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Volumn 80, Issue 1, 1998, Pages 155-160

Fibrino(geno)lytic properties of purified hementerin, a metalloproteinase from the leech Haementeria depressa

Author keywords

[No Author keywords available]

Indexed keywords

FIBRIN; FIBRINOGEN; HEMENTERIN; METALLOPROTEINASE; UNCLASSIFIED DRUG;

EID: 0031927813     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1615155     Document Type: Article
Times cited : (29)

References (43)
  • 1
    • 0002731806 scopus 로고
    • Ferment anticoagulant de 1 "Ixodes ricinus"
    • Sabbatani L. Ferment anticoagulant de 1 "Ixodes ricinus". Arch Ital Biol 1899; 31: 37-53.
    • (1899) Arch Ital Biol , vol.31 , pp. 37-53
    • Sabbatani, L.1
  • 2
    • 34447609147 scopus 로고
    • Über die Einwirkung eines Sekretes des officinellen Blutegels auf die Gerinnbarkeit des Blutes
    • Haycraft JB. Über die Einwirkung eines Sekretes des officinellen Blutegels auf die Gerinnbarkeit des Blutes. Naunyn-Schmiedeberg's Arch Exp Path Pharmak 1884; 18: 209-17.
    • (1884) Naunyn-Schmiedeberg's Arch Exp Path Pharmak , vol.18 , pp. 209-217
    • Haycraft, J.B.1
  • 3
    • 0000319455 scopus 로고
    • Hirudin as an inhibitor of thrombin
    • Perlmann GE, Lorand L, eds. New York: Academic Press
    • Markwardt F. Hirudin as an inhibitor of thrombin, in Methods in Enzymology. Perlmann GE, Lorand L, eds. New York: Academic Press 1470; 19: 924-32.
    • (1470) Methods in Enzymology , vol.19 , pp. 924-932
    • Markwardt, F.1
  • 4
    • 0022762461 scopus 로고
    • Chemical synthesis and expression of a gene coding for hirudin, the thrombin-specific inhibitor from the leech Hirudo medicinalis
    • Bergmann C, Dodt J, Köhler S, Fink E, Gassen HG. Chemical synthesis and expression of a gene coding for hirudin, the thrombin-specific inhibitor from the leech Hirudo medicinalis. Biol Chem Hoppe Seyler 1986; 367: 731-40.
    • (1986) Biol Chem Hoppe Seyler , vol.367 , pp. 731-740
    • Bergmann, C.1    Dodt, J.2    Köhler, S.3    Fink, E.4    Gassen, H.G.5
  • 5
    • 0022829882 scopus 로고
    • Cloning and expression in Escherichia coli of a synthetic DNA for hirudin, the blood coagulation inhibitor in the leech
    • Fortkamp E, Rieger M, Heisterberg-Moutses G, Schweitzer S, Sommer R. Cloning and expression in Escherichia coli of a synthetic DNA for hirudin, the blood coagulation inhibitor in the leech. DNA 1986; 5: 511-7.
    • (1986) DNA , vol.5 , pp. 511-517
    • Fortkamp, E.1    Rieger, M.2    Heisterberg-Moutses, G.3    Schweitzer, S.4    Sommer, R.5
  • 7
    • 0027479693 scopus 로고
    • The effect of a long-acting recombinant hinidin (PEG-hirudin) on experimental disseminated intravascular coagulation (DIC) in rabbits
    • Zawilska K, Zozulinska M, Turowiecka Z, Blahut M, Drobnik L, Vinazzer H. The effect of a long-acting recombinant hinidin (PEG-hirudin) on experimental disseminated intravascular coagulation (DIC) in rabbits. Thromb Res 1993; 69: 315-20.
    • (1993) Thromb Res , vol.69 , pp. 315-320
    • Zawilska, K.1    Zozulinska, M.2    Turowiecka, Z.3    Blahut, M.4    Drobnik, L.5    Vinazzer, H.6
  • 8
    • 0025899470 scopus 로고
    • Hirudin and derivatives as anticoagulant agents
    • Markwardt F. Hirudin and derivatives as anticoagulant agents. Thromb Haemost 1991; 66: 141-52.
    • (1991) Thromb Haemost , vol.66 , pp. 141-152
    • Markwardt, F.1
  • 9
    • 0016778913 scopus 로고
    • Fibrinogenolytic substance (Hementerin) of Brazilian blood-sucking leeches (Haementeria lutzi Pinto 1920)
    • Kelen EMA, Rosenfeld G. Fibrinogenolytic substance (Hementerin) of Brazilian blood-sucking leeches (Haementeria lutzi Pinto 1920). Haemostasis 1975; 4: 51-64.
    • (1975) Haemostasis , vol.4 , pp. 51-64
    • Kelen, E.M.A.1    Rosenfeld, G.2
  • 10
    • 0013592073 scopus 로고
    • Hementerin, a potent in vitro activator of the human fibrinolytic system
    • Davidson JF, Bachmann F, Bouvier CA, Kruithof EKO, eds. Edinburgh: Churchill Livingstone
    • Kelen EMA, Hruby VJ, Tomy SC, Pinheiro ME. Hementerin, a potent in vitro activator of the human fibrinolytic system. In: Progress in Fibrinolysis (Davidson JF, Bachmann F, Bouvier CA, Kruithof EKO, eds. Edinburgh: Churchill Livingstone 1983; 6: 95-8.
    • (1983) Progress in Fibrinolysis , vol.6 , pp. 95-98
    • Kelen, E.M.A.1    Hruby, V.J.2    Tomy, S.C.3    Pinheiro, M.E.4
  • 11
    • 0019814540 scopus 로고
    • Composition of salivary gland extracts from the leech Haementeria ghilianii
    • Budzynski AZ, Olexa SA, Sawyer RT. Composition of salivary gland extracts from the leech Haementeria ghilianii. Proc Soc Exp Biol Med USA 1981; 168: 259-65.
    • (1981) Proc Soc Exp Biol Med USA , vol.168 , pp. 259-265
    • Budzynski, A.Z.1    Olexa, S.A.2    Sawyer, R.T.3
  • 12
    • 0021682646 scopus 로고
    • Fibrinogen degradation by hementin, a fibrinogenolytic anticoagulant from the salivary glands of the leech Haementeria ghilianii
    • Malinconico SM, Katz JB, Budzynski AZ. Fibrinogen degradation by hementin, a fibrinogenolytic anticoagulant from the salivary glands of the leech Haementeria ghilianii. J Lab Clin Med 1984; 104: 842-54.
    • (1984) J Lab Clin Med , vol.104 , pp. 842-854
    • Malinconico, S.M.1    Katz, J.B.2    Budzynski, A.Z.3
  • 13
    • 0025240324 scopus 로고
    • Purification and characterization of hementin, a fibrinogenolytic protease from the leech Haementeria ghilianii
    • Swadesh JK, Huang IY, Budzynski AZ. Purification and characterization of hementin, a fibrinogenolytic protease from the leech Haementeria ghilianii. J Chromatography 1990; 502: 359-69.
    • (1990) J Chromatography , vol.502 , pp. 359-369
    • Swadesh, J.K.1    Huang, I.Y.2    Budzynski, A.Z.3
  • 14
    • 0024321427 scopus 로고
    • Isolation and structural characterization of a potent inhibitor of coagulation factor Xa from the leech Haementeria ghilianii
    • Condra C, Nutt E, Petroski CJ, Simpson E, Friedman PA, Jacobs JW. Isolation and structural characterization of a potent inhibitor of coagulation factor Xa from the leech Haementeria ghilianii. Thromb Haemost 1989; 61: 437-41.
    • (1989) Thromb Haemost , vol.61 , pp. 437-441
    • Condra, C.1    Nutt, E.2    Petroski, C.J.3    Simpson, E.4    Friedman, P.A.5    Jacobs, J.W.6
  • 15
    • 0023189460 scopus 로고
    • Isolation and characterization of antistasin. An inhibitor of metastasis and coagulation
    • Tuszynski GP, Gasic TB, Gasic GJ. Isolation and characterization of antistasin. An inhibitor of metastasis and coagulation. J Biol Chem 1987; 262: 9718-23.
    • (1987) J Biol Chem , vol.262 , pp. 9718-9723
    • Tuszynski, G.P.1    Gasic, T.B.2    Gasic, G.J.3
  • 16
    • 0024445042 scopus 로고
    • Antistasin, a leech-derived inhibitor of factor Xa. Kinetic analysis of enzyme inhibition and identification of the reactive site
    • Dunwiddie C, Thromberry NA, Bull HG, Sardana M, Friedman PA, Jacobs JW, Simpson E. Antistasin, a leech-derived inhibitor of factor Xa. Kinetic analysis of enzyme inhibition and identification of the reactive site. J Biol Chem 1988; 264: 16694-9.
    • (1988) J Biol Chem , vol.264 , pp. 16694-16699
    • Dunwiddie, C.1    Thromberry, N.A.2    Bull, H.G.3    Sardana, M.4    Friedman, P.A.5    Jacobs, J.W.6    Simpson, E.7
  • 17
    • 0025329916 scopus 로고
    • Decorsin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora
    • Seymour JL, Henzel WJ, Nevins B, Stults JT, Lazarus A. Decorsin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora. J Biol Chem 1990; 265: 10143-7.
    • (1990) J Biol Chem , vol.265 , pp. 10143-10147
    • Seymour, J.L.1    Henzel, W.J.2    Nevins, B.3    Stults, J.T.4    Lazarus, A.5
  • 18
    • 0026331936 scopus 로고
    • Ornatins: Potent glycoprotein IIb-IIIa antagonists and platelet aggregation inhibitors from the leech Placobdella ornata
    • Mazur P, Henzel WJ, Seymour JL, Lazarus RA. Ornatins: potent glycoprotein IIb-IIIa antagonists and platelet aggregation inhibitors from the leech Placobdella ornata. Eur J Biochem 1991; 202: 1073-82.
    • (1991) Eur J Biochem , vol.202 , pp. 1073-1082
    • Mazur, P.1    Henzel, W.J.2    Seymour, J.L.3    Lazarus, R.A.4
  • 20
    • 2642685146 scopus 로고
    • Sobre la identidad de Blennobdella depressa Em. Blanchard, 1849 y la existencia de Haementeria officinalis de Filippi, 1849 en Estados Unidos (Hirudinea, Glossiphoniiformes)
    • Ringuelet RA. Sobre la identidad de Blennobdella depressa Em. Blanchard, 1849 y la existencia de Haementeria officinalis de Filippi, 1849 en Estados Unidos (Hirudinea, Glossiphoniiformes). Physis 1972; 31: 97-8.
    • (1972) Physis , vol.31 , pp. 97-98
    • Ringuelet, R.A.1
  • 22
    • 0001408345 scopus 로고
    • The preparation and some properties of fibrinogen precipitated from human plasma by glycine
    • Kazal LA, Amsel S, Miller OP, Tocantins LM. The preparation and some properties of fibrinogen precipitated from human plasma by glycine. Proc Soc Exp Biol Med USA 1963; 113: 989-94.
    • (1963) Proc Soc Exp Biol Med USA , vol.113 , pp. 989-994
    • Kazal, L.A.1    Amsel, S.2    Miller, O.P.3    Tocantins, L.M.4
  • 24
    • 0014932863 scopus 로고
    • Plasminogen: Purification from human plasma by affinity chromatography
    • Deutsch DG, Mertz ET. Plasminogen: purification from human plasma by affinity chromatography. Science 1970; 170: 1095-6.
    • (1970) Science , vol.170 , pp. 1095-1096
    • Deutsch, D.G.1    Mertz, E.T.2
  • 25
    • 0025718644 scopus 로고
    • Characterization of the binding of plasminogen to fibrin surfaces: The role of carboxy-terminal lysines
    • Fleury V, Anglés-Cano E. Characterization of the binding of plasminogen to fibrin surfaces: the role of carboxy-terminal lysines. Biochemistry 1991; 30: 7630-8.
    • (1991) Biochemistry , vol.30 , pp. 7630-7638
    • Fleury, V.1    Anglés-Cano, E.2
  • 26
    • 0018178434 scopus 로고
    • A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples
    • Markwell MAK, Haa SM, Bieber LL, Tolbert NE. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem 1978; 87: 206-10.
    • (1978) Anal Biochem , vol.87 , pp. 206-210
    • Markwell, M.A.K.1    Haa, S.M.2    Bieber, L.L.3    Tolbert, N.E.4
  • 29
    • 0021055664 scopus 로고
    • A study of the fibrin plate assay of fibrinolytic agents. Optimal conditions, reproducibility and precision
    • Jespersen J, Astrup T. A study of the fibrin plate assay of fibrinolytic agents. Optimal conditions, reproducibility and precision. Haemostasis 1983; 13: 301-15.
    • (1983) Haemostasis , vol.13 , pp. 301-315
    • Jespersen, J.1    Astrup, T.2
  • 30
    • 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 1970; 227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0027300059 scopus 로고
    • Sodium dodecyl sulfate-induced dissociation of complexes between tissue plasminogen activator and its specific inhibitor
    • Gaussem P, Grailhe P, Anglés-Cano E. Sodium dodecyl sulfate-induced dissociation of complexes between tissue plasminogen activator and its specific inhibitor. J Biol Chem 1993; 268: 12150-5.
    • (1993) J Biol Chem , vol.268 , pp. 12150-12155
    • Gaussem, P.1    Grailhe, P.2    Anglés-Cano, E.3
  • 32
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber K, Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem 1968; 244: 4406-12.
    • (1968) J Biol Chem , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 33
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels, a modified procedure with enhanced uniform sensitivity
    • Morrissey JH. Silver stain for proteins in polyacrylamide gels, a modified procedure with enhanced uniform sensitivity. Anal Biochem 1981; 117: 307-10.
    • (1981) Anal Biochem , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 34
    • 0025766888 scopus 로고
    • The formation of complexes between human plasminogen activator inhibitor-1 (PAI-1) and sodium dodecyl sulfate
    • Gaussem P, Anglés-Cano E. The formation of complexes between human plasminogen activator inhibitor-1 (PAI-1) and sodium dodecyl sulfate. Biochim Biophys Acta 1991; 1079: 321-9.
    • (1991) Biochim Biophys Acta , vol.1079 , pp. 321-329
    • Gaussem, P.1    Anglés-Cano, E.2
  • 36
    • 0022443667 scopus 로고
    • A spectrophotometric solid-phase fibrin-tissue plasminogen activator activity assay (SOFIA-TPA) for high-fibrin-affinity tissue plasminogen activators
    • Anglés-Cano E. A spectrophotometric solid-phase fibrin-tissue plasminogen activator activity assay (SOFIA-TPA) for high-fibrin-affinity tissue plasminogen activators. Anal Biochem 1986; 153: 201-10.
    • (1986) Anal Biochem , vol.153 , pp. 201-210
    • Anglés-Cano, E.1
  • 37
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Procedure and some applications. Proc Natl Acad Sci USA 1979; 76: 4350-4.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 38
    • 0022520242 scopus 로고
    • Production and characterization of a monoclonal antibody reactive with a specific neoantigenic determinant (comprising Bβ 54-118) in degradation products of fibrin and of fibrinogen
    • Koppert PW, Koopman J, Haverkate F, Nieuwenhuizen W. Production and characterization of a monoclonal antibody reactive with a specific neoantigenic determinant (comprising Bβ 54-118) in degradation products of fibrin and of fibrinogen. Blood 1986; 68: 437-41.
    • (1986) Blood , vol.68 , pp. 437-441
    • Koppert, P.W.1    Koopman, J.2    Haverkate, F.3    Nieuwenhuizen, W.4
  • 40
    • 0020664311 scopus 로고
    • Plasminogen activation by tissue activator is accelerated in the presence of fibrin(ogen) cyanogen bromide fragment FCB-2
    • Nieuwenhuizen W, Verheijen JH, Vermond A, Chang GTG. Plasminogen activation by tissue activator is accelerated in the presence of fibrin(ogen) cyanogen bromide fragment FCB-2. Biochim Biophys Acta 1983; 755: 531-3.
    • (1983) Biochim Biophys Acta , vol.755 , pp. 531-533
    • Nieuwenhuizen, W.1    Verheijen, J.H.2    Vermond, A.3    Chang, G.T.G.4
  • 41
    • 0025113502 scopus 로고
    • A unique proteolytic fragment of human fibrinogen containing the A-alpha COOH-terminal domain of the native molecule
    • Kirschbaum NE, Budzynski AZ. A unique proteolytic fragment of human fibrinogen containing the A-alpha COOH-terminal domain of the native molecule. J Biol Chem 1990; 265: 13669-76.
    • (1990) J Biol Chem , vol.265 , pp. 13669-13676
    • Kirschbaum, N.E.1    Budzynski, A.Z.2
  • 42
    • 0026102681 scopus 로고
    • Interaction of hementin with fibrinogen and fibrin
    • Budzynski AZ. Interaction of hementin with fibrinogen and fibrin. Blood Coag Fibrinolysis 1991; 2: 149-52.
    • (1991) Blood Coag Fibrinolysis , vol.2 , pp. 149-152
    • Budzynski, A.Z.1
  • 43
    • 0014690463 scopus 로고
    • High molecular weight derivatives of human fibrinogen produced by plasmin. II. Mechanisms of their anticoagulant activity
    • Marder VJ, Shulman NR. High molecular weight derivatives of human fibrinogen produced by plasmin. II. Mechanisms of their anticoagulant activity. J Biol Chem 1969; 244: 2120-4.
    • (1969) J Biol Chem , vol.244 , pp. 2120-2124
    • Marder, V.J.1    Shulman, N.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.