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Volumn 1434, Issue 1, 1999, Pages 94-102

Lebetase, an α(β)-fibrin(ogen)olytic metalloproteinase of Vipera lebetina snake venom, is inhibited by human α-macroglobulins

Author keywords

2 Macroglobulin; Fibrinogen; Lebetase; Metalloproteinase; Pregnancy zone protein; Vipera lebetina

Indexed keywords

ALPHA 2 MACROGLOBULIN; ANTICOAGULANT AGENT; LEBETASE; METALLOPROTEINASE; PREGNANCY ASSOCIATED ALPHA2 GLYCOPROTEIN; SNAKE VENOM; UNCLASSIFIED DRUG;

EID: 0032737975     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00164-8     Document Type: Article
Times cited : (18)

References (30)
  • 1
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • Markland F.S. Snake venoms and the hemostatic system. Toxicon. 36:1998;1749-1800.
    • (1998) Toxicon , vol.36 , pp. 1749-1800
    • Markland, F.S.1
  • 2
    • 0026675418 scopus 로고
    • The direct-acting α-fibrin(ogen)olytic enzymes from snake venoms
    • Siigur E., Siigur J. The direct-acting α-fibrin(ogen)olytic enzymes from snake venoms. J. Toxicol. Toxin Rev. 11:1992;91-113.
    • (1992) J. Toxicol. Toxin Rev. , vol.11 , pp. 91-113
    • Siigur, E.1    Siigur, J.2
  • 3
    • 0032053249 scopus 로고    scopus 로고
    • Biochemical characterization of lebetase, a direct-acting fibrinolytic enzyme from Vipera lebetina snake venom
    • Siigur J., Samel M., Tõnismägi K., Subbi J., Siigur E., Tu A.T. Biochemical characterization of lebetase, a direct-acting fibrinolytic enzyme from Vipera lebetina snake venom. Tromb. Res. 90:1998;39-49.
    • (1998) Tromb. Res. , vol.90 , pp. 39-49
    • Siigur, J.1    Samel, M.2    Tõnismägi, K.3    Subbi, J.4    Siigur, E.5    Tu, A.T.6
  • 4
    • 0030570469 scopus 로고    scopus 로고
    • CDNA cloning and deduced amino acid sequence of fibrinolytic enzyme (lebetase) from Vipera lebetina snake venom
    • Siigur E., Aaspôllu A., Tu A.T., Siigur J. cDNA cloning and deduced amino acid sequence of fibrinolytic enzyme (lebetase) from Vipera lebetina snake venom. Biochem. Biophys. Res. Commun. 224:1996;229-236.
    • (1996) Biochem. Biophys. Res. Commun. , vol.224 , pp. 229-236
    • Siigur, E.1    Aaspôllu, A.2    Tu, A.T.3    Siigur, J.4
  • 5
    • 0018763129 scopus 로고
    • The electrophoretically 'slow' and fast forms of the alpha 2-macroglobulin molecule
    • Barrett A.J., Brown M.A., Sayers C.A. The electrophoretically 'slow' and fast forms of the alpha 2-macroglobulin molecule. Biochem. J. 181:1979;401-418.
    • (1979) Biochem. J. , vol.181 , pp. 401-418
    • Barrett, A.J.1    Brown, M.A.2    Sayers, C.A.3
  • 6
    • 0022998261 scopus 로고
    • Primary structure of human alpha 2-macroglobulin. Complete disulfide bridge assignment and localization of two interchain bridges in the dimeric proteinase binding unit
    • Jensen P.E.H., Sottrup-Jensen L. Primary structure of human alpha 2-macroglobulin. Complete disulfide bridge assignment and localization of two interchain bridges in the dimeric proteinase binding unit. J. Biol. Chem. 261:1986;15863-15869.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15863-15869
    • Jensen, P.E.H.1    Sottrup-Jensen, L.2
  • 7
    • 0015896128 scopus 로고
    • The interaction of alpha 2-macroglobulin with proteinases, characteristics and specificity of the reaction and hypothesis concerning its molecular mechanism
    • Barrett A.J., Starkey P.M. The interaction of alpha 2-macroglobulin with proteinases, characteristics and specificity of the reaction and hypothesis concerning its molecular mechanism. Biochem. J. 133:1973;709-724.
    • (1973) Biochem. J. , vol.133 , pp. 709-724
    • Barrett, A.J.1    Starkey, P.M.2
  • 8
    • 0019818065 scopus 로고
    • Receptor-mediated endocytosis of alpha 2-macroglobulin-protease complexes by fibroblasts in culture. Competitive inhibition by bacitracin
    • Van Leuven F., Marynen P., Cassiman J.-J., Van den Berghe H. Receptor-mediated endocytosis of alpha 2-macroglobulin-protease complexes by fibroblasts in culture. Competitive inhibition by bacitracin. FEBS Lett. 134:1981;83-87.
    • (1981) FEBS Lett. , vol.134 , pp. 83-87
    • Van Leuven, F.1    Marynen, P.2    Cassiman, J.-J.3    Van Den Berghe, H.4
  • 9
    • 0019021441 scopus 로고
    • Covalent binding of proteinases in their reaction with alpha 2-macroglobulin
    • Salvesen G.S., Barrett A.J. Covalent binding of proteinases in their reaction with alpha 2-macroglobulin. Biochem. J. 187:1980;695-701.
    • (1980) Biochem. J. , vol.187 , pp. 695-701
    • Salvesen, G.S.1    Barrett, A.J.2
  • 10
    • 0027276844 scopus 로고
    • Production of conformation-specific monoclonal antibodies against alpha 2-macroglobulin in human blood
    • Birkenmeier G., Stigbrand T. Production of conformation-specific monoclonal antibodies against alpha 2-macroglobulin in human blood. J. Immunol. Methods. 162:1993;59-67.
    • (1993) J. Immunol. Methods , vol.162 , pp. 59-67
    • Birkenmeier, G.1    Stigbrand, T.2
  • 11
    • 0023619707 scopus 로고
    • A two-site monoclonal enzyme immunoassay for pregnancy-associated alpha 2-glycoprotein
    • Carlsson L., Sottrup-Jensen L., Stigbrand T. A two-site monoclonal enzyme immunoassay for pregnancy-associated alpha 2-glycoprotein. J. Immunol. Methods. 104:1987;73-79.
    • (1987) J. Immunol. Methods , vol.104 , pp. 73-79
    • Carlsson, L.1    Sottrup-Jensen, L.2    Stigbrand, T.3
  • 12
    • 0343267782 scopus 로고    scopus 로고
    • Cross-reactivities of polyclonal antibodies against lebetase, fibrinolytic enzyme of Levantine viper (Vipera lebetina) venom
    • Siigur J., Tõnismägi K., Tu A.T., Siigur E. Cross-reactivities of polyclonal antibodies against lebetase, fibrinolytic enzyme of Levantine viper (Vipera lebetina) venom. Toxicon. 34:1996;608-613.
    • (1996) Toxicon , vol.34 , pp. 608-613
    • Siigur, J.1    Tõnismägi, K.2    Tu, A.T.3    Siigur, E.4
  • 13
    • 0031214644 scopus 로고    scopus 로고
    • Purification of pregnancy zone protein and its receptor binding domain from human plasma
    • Arbelaez L.F., Stigbrand T. Purification of pregnancy zone protein and its receptor binding domain from human plasma. Protein Expr. Purif. 10:1997;301-308.
    • (1997) Protein Expr. Purif. , vol.10 , pp. 301-308
    • Arbelaez, L.F.1    Stigbrand, T.2
  • 14
    • 0025818718 scopus 로고
    • Purification and characterization of lebetase, a fibrinolytic enzyme from Vipera lebetina (snake) venom
    • Siigur E., Siigur J. Purification and characterization of lebetase, a fibrinolytic enzyme from Vipera lebetina (snake) venom. Biochim. Biophys. Acta. 1074:1991;223-229.
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 223-229
    • Siigur, E.1    Siigur, J.2
  • 15
    • 0019784199 scopus 로고
    • Clearance and binding of two electrophoretic 'fast' forms of human alpha 2-macroglobulin
    • Imber M.J., Pizzo S.V. Clearance and binding of two electrophoretic 'fast' forms of human alpha 2-macroglobulin. J. Biol. Chem. 256:1981;8134-8139.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8134-8139
    • Imber, M.J.1    Pizzo, S.V.2
  • 16
    • 77956127888 scopus 로고
    • The preparation of 131-I-labelled human growth hormone of high specific radioactivity
    • Greenwood F.C., Hunter W.M., Glover J.S. The preparation of 131-I-labelled human growth hormone of high specific radioactivity. Biochem. J. 89:1963;114-123.
    • (1963) Biochem. J. , vol.89 , pp. 114-123
    • Greenwood, F.C.1    Hunter, W.M.2    Glover, J.S.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon G. Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, G.3
  • 20
    • 0024333351 scopus 로고
    • Alpha-macroglobulins: Structure, shape, and mechanism of proteinase complex formation
    • Sottrup-Jensen L. Alpha-macroglobulins: structure, shape, and mechanism of proteinase complex formation. J. Biol. Chem. 264:1989;11539-11542.
    • (1989) J. Biol. Chem. , vol.264 , pp. 11539-11542
    • Sottrup-Jensen, L.1
  • 21
    • 0025196271 scopus 로고
    • Biochemical characteristics of fibrolase, a fibrinolytic protease from snake venom
    • Ahmed N.K., Tennant K.D., Markland F.S., Lacz J.P. Biochemical characteristics of fibrolase, a fibrinolytic protease from snake venom. Haemostasis. 20:1990;147-154.
    • (1990) Haemostasis , vol.20 , pp. 147-154
    • Ahmed, N.K.1    Tennant, K.D.2    Markland, F.S.3    Lacz, J.P.4
  • 22
    • 0028986636 scopus 로고
    • Biochemical characterization of basilase, a fibrinolytic enzyme from Crotalus basiliscus basiliscus
    • Datta G., Dong A., Witt J., Tu A.T. Biochemical characterization of basilase, a fibrinolytic enzyme from Crotalus basiliscus basiliscus. Arch. Biochem. Biophys. 317:1995;365-373.
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 365-373
    • Datta, G.1    Dong, A.2    Witt, J.3    Tu, A.T.4
  • 23
    • 0024298861 scopus 로고
    • Purification and biochemical characterization of atroxase, a nonhemorrhagic fibrinolytic protease from Western diamondback rattlesnake venom
    • Willis T.W., Tu A.T. Purification and biochemical characterization of atroxase, a nonhemorrhagic fibrinolytic protease from Western diamondback rattlesnake venom. Biochemistry. 27:1988;4769-4777.
    • (1988) Biochemistry , vol.27 , pp. 4769-4777
    • Willis, T.W.1    Tu, A.T.2
  • 24
    • 0031842808 scopus 로고    scopus 로고
    • Inhibition of a snake venom hemorrhagic metalloproteinase by human and rat macroglobulins
    • Anai K., Sugiki M., Yoshida E., Maruyama M. Inhibition of a snake venom hemorrhagic metalloproteinase by human and rat macroglobulins. Toxicon. 36:1998;1127-1139.
    • (1998) Toxicon , vol.36 , pp. 1127-1139
    • Anai, K.1    Sugiki, M.2    Yoshida, E.3    Maruyama, M.4
  • 27
    • 0022263013 scopus 로고
    • Purification and partial characterization of the hemorrhagic factor from the venom of Crotalus adamantus (Eastern diamondback rattlesnake)
    • Kurecki T., Kress L.F. Purification and partial characterization of the hemorrhagic factor from the venom of Crotalus adamantus (Eastern diamondback rattlesnake). Toxicon. 23:1985;657-668.
    • (1985) Toxicon , vol.23 , pp. 657-668
    • Kurecki, T.1    Kress, L.F.2
  • 29
    • 0029055393 scopus 로고
    • Snake venom metalloendopeptidases: Reprolysins
    • Bjarnason J.B., Fox J.W. Snake venom metalloendopeptidases: reprolysins. Methods Enzymol. 248:1995;345-368.
    • (1995) Methods Enzymol. , vol.248 , pp. 345-368
    • Bjarnason, J.B.1    Fox, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.