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Volumn 93, Issue 1, 1996, Pages 153-160

Comparison of sustained antithrombotic effects of inhibitors of thrombin and factor Xa in experimental thrombosis

Author keywords

anticoagulants; fibrinolysis; thrombosis

Indexed keywords

CVS 995; HIRULOG; LEPIRUDIN; THROMBIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 0030022915     PISSN: 00097322     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.CIR.93.1.153     Document Type: Article
Times cited : (36)

References (35)
  • 1
    • 0026434005 scopus 로고
    • Heparin
    • Hirsh J. Heparin. N Engl J Med. 1991;324:1565-1574.
    • (1991) N Engl J Med , vol.324 , pp. 1565-1574
    • Hirsh, J.1
  • 3
    • 0022345880 scopus 로고
    • A comparison between low molecular weight heparin (KABI 2165) and standard heparin in the intravenous treatment of deep venous thrombosis
    • Bratt G, Tornebohm E, Gragvist S, Aberg, Lockner D. A comparison between low molecular weight heparin (KABI 2165) and standard heparin in the intravenous treatment of deep venous thrombosis. Thromb Haemost. 1985;54:813-817.
    • (1985) Thromb Haemost , vol.54 , pp. 813-817
    • Bratt, G.1    Tornebohm, E.2    Gragvist, S.3    Aberg4    Lockner, D.5
  • 4
    • 0026460878 scopus 로고
    • Acenocoumarol and heparin compared with acenocoumarol alone in the initial treatment of proximal vein thrombosis
    • Brandjes DPM, Heyboer H, Büller HR, de Rijk M, Jagt H, ten Gate JW. Acenocoumarol and heparin compared with acenocoumarol alone in the initial treatment of proximal vein thrombosis. N Engl J Med. 1992;327:1485-1489.
    • (1992) N Engl J Med , vol.327 , pp. 1485-1489
    • Brandjes, D.P.M.1    Heyboer, H.2    Büller, H.R.3    De Rijk, M.4    Jagt, H.5    Ten Gate, J.W.6
  • 7
    • 0025335032 scopus 로고
    • GISSI-2. A factorial randomized trial of alteplase versus streptokinase and heparin versus no heparin among 12,490 patients with acute myocardial infarction
    • GISSI-2. A factorial randomized trial of alteplase versus streptokinase and heparin versus no heparin among 12,490 patients with acute myocardial infarction. Lancet. 1990;1:65-71.
    • (1990) Lancet , vol.1 , pp. 65-71
  • 8
    • 0026732576 scopus 로고
    • Sustained antithrombotic activity of hirudin after its plasma clearance: Comparison with heparin
    • Agnelli G, Renga C, Weitz JI, Nenci GG, Hirsh J. Sustained antithrombotic activity of hirudin after its plasma clearance: comparison with heparin. Blood. 1992;80:960-965.
    • (1992) Blood , vol.80 , pp. 960-965
    • Agnelli, G.1    Renga, C.2    Weitz, J.I.3    Nenci, G.G.4    Hirsh, J.5
  • 9
    • 0025146426 scopus 로고
    • Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors
    • Weitz JI, Hudoba M, Massel D, Maraganore J, Hirsh J. Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors. J Clin Invest. 1990;86:385-391.
    • (1990) J Clin Invest , vol.86 , pp. 385-391
    • Weitz, J.I.1    Hudoba, M.2    Massel, D.3    Maraganore, J.4    Hirsh, J.5
  • 11
    • 0024582671 scopus 로고
    • Effects of thrombin inhibition on the development of acute platelet-thrombus deposition during angioplasty in pigs: Heparin versus recombinant hirudin, a specific thrombin inhibitor
    • Heras MH, Chesebro JH, Penny WJ, Kent RB, Badimon L, Fuster V. Effects of thrombin inhibition on the development of acute platelet-thrombus deposition during angioplasty in pigs: heparin versus recombinant hirudin, a specific thrombin inhibitor. Circulation. 1989;79:657-665.
    • (1989) Circulation , vol.79 , pp. 657-665
    • Heras, M.H.1    Chesebro, J.H.2    Penny, W.J.3    Kent, R.B.4    Badimon, L.5    Fuster, V.6
  • 12
    • 0025375504 scopus 로고
    • Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa
    • Waxman L, Smith DE, Arcuri KE, Vlasuk GP. Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science. 1990;248:593-596.
    • (1990) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3    Vlasuk, G.P.4
  • 14
    • 0025346345 scopus 로고
    • Design and characterisation of Hirulogs: A novel class of bivalent peptide inhibitors of thrombin
    • Maraganore JM, Bourdon P, Jablonski J, Ramachandran KL, Fenton JW. Design and characterisation of Hirulogs: a novel class of bivalent peptide inhibitors of thrombin. Biochemistry. 1990;29: 7095-7101.
    • (1990) Biochemistry , vol.29 , pp. 7095-7101
    • Maraganore, J.M.1    Bourdon, P.2    Jablonski, J.3    Ramachandran, K.L.4    Fenton, J.W.5
  • 19
    • 0026720153 scopus 로고
    • The effect of thrombin inhibitors on tissue plasminogen activator-induced thrombolysis in a rat model
    • Klement P, Borm A, Hirsh J, Maraganore J, Wilson G, Weitz J. The effect of thrombin inhibitors on tissue plasminogen activator-induced thrombolysis in a rat model. Thromb Haemost. 1992;68: 64-68.
    • (1992) Thromb Haemost , vol.68 , pp. 64-68
    • Klement, P.1    Borm, A.2    Hirsh, J.3    Maraganore, J.4    Wilson, G.5    Weitz, J.6
  • 20
    • 0026059199 scopus 로고
    • Antithrombotic efficacy of recombinant tick anticoagulant peptide: A potent inhibitor of coagulation factor Xa in a primate model of arterial thrombosis
    • Schaffer LW, Davidson JT, Vlasuk GP, Siegl PKS. Antithrombotic efficacy of recombinant tick anticoagulant peptide: a potent inhibitor of coagulation factor Xa in a primate model of arterial thrombosis. Circulation. 1991;84:1741-1748.
    • (1991) Circulation , vol.84 , pp. 1741-1748
    • Schaffer, L.W.1    Davidson, J.T.2    Vlasuk, G.P.3    Siegl, P.K.S.4
  • 21
    • 0026558347 scopus 로고
    • Conjunctive enhancement of enzymatic thrombolysis and prevention of thrombotic reocclusion with selective factor Xa inhibitor, tick anticoagulant peptide
    • Sitko GR, Ramjit DR, Stabilito II, Lehman D, Lynch JJ, Vlasuk GP. Conjunctive enhancement of enzymatic thrombolysis and prevention of thrombotic reocclusion with selective factor Xa inhibitor, tick anticoagulant peptide. Circulation. 1992;85:805-815.
    • (1992) Circulation , vol.85 , pp. 805-815
    • Sitko, G.R.1    Ramjit, D.R.2    Stabilito, I.I.3    Lehman, D.4    Lynch, J.J.5    Vlasuk, G.P.6
  • 22
    • 0025891319 scopus 로고
    • Comparison of the in vivo anticoagulant properties of standard heparin and the highly selective factor Xa inhibitors antistasin and tick anticoagulant peptide (TAP) in a rabbit model of venous thrombosis
    • Vlasuk GP, Ramjit D, Fujita T, Dunwiddie CT, Nutt EM, Smith DE, Shebuski RJ. Comparison of the in vivo anticoagulant properties of standard heparin and the highly selective factor Xa inhibitors antistasin and tick anticoagulant peptide (TAP) in a rabbit model of venous thrombosis. Thromb Haemost. 1991;65:257-262.
    • (1991) Thromb Haemost , vol.65 , pp. 257-262
    • Vlasuk, G.P.1    Ramjit, D.2    Fujita, T.3    Dunwiddie, C.T.4    Nutt, E.M.5    Smith, D.E.6    Shebuski, R.J.7
  • 24
    • 0026569416 scopus 로고
    • Comparison of subcutaneous low-molecular weight heparin with intravenous standard heparin in proximal deep-vein thrombosis
    • Prandoni P, Lensing AWA, Büller HR, Carta M, Cogo A, Vigo M, Casara D, Ruol A, ten Cate JW. Comparison of subcutaneous low-molecular weight heparin with intravenous standard heparin in proximal deep-vein thrombosis. Lancet. 1992;1:441-445.
    • (1992) Lancet , vol.1 , pp. 441-445
    • Prandoni, P.1    Lensing, A.W.A.2    Büller, H.R.3    Carta, M.4    Cogo, A.5    Vigo, M.6    Casara, D.7    Ruol, A.8    Ten Cate, J.W.9
  • 26
    • 0028081167 scopus 로고
    • High-level secretion and very efficint isotropic labeling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast, Piscina pastoris
    • Laroche Y, Storme V, DeMeutter J, Messens J, Lauwereys M. High-level secretion and very efficint isotropic labeling of tick anticoagulant peptide (TAP) expressed in the methylotrophic yeast, Piscina pastoris. Biotechnology. 1994;12:1119-1124.
    • (1994) Biotechnology , vol.12 , pp. 1119-1124
    • Laroche, Y.1    Storme, V.2    DeMeutter, J.3    Messens, J.4    Lauwereys, M.5
  • 27
    • 0020359280 scopus 로고
    • A simple sensitive spectrophotometric assay for extrinsic (tissue-type) plasminogen activator applicable to measurements in plasma
    • Verheijen JH, Mullaart E, Chang GTG, Kluft C, Wijngaards G. A simple sensitive spectrophotometric assay for extrinsic (tissue-type) plasminogen activator applicable to measurements in plasma. Thromb Haemost. 1982;48:266-269.
    • (1982) Thromb Haemost , vol.48 , pp. 266-269
    • Verheijen, J.H.1    Mullaart, E.2    Chang, G.T.G.3    Kluft, C.4    Wijngaards, G.5
  • 28
    • 0021214374 scopus 로고
    • Evidence for the occurrence of a fast-acting inhibitor for tissue-type plasminogen activator in human plasma
    • Verheijen JH, Chang GTG, Kluft C. Evidence for the occurrence of a fast-acting inhibitor for tissue-type plasminogen activator in human plasma. Thromb Haemost. 1984;51:392-395.
    • (1984) Thromb Haemost , vol.51 , pp. 392-395
    • Verheijen, J.H.1    Chang, G.T.G.2    Kluft, C.3
  • 29
    • 0023553278 scopus 로고
    • Effect of thrombin on the production of plasminogen activators and PA inhibitor-1 by human foreskin microvascular endothelial cells
    • Van Hinsberg VWM, Sprengers ED, Kooistra T. Effect of thrombin on the production of plasminogen activators and PA inhibitor-1 by human foreskin microvascular endothelial cells. Thromb Haemost. 1987;57:148-153.
    • (1987) Thromb Haemost. , vol.57 , pp. 148-153
    • Van Hinsberg, V.W.M.1    Sprengers, E.D.2    Kooistra, T.3
  • 30
    • 45949121083 scopus 로고
    • Secretion of tissue-type plasminogen activator and plasminogen activator inhibitor by cultured human endothelial cells: Modulation by thrombin, endotoxin, and histamin
    • Hanss M, Collen D. Secretion of tissue-type plasminogen activator and plasminogen activator inhibitor by cultured human endothelial cells: modulation by thrombin, endotoxin, and histamin. J Lab Clin Med. 1987;109:97-104.
    • (1987) J Lab Clin Med , vol.109 , pp. 97-104
    • Hanss, M.1    Collen, D.2
  • 31
    • 0023939414 scopus 로고
    • Increased resistance to plasmic degradation of fibrin with highly cross-linked α-polymer chains formed at high factor XIII concentrations
    • Francis CW, Marder VJ. Increased resistance to plasmic degradation of fibrin with highly cross-linked α-polymer chains formed at high factor XIII concentrations. Blood. 1988;71:1361-1365.
    • (1988) Blood , vol.71 , pp. 1361-1365
    • Francis, C.W.1    Marder, V.J.2
  • 32
    • 85035157179 scopus 로고    scopus 로고
    • Crosslinking of α2-antiplasmin to fibrin is a key factor in regulation blood clot lysis: Species difference
    • In press
    • Van Giezen JJJ, Minkema J, Bouma BN, Jansen JWCM. Crosslinking of α2-antiplasmin to fibrin is a key factor in regulation blood clot lysis: species difference. Blood Coagul Fibrinol. In press.
    • Blood Coagul Fibrinol.
    • Van Giezen, J.J.J.1    Minkema, J.2    Bouma, B.N.3    Jansen, J.W.C.M.4
  • 33
    • 0025113207 scopus 로고
    • Fibrin polymerisation and its regulatory role in haemostasis
    • Mosesson MW. Fibrin polymerisation and its regulatory role in haemostasis. J Lab Clin Med. 1990;116:8-17.
    • (1990) J Lab Clin Med , vol.116 , pp. 8-17
    • Mosesson, M.W.1
  • 34
    • 0018864494 scopus 로고
    • Cross-linking of α2-plasmin inhibitor to fibrin by fibrin-stabilizing factor
    • Sakata Y, Aoki N. Cross-linking of α2-plasmin inhibitor to fibrin by fibrin-stabilizing factor. J Clin Invest. 1980;65:290-297.
    • (1980) J Clin Invest , vol.65 , pp. 290-297
    • Sakata, Y.1    Aoki, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.