메뉴 건너뛰기




Volumn 56, Issue 8, 2010, Pages 1459-1469

Purification, cloning and characterization of a metalloproteinase from Naja atra venom

Author keywords

Cobra venom; Complement; Complement inhibition; Fibrinogenase; Metalloproteinase

Indexed keywords

ALTERNATIVE COMPLEMENT PATHWAY C3 C5 CONVERTASE; ATRASE B; AZOCASEIN; BENZOYLARGININE ETHYL ESTER; CASEIN; COMPLEMENT COMPONENT C6; COMPLEMENT COMPONENT C7; COMPLEMENT COMPONENT C8; COMPLEMENTARY DNA; FIBRIN; FIBRINOGEN; METALLOPROTEINASE; SNAKE VENOM; UNCLASSIFIED DRUG;

EID: 77958462138     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2010.08.013     Document Type: Article
Times cited : (41)

References (44)
  • 1
    • 0018967086 scopus 로고
    • Fibrinolytic enzyme(s) in western diamondback rattlesnake (Crotalus atrox) venom
    • Bajwa S.S., Markland F.S., Russell F.E. Fibrinolytic enzyme(s) in western diamondback rattlesnake (Crotalus atrox) venom. Toxicon 1980, 18:285-290.
    • (1980) Toxicon , vol.18 , pp. 285-290
    • Bajwa, S.S.1    Markland, F.S.2    Russell, F.E.3
  • 2
    • 0014596161 scopus 로고
    • Two anticomplementary factors in cobra venom: hemolysis of guinea pig erythrocytes by one of them
    • Ballow M., Cochrane C.G. Two anticomplementary factors in cobra venom: hemolysis of guinea pig erythrocytes by one of them. J. Immunol. 1969, 103:944-952.
    • (1969) J. Immunol. , vol.103 , pp. 944-952
    • Ballow, M.1    Cochrane, C.G.2
  • 3
    • 0030843099 scopus 로고    scopus 로고
    • Purification of M5, a fibrinolytic proteinase from Crotalus molossus molossus venom that attacks complement
    • Chen T., Rael E.D. Purification of M5, a fibrinolytic proteinase from Crotalus molossus molossus venom that attacks complement. Int. J. Biochem. Cell Biol. 1997, 29:789-799.
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 789-799
    • Chen, T.1    Rael, E.D.2
  • 4
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois M., Gilles K.A., Hamilton J.K., Rebers P.A., Smith F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 1956, 28:350-356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 5
    • 0018818718 scopus 로고
    • In vitro studies on complement inactivation by snake venoms
    • Eggertsen G., Fohlman J., Sjöquist J. In vitro studies on complement inactivation by snake venoms. Toxicon 1980, 18:87-96.
    • (1980) Toxicon , vol.18 , pp. 87-96
    • Eggertsen, G.1    Fohlman, J.2    Sjöquist, J.3
  • 6
    • 0021687769 scopus 로고
    • Purification and properties of a fibrinogenase from the venom of Naja nigricollis
    • Evans H.J. Purification and properties of a fibrinogenase from the venom of Naja nigricollis. Biochim. Biophys. Acta 1984, 802:49-54.
    • (1984) Biochim. Biophys. Acta , vol.802 , pp. 49-54
    • Evans, H.J.1
  • 7
    • 0029987839 scopus 로고    scopus 로고
    • The instructive role of innate immunity in the acquired immune response
    • Fearon D.T., Locksley R.M. The instructive role of innate immunity in the acquired immune response. Science 1996, 272:50-53.
    • (1996) Science , vol.272 , pp. 50-53
    • Fearon, D.T.1    Locksley, R.M.2
  • 8
    • 19544382337 scopus 로고    scopus 로고
    • Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases
    • Fox J.W., Serrano S.M.T. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 2005, 45:969-985.
    • (2005) Toxicon , vol.45 , pp. 969-985
    • Fox, J.W.1    Serrano, S.M.T.2
  • 9
    • 0028219635 scopus 로고
    • Purification from Vipera lebetina (desert adder) venom of a protein that depletes human complement
    • Gasmi A., Louzir H., Karoui H., Ayeb M., Dellagi K. Purification from Vipera lebetina (desert adder) venom of a protein that depletes human complement. Nat. Toxins 1994, 2:44-48.
    • (1994) Nat. Toxins , vol.2 , pp. 44-48
    • Gasmi, A.1    Louzir, H.2    Karoui, H.3    Ayeb, M.4    Dellagi, K.5
  • 10
    • 0015240283 scopus 로고
    • Glycoproteins of cell surfaces. A comparative study of three different cell surfaces of the rat
    • Glossmann H., Neville D.M. Glycoproteins of cell surfaces. A comparative study of three different cell surfaces of the rat. J. Biol. Chem. 1971, 246:6339-6346.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6339-6346
    • Glossmann, H.1    Neville, D.M.2
  • 11
    • 76749145540 scopus 로고    scopus 로고
    • Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins
    • Guan H.H., Goh K.S., Davamani F., Wu P.L., Huang Y.W., Jeyakanthan J., Wu W.G., Chen C.J. Structures of two elapid snake venom metalloproteases with distinct activities highlight the disulfide patterns in the D domain of ADAMalysin family proteins. J. Struct. Biol. 2010, 169:294-303.
    • (2010) J. Struct. Biol. , vol.169 , pp. 294-303
    • Guan, H.H.1    Goh, K.S.2    Davamani, F.3    Wu, P.L.4    Huang, Y.W.5    Jeyakanthan, J.6    Wu, W.G.7    Chen, C.J.8
  • 12
    • 34247572893 scopus 로고    scopus 로고
    • Isolation and cloning of a metalloproteinase from king cobra snake venom
    • Guo X.X., Zeng L., Lee W.H., Zhang Y., Jin Y. Isolation and cloning of a metalloproteinase from king cobra snake venom. Toxicon 2007, 49:954-965.
    • (2007) Toxicon , vol.49 , pp. 954-965
    • Guo, X.X.1    Zeng, L.2    Lee, W.H.3    Zhang, Y.4    Jin, Y.5
  • 13
    • 0028924054 scopus 로고
    • Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo)
    • Gutiérrez J.M., Romero M., Díaz C., Borkow G., Ovadia M. Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo). Toxicon 1995, 33:19-29.
    • (1995) Toxicon , vol.33 , pp. 19-29
    • Gutiérrez, J.M.1    Romero, M.2    Díaz, C.3    Borkow, G.4    Ovadia, M.5
  • 14
    • 47249120139 scopus 로고    scopus 로고
    • The spectrum of complement alternative pathway-mediated diseases
    • Holers V.M. The spectrum of complement alternative pathway-mediated diseases. Immunol. Rev. 2008, 223:300-316.
    • (2008) Immunol. Rev. , vol.223 , pp. 300-316
    • Holers, V.M.1
  • 15
    • 2442667974 scopus 로고    scopus 로고
    • The alternative pathway of complement in disease: opportunities for therapeutic targeting
    • Holers V.M., Thurman J.M. The alternative pathway of complement in disease: opportunities for therapeutic targeting. Mol. Immunol. 2004, 41:147-152.
    • (2004) Mol. Immunol. , vol.41 , pp. 147-152
    • Holers, V.M.1    Thurman, J.M.2
  • 16
  • 17
    • 0036232455 scopus 로고    scopus 로고
    • A non-toxic anticoagulant metalloprotease: purification and characterization from India cobra (Naja naja naja) venom
    • Jagadeesha D.K., Shashidhara Murthy R., Girish K.S., Kemparaju K. A non-toxic anticoagulant metalloprotease: purification and characterization from India cobra (Naja naja naja) venom. Toxicon 2002, 40:667-675.
    • (2002) Toxicon , vol.40 , pp. 667-675
    • Jagadeesha, D.K.1    Shashidhara Murthy, R.2    Girish, K.S.3    Kemparaju, K.4
  • 18
    • 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 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 36849046139 scopus 로고    scopus 로고
    • Profiling the enzymatic properties and inhibition of human complement factor B
    • Le G.T., Abbenante G., Fairlie D.P. Profiling the enzymatic properties and inhibition of human complement factor B. J. Biol. Chem. 2007, 282:34809-34816.
    • (2007) J. Biol. Chem. , vol.282 , pp. 34809-34816
    • Le, G.T.1    Abbenante, G.2    Fairlie, D.P.3
  • 20
    • 0017377186 scopus 로고
    • Purification, characterization and analysis of the mechanism of action of four anti-complementary factors in Crotalus atrox venom
    • Man D.P., Minta J.O. Purification, characterization and analysis of the mechanism of action of four anti-complementary factors in Crotalus atrox venom. Immunochemistry 1977, 14:521-527.
    • (1977) Immunochemistry , vol.14 , pp. 521-527
    • Man, D.P.1    Minta, J.O.2
  • 22
    • 0025314948 scopus 로고
    • Isolation of two hemorrhagic toxins from Crotalus basiliscus basiliscus (Mexican west coast rattlesnake) venom and their effect on blood clotting and complement
    • Molina O., Seriel R.K., Martinez M., Sierra M.L., Varela-Ramirez A., Rael E.D. Isolation of two hemorrhagic toxins from Crotalus basiliscus basiliscus (Mexican west coast rattlesnake) venom and their effect on blood clotting and complement. Int. J. Biochem. 1990, 22:253-261.
    • (1990) Int. J. Biochem. , vol.22 , pp. 253-261
    • Molina, O.1    Seriel, R.K.2    Martinez, M.3    Sierra, M.L.4    Varela-Ramirez, A.5    Rael, E.D.6
  • 23
    • 22544457584 scopus 로고    scopus 로고
    • Strategies of therapeutic complement inhibition
    • Mollnes T.E., Kirschfink M. Strategies of therapeutic complement inhibition. Mol. Immunol. 2006, 43:107-121.
    • (2006) Mol. Immunol. , vol.43 , pp. 107-121
    • Mollnes, T.E.1    Kirschfink, M.2
  • 24
    • 0024205864 scopus 로고
    • A novel cleavage product of human complement component C3 with structural and functional properties of cobra venom factor
    • O'Keefe M.C., Caporale L.H., Vogel C.W. A novel cleavage product of human complement component C3 with structural and functional properties of cobra venom factor. J. Biol. Chem. 1988, 263:12690-12697.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12690-12697
    • O'Keefe, M.C.1    Caporale, L.H.2    Vogel, C.W.3
  • 25
    • 0017231072 scopus 로고
    • Fibrinogenolytic enzymes of Trimeresurus mucrosquamatus venom
    • Ouyang C., Teng C.M. Fibrinogenolytic enzymes of Trimeresurus mucrosquamatus venom. Biochim. Biophys. Acta 1976, 420:298-308.
    • (1976) Biochim. Biophys. Acta , vol.420 , pp. 298-308
    • Ouyang, C.1    Teng, C.M.2
  • 26
    • 0018088785 scopus 로고
    • Hemorrhagic toxins from rattlesnake (Crotalus atrox) venom. Pathogenesis of hemorrhage induced by three purified toxins
    • Ownby C.L., Bjarnason J., Tu A.T. Hemorrhagic toxins from rattlesnake (Crotalus atrox) venom. Pathogenesis of hemorrhage induced by three purified toxins. Am. J. Pathol. 1978, 93:201-210.
    • (1978) Am. J. Pathol. , vol.93 , pp. 201-210
    • Ownby, C.L.1    Bjarnason, J.2    Tu, A.T.3
  • 27
    • 0026689714 scopus 로고
    • Purification, characterization, and fibrinogen cleavage sites of three fibrinolytic enzymes from the venom of Crotalus basiliscus basiliscus
    • Retzios A.D., Markland F.S. Purification, characterization, and fibrinogen cleavage sites of three fibrinolytic enzymes from the venom of Crotalus basiliscus basiliscus. Biochemistry 1992, 31:4547-4557.
    • (1992) Biochemistry , vol.31 , pp. 4547-4557
    • Retzios, A.D.1    Markland, F.S.2
  • 28
    • 0023473794 scopus 로고
    • Rapid isoelectric focusing in a vertical polyacrylamide minigel system
    • Robertson E.F., Dannelly H.K., Malloy P.J., Reeves H.C. Rapid isoelectric focusing in a vertical polyacrylamide minigel system. Anal. Biochem. 1987, 167:290-294.
    • (1987) Anal. Biochem. , vol.167 , pp. 290-294
    • Robertson, E.F.1    Dannelly, H.K.2    Malloy, P.J.3    Reeves, H.C.4
  • 29
    • 33645978992 scopus 로고    scopus 로고
    • Emerging patterns in complement-mediated pathogen recognition
    • Roozendaal R., Carroll M.C. Emerging patterns in complement-mediated pathogen recognition. Cell 2006, 125:29-32.
    • (2006) Cell , vol.125 , pp. 29-32
    • Roozendaal, R.1    Carroll, M.C.2
  • 30
    • 0034501076 scopus 로고    scopus 로고
    • Complement: a critical test of its biological importance
    • Schmidt B.Z., Colten H.R. Complement: a critical test of its biological importance. Immunol. Rev. 2000, 178:166-176.
    • (2000) Immunol. Rev. , vol.178 , pp. 166-176
    • Schmidt, B.Z.1    Colten, H.R.2
  • 32
    • 0019297965 scopus 로고
    • The eighth component of human complement. Purification and physicochemical characterization of its unusual subunit structure
    • Steckel E.W., York R.G., Monahan J.B., Sodetz J.M. The eighth component of human complement. Purification and physicochemical characterization of its unusual subunit structure. J. Biol. Chem. 1980, 255:11997-12005.
    • (1980) J. Biol. Chem. , vol.255 , pp. 11997-12005
    • Steckel, E.W.1    York, R.G.2    Monahan, J.B.3    Sodetz, J.M.4
  • 33
    • 68849113423 scopus 로고    scopus 로고
    • Purification and characterization of a metalloproteinase with weak fibrinogenolytic activity from Naja atra venom
    • Sun Q.Y., Li M., Yang F.M. Purification and characterization of a metalloproteinase with weak fibrinogenolytic activity from Naja atra venom. Chin. J. Biochem. Mol. Biol. 2007, 23:835-843.
    • (2007) Chin. J. Biochem. Mol. Biol. , vol.23 , pp. 835-843
    • Sun, Q.Y.1    Li, M.2    Yang, F.M.3
  • 34
    • 0032433172 scopus 로고    scopus 로고
    • Evolution and diversity of the complement system of poikilothermic vertebrates
    • Sunyer J.O., Lambris J.D. Evolution and diversity of the complement system of poikilothermic vertebrates. Immunol. Rev. 1998, 166:39-57.
    • (1998) Immunol. Rev. , vol.166 , pp. 39-57
    • Sunyer, J.O.1    Lambris, J.D.2
  • 35
    • 31144460785 scopus 로고    scopus 로고
    • The central role of the alternative complement pathway in human disease
    • Thurman J.M., Holers V.M. The central role of the alternative complement pathway in human disease. J. Immunol. 2006, 176:1305-1310.
    • (2006) J. Immunol. , vol.176 , pp. 1305-1310
    • Thurman, J.M.1    Holers, V.M.2
  • 36
    • 0028607939 scopus 로고
    • Purification and characterization of fibrolase isoforms from venom of individual southern copperhead (Agkistrodon contortrix contortrix) snakes
    • Trikha M., Schmitmeier S., Markland F.S. Purification and characterization of fibrolase isoforms from venom of individual southern copperhead (Agkistrodon contortrix contortrix) snakes. Toxicon 1994, 32:1521-1531.
    • (1994) Toxicon , vol.32 , pp. 1521-1531
    • Trikha, M.1    Schmitmeier, S.2    Markland, F.S.3
  • 37
    • 0014150449 scopus 로고
    • Hemorrhagic and proteolytic activities of Thailand snake venoms
    • Tu A.T., Toom P.M., Ganthavorn S. Hemorrhagic and proteolytic activities of Thailand snake venoms. Biochem. Pharmacol. 1967, 16:2125-2130.
    • (1967) Biochem. Pharmacol. , vol.16 , pp. 2125-2130
    • Tu, A.T.1    Toom, P.M.2    Ganthavorn, S.3
  • 38
    • 0019479966 scopus 로고
    • Isolation and properties of a complement inhibitor from Naja haje venom, distinct from known anticomplementary factors in cobra venom
    • von Zabern I., Przyklenk H., Damerau B., Zimmermann B. Isolation and properties of a complement inhibitor from Naja haje venom, distinct from known anticomplementary factors in cobra venom. Scand. J. Immunol. 1981, 14:109-120.
    • (1981) Scand. J. Immunol. , vol.14 , pp. 109-120
    • von Zabern, I.1    Przyklenk, H.2    Damerau, B.3    Zimmermann, B.4
  • 39
    • 0035810399 scopus 로고    scopus 로고
    • Complement. First of two parts
    • Walport M.J. Complement. First of two parts. N. Engl. J. Med. 2001, 344:1058-1066.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1058-1066
    • Walport, M.J.1
  • 40
    • 0035849176 scopus 로고    scopus 로고
    • Complement. Second of two parts
    • Walport M.J. Complement. Second of two parts. N. Engl. J. Med. 2001, 344:1140-1144.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1140-1144
    • Walport, M.J.1
  • 41
    • 0010229714 scopus 로고    scopus 로고
    • Characterization of mocarhagin, a cobra venom metalloproteinase from Naja mocambique mocambique, and related proteins from other elapidae venoms
    • Ward C.M., Vinogradov D.V., Andrews R.K., Berndt M.C. Characterization of mocarhagin, a cobra venom metalloproteinase from Naja mocambique mocambique, and related proteins from other elapidae venoms. Toxicon 1996, 34:1203-1206.
    • (1996) Toxicon , vol.34 , pp. 1203-1206
    • Ward, C.M.1    Vinogradov, D.V.2    Andrews, R.K.3    Berndt, M.C.4
  • 43
    • 0036379701 scopus 로고    scopus 로고
    • Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase
    • Yamamoto C., Tsuru D., Oda-Ueda N., Ohno M., Hattori S., Kim S.T. Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase. Immunology 2002, 107:111-117.
    • (2002) Immunology , vol.107 , pp. 111-117
    • Yamamoto, C.1    Tsuru, D.2    Oda-Ueda, N.3    Ohno, M.4    Hattori, S.5    Kim, S.T.6
  • 44
    • 0032746270 scopus 로고    scopus 로고
    • Fibrinogenolytic properties of natrahagin (a proteinase from cobra venom) and its effect on human platelet aggregation
    • Zhu Z.G., Wu S.G. Fibrinogenolytic properties of natrahagin (a proteinase from cobra venom) and its effect on human platelet aggregation. Acta Pharmacol. Sin. 1999, 20:944-947.
    • (1999) Acta Pharmacol. Sin. , vol.20 , pp. 944-947
    • Zhu, Z.G.1    Wu, S.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.