메뉴 건너뛰기




Volumn 89, Issue 9, 1997, Pages 3243-3252

Potent antithrombin activity and delayed clearance from the circulation characterize recombinant hirudin genetically fused to albumin

Author keywords

[No Author keywords available]

Indexed keywords

ALBUMIN; ANTITHROMBIN; LEPIRUDIN;

EID: 0030942608     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v89.9.3243     Document Type: Article
Times cited : (104)

References (44)
  • 1
    • 0024416485 scopus 로고
    • Development of hirudin as an antithrombotic agent
    • Markwardt F: Development of hirudin as an antithrombotic agent. Semin Thromb Hemost 15:269, 1991
    • (1991) Semin Thromb Hemost , vol.15 , pp. 269
    • Markwardt, F.1
  • 2
    • 0024445042 scopus 로고
    • Antistasin, a leech-derived inhibitor of factor Xa: Kinetic analysis of enzyme inhibition and identification of the reactive site
    • Dunwiddie CT, Thornberry N, Bull H, Sardana M, Friedman P, Jacobs J, Simpson E: Antistasin, a leech-derived inhibitor of factor Xa: Kinetic analysis of enzyme inhibition and identification of the reactive site. J Biol Chem 264:16694, 1989
    • (1989) J Biol Chem , vol.264 , pp. 16694
    • Dunwiddie, C.T.1    Thornberry, N.2    Bull, H.3    Sardana, M.4    Friedman, P.5    Jacobs, J.6    Simpson, E.7
  • 3
    • 0025375504 scopus 로고
    • Tick anticoagulant peptide is a novel inhibitor of factor Xa
    • Waxman L, Smith DE, Arcuri KE, Vlasuk GP: Tick anticoagulant peptide is a novel inhibitor of factor Xa. Science 248:593, 1990
    • (1990) Science , vol.248 , pp. 593
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3    Vlasuk, G.P.4
  • 4
    • 0028812448 scopus 로고
    • Purification and partial characterization of draculin, the anticoagulant factor present in the saliva of vampire bats (Desmondus rotundus)
    • Apitz-Castro R, Béguin S, Tablante A, Bartoli F, Holt JC, Hemker HC: Purification and partial characterization of draculin, the anticoagulant factor present in the saliva of vampire bats (Desmondus rotundus). Thromb Haemost 73:94, 1994
    • (1994) Thromb Haemost , vol.73 , pp. 94
    • Apitz-Castro, R.1    Béguin, S.2    Tablante, A.3    Bartoli, F.4    Holt, J.C.5    Hemker, H.C.6
  • 6
    • 0022760451 scopus 로고
    • Isolation and characterization of hirudin isoinhibitors and sequence analysis of hirudin PA
    • Dodt T, Machleidt W, Seemueller U, Machlev R, Fritz H: Isolation and characterization of hirudin isoinhibitors and sequence analysis of hirudin PA. Biol Chem Hoppe Seyler 367:803, 1986
    • (1986) Biol Chem Hoppe Seyler , vol.367 , pp. 803
    • Dodt, T.1    Machleidt, W.2    Seemueller, U.3    Machlev, R.4    Fritz, H.5
  • 7
    • 0022521744 scopus 로고
    • Kinetics of the inhibition of thrombin by hirudin
    • Stone RS, Hofsteenge J: Kinetics of the inhibition of thrombin by hirudin. Biochemistry 25:4622, 1986
    • (1986) Biochemistry , vol.25 , pp. 4622
    • Stone, R.S.1    Hofsteenge, J.2
  • 10
    • 0024451152 scopus 로고
    • Biology of recombinant hirudin (CGP 39393). a new prospect in the treatment of thrombosis
    • Talbot MD: Biology of recombinant hirudin (CGP 39393). A new prospect in the treatment of thrombosis. Semin Thromb Hemost 15:293, 1989
    • (1989) Semin Thromb Hemost , vol.15 , pp. 293
    • Talbot, M.D.1
  • 12
    • 0023779072 scopus 로고
    • Evidence for the identity of hirudin isolated after kidney passage with the starting material
    • Henschen A, Markwardt F, Walsmann P: Evidence for the identity of hirudin isolated after kidney passage with the starting material. Folia Haematol 115:59, 1988
    • (1988) Folia Haematol , vol.115 , pp. 59
    • Henschen, A.1    Markwardt, F.2    Walsmann, P.3
  • 13
    • 0029160038 scopus 로고
    • Advances in antithrombotic therapy: Novel reagents
    • Turpie AGG, Weitz JI, Hirsh J: Advances in antithrombotic therapy: Novel reagents. Thromb Haemost 74:565, 1995
    • (1995) Thromb Haemost , vol.74 , pp. 565
    • Turpie, A.G.G.1    Weitz, J.I.2    Hirsh, J.3
  • 15
    • 0027479693 scopus 로고
    • The effect of a long-lasting recombinant hirudin (PEG-hirudin) on experimental disseminated intravascular coagulation (DIG) in rabbits
    • Zawilska K, Zozulinska M, Turowiecka Z, Blahut M, Drobnik L, Vinazzer H: The effect of a long-lasting recombinant hirudin (PEG-hirudin) on experimental disseminated intravascular coagulation (DIG) in rabbits. Thromb Res 69:315, 1993
    • (1993) Thromb Res , vol.69 , pp. 315
    • Zawilska, K.1    Zozulinska, M.2    Turowiecka, Z.3    Blahut, M.4    Drobnik, L.5    Vinazzer, H.6
  • 16
    • 0029835392 scopus 로고    scopus 로고
    • A comparison of recombinant hirudin with heparin for the treatment of acute coronary syndromes
    • GUSTO lib Investigators: A comparison of recombinant hirudin with heparin for the treatment of acute coronary syndromes. N Engl J Med 335:775, 1996
    • (1996) N Engl J Med , vol.335 , pp. 775
  • 18
    • 0003185280 scopus 로고
    • Gene synthesis: Assembly of target sequences using mutually priming long oligonucleotides
    • in Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (eds): Media, PA, Wiley
    • Moore DD: Gene synthesis: Assembly of target sequences using mutually priming long oligonucleotides, in Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K (eds): Current Protocols in Molecular Biology. Media, PA, Wiley, 1987, p 3.5.8
    • (1987) Current Protocols in Molecular Biology. , pp. 358
    • Moore, D.D.1
  • 21
    • 0026696565 scopus 로고
    • Molecular cloning and expression of rabbit antithrombin III
    • Sheffield WP, Brothers AB, Hatton MWC, Clarke BJ, Blajchman MA: Molecular cloning and expression of rabbit antithrombin III. Blood 79:2330, 1992
    • (1992) Blood , vol.79 , pp. 2330
    • Sheffield, W.P.1    Brothers, A.B.2    Hatton, M.W.C.3    Clarke, B.J.4
  • 22
    • 0028362250 scopus 로고
    • Molecular cloning and expression of rabbit heparin cofactor II: A plasma thrombin inhibitor highly conserved between species
    • Sheffield WP, Schuyler PD, Blajchman MA: Molecular cloning and expression of rabbit heparin cofactor II: A plasma thrombin inhibitor highly conserved between species. Thromb Haemost 71:778, 1994
    • (1994) Thromb Haemost , vol.71 , pp. 778
    • Sheffield, W.P.1    Schuyler, P.D.2
  • 23
    • 0026315433 scopus 로고
    • Receptor-mediated gene delivery in vivo: Partial correction of genetic analbuminemia in rats
    • Wu GY, Wilson GM, Shabby F, Grossman M, Shafritz DA, Wu CH: Receptor-mediated gene delivery in vivo: Partial correction of genetic analbuminemia in rats. J Biol Chem 266:14338, 1991
    • (1991) J Biol Chem , vol.266 , pp. 14338
    • Wu, G.Y.1    Wilson, G.M.2    Shabby, F.3    Grossman, M.4    Shafritz, D.A.5    Wu, C.H.6
  • 24
    • 0021253525 scopus 로고
    • Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing
    • Henikoff S: Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene 28:351, 1984
    • (1984) Gene , vol.28 , pp. 351
    • Henikoff, S.1
  • 25
    • 0024283936 scopus 로고
    • A versatile in vivo and in vitro eukaryotic expression vector for protein engineering
    • Green S, Isseman I, Sheer E: A versatile in vivo and in vitro eukaryotic expression vector for protein engineering. Nucleic Acids Res 16:369, 1988
    • (1988) Nucleic Acids Res , vol.16 , pp. 369
    • Green, S.1    Isseman, I.2    Sheer, E.3
  • 27
    • 0028037888 scopus 로고
    • Amino acid substitutions of the P2 residue of antithrombin that either enhance or impair function
    • Sheffield WP, Blajchman MA: Amino acid substitutions of the P2 residue of antithrombin that either enhance or impair function. Thromb Res 75:293, 1994
    • (1994) Thromb Res , vol.75 , pp. 293
    • Sheffield, W.P.1    Blajchman, M.A.2
  • 28
    • 0018406314 scopus 로고
    • Use of kinetic analysis and mathematical modeling in the study of metabolic pathways in vivo
    • Carson ER, Jones EA: Use of kinetic analysis and mathematical modeling in the study of metabolic pathways in vivo. N Engl J Med 300:1016, 1979
    • (1979) N Engl J Med , vol.300 , pp. 1016
    • Carson, E.R.1    Jones, E.A.2
  • 29
    • 0021265717 scopus 로고
    • In vivo behaviour of radioiodinated rabbit antithrombin III. Demonstration of a non-circulating vascular compartment
    • Carlson TH, Atencio AC, Simon TB: In vivo behaviour of radioiodinated rabbit antithrombin III. Demonstration of a non-circulating vascular compartment. J Clin Invest 74:191, 1984
    • (1984) J Clin Invest , vol.74 , pp. 191
    • Carlson, T.H.1    Atencio, A.C.2    Simon, T.B.3
  • 30
    • 0022003081 scopus 로고
    • Comparison of the behaviour in vivo of two molecular forms of antithrombin III
    • Carlson TH, Atencio AC, Simon TH: Comparison of the behaviour in vivo of two molecular forms of antithrombin III. Biochem J 225:557, 1985
    • (1985) Biochem J , vol.225 , pp. 557
    • Carlson, T.H.1    Atencio, A.C.2    Simon, T.H.3
  • 31
    • 0028858172 scopus 로고
    • Intracellular events determine the fate of antithrombin Utah
    • Sheffield WP, Castillo JE, Blajchman MA: Intracellular events determine the fate of antithrombin Utah. Blood 86:3461, 1995
    • (1995) Blood , vol.86 , pp. 3461
    • Sheffield, W.P.1    Castillo, J.E.2    Blajchman, M.A.3
  • 32
    • 0027438174 scopus 로고
    • CX-397, a novel recombinant hirudin analog having a hybrid sequence of hirudin variants-1 and -3
    • Komatsu Y, Noda A, Misawa S, Sukesada A, Hiyasa H: CX-397, a novel recombinant hirudin analog having a hybrid sequence of hirudin variants-1 and -3. Biochem Biophys Res Commun 196:773, 1993
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 773
    • Komatsu, Y.1    Noda, A.2    Misawa, S.3    Sukesada, A.4    Hiyasa, H.5
  • 33
    • 0008915717 scopus 로고
    • Nucleotide sequence and the encoded amino acids of human serum albumin mRNA
    • Dugiaczyk A, Law SW, Dennison OE: Nucleotide sequence and the encoded amino acids of human serum albumin mRNA. Proc Natl Acad Sei USA 79:71, 1982
    • (1982) Proc Natl Acad Sei USA , vol.79 , pp. 71
    • Dugiaczyk, A.1    Law, S.W.2    Dennison, O.E.3
  • 34
    • 0027219371 scopus 로고
    • X-ray and primary structure of horse serum albumin (Equus caballus) at 0.27 nm resolution
    • Ho JX, Holowachuk EW, Norton EJ, Twigg PD, Carter DC: X-ray and primary structure of horse serum albumin (Equus caballus) at 0.27 nm resolution. Eur J Biochem 215:205, 1993
    • (1993) Eur J Biochem , vol.215 , pp. 205
    • Ho, J.X.1    Holowachuk, E.W.2    Norton, E.J.3    Twigg, P.D.4    Carter, D.C.5
  • 35
    • 0015900723 scopus 로고
    • Selective removal of albumin from plasma by affinity chromatography
    • Travis J, Pannell R: Selective removal of albumin from plasma by affinity chromatography. Clin Chim Acta 49:49, 1973
    • (1973) Clin Chim Acta , vol.49 , pp. 49
    • Travis, J.1    Pannell, R.2
  • 36
    • 0028202551 scopus 로고
    • Radiolabeled r-hirudin as a measure of thrombin activity at, or within, the rabbit aorta wall in vitro and in vivo
    • Hatton MWC, Ross-Ouellet B: Radiolabeled r-hirudin as a measure of thrombin activity at, or within, the rabbit aorta wall in vitro and in vivo. Thromb Haemost 71:499, 1994
    • (1994) Thromb Haemost , vol.71 , pp. 499
    • Hatton, M.W.C.1    Ross-Ouellet, B.2
  • 38
    • 0023766115 scopus 로고
    • Use of sitedirected mutagenesis to investigate the basis for the specificity of hirudin
    • Braun PJ, Dennis S, Hofsteenge J, Stone SR: Use of sitedirected mutagenesis to investigate the basis for the specificity of hirudin. Biochemistry 27:6517, 1988
    • (1988) Biochemistry , vol.27 , pp. 6517
    • Braun, P.J.1    Dennis, S.2    Hofsteenge, J.3    Stone, S.R.4
  • 39
    • 0027217174 scopus 로고
    • On glucose transport and non-enzymic glycation of proteins in vivo
    • Hatton MWC, Richardson M, Winocour PD: On glucose transport and non-enzymic glycation of proteins in vivo. J Theor Biol 161:481, 1993
    • (1993) J Theor Biol , vol.161 , pp. 481
    • Hatton, M.W.C.1    Richardson, M.2    Winocour, P.D.3
  • 40
    • 0028255957 scopus 로고
    • Covalent linkage of streptokinase to recombinant hirudin: A novel thrombolytic agent with antithrombotic properties
    • Phaneuf MD, Ozaki CK, Johnstone MT, Loza J-P, Quist WC, LoGerfo FW: Covalent linkage of streptokinase to recombinant hirudin: A novel thrombolytic agent with antithrombotic properties. Thromb Haemost 71:481, 1994
    • (1994) Thromb Haemost , vol.71 , pp. 481
    • Phaneuf, M.D.1    Ozaki, C.K.2    Johnstone, M.T.3    Loza, J.-P.4    Quist, W.C.5    Logerfo, F.W.6
  • 41
    • 0027953821 scopus 로고
    • Synthesis and characterization of a recombinant hirudin-albumin complex
    • Phaneuf MD, Ito RK, LoGerfo FW: Synthesis and characterization of a recombinant hirudin-albumin complex. Blood Coagul Fibrin 5:641, 1994
    • (1994) Blood Coagul Fibrin , vol.5 , pp. 641
    • Phaneuf, M.D.1    Ito, R.K.2    Logerfo, F.W.3
  • 42
    • 0027964241 scopus 로고
    • Direct thrombin inhibition with rec-hirudin (COP 39393) as prophylaxis of thromboembolic complications after total hip replacement
    • Eriksson BI, Kalebo P, Ekman S, Lindbratt S, Kerry R, Close P: Direct thrombin inhibition with rec-hirudin (COP 39393) as prophylaxis of thromboembolic complications after total hip replacement. Thromb Haemost 72:227, 1994
    • (1994) Thromb Haemost , vol.72 , pp. 227
    • Eriksson, B.I.1    Kalebo, P.2    Ekman, S.3    Lindbratt, S.4    Kerry, R.5    Close, P.6
  • 43
    • 0028092111 scopus 로고
    • Hirudin in myocardial infarction. Safety report from the thrombolysis and thrombin inhibition in myocardial infarction (TIMI-9A) trial
    • Antman E, for the TIMI-9A Investigators: Hirudin in myocardial infarction. Safety report from the thrombolysis and thrombin inhibition in myocardial infarction (TIMI-9A) trial. Circulation 90:1638, 1994
    • (1994) Circulation , vol.90 , pp. 1638
    • Antman, E.1
  • 44
    • 0028037517 scopus 로고
    • Randomised trial of intravenous heparin versus recombinant hirudin for acute coronary syndromes
    • GUSTO Ha Investigators: Randomised trial of intravenous heparin versus recombinant hirudin for acute coronary syndromes. Circulation 90:1631, 1994
    • (1994) Circulation , vol.90 , pp. 1631


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.