongation of the deduced amino acid sequence
    • 2-plasmin inhibitor: A frameshift mutation leading to elongation of the deduced amino acid sequence. J Clin Invest 83:1598, 1989
    • (1989) J Clin Invest , vol.83 , pp. 1598
    • Miura, O.1    Hirosawa, S.2    Kato, A.3    Aoki, N.4
  • 28
    • 0026580101 scopus 로고
    • Secretion of α1-proteinase inhibitor requires an almost full length of molecule
    • Brodbeck RM, Brown JL. Secretion of α1-proteinase inhibitor requires an almost full length of molecule. J Biol Chem 267:294, 1992
    • (1992) J Biol Chem , vol.267 , pp. 294
    • Brodbeck, R.M.1    Brown, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.