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Volumn 49, Issue 5, 2007, Pages 734-739

Neutralization of the haemorrhagic activities of viperine snake venoms and venom metalloproteinases using synthetic peptide inhibitors and chelators

Author keywords

Chelator; Echis; Haemorrhagic activity; Metalloproteinase; Peptide inhibitor; Snake venom

Indexed keywords

CGS 27023A; CHELATING AGENT; EDETIC ACID; ETHYLENE GLYCOL 1,2 BIS(2 AMINOPHENYL) ETHER N,N,N',N' TETRAACETIC ACID; MARIMASTAT; METAL ION; METALLOPROTEINASE INHIBITOR; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PRINOMASTAT; SYNTHETIC PEPTIDE; TANOMASTAT; VIPER VENOM;

EID: 33947302585     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2006.11.020     Document Type: Article
Times cited : (69)

References (40)
  • 2
    • 0017883906 scopus 로고
    • Haemorrhagic toxins from Western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in haemorrhagic toxin e
    • Bjarnason J.B., and Tu A.T. Haemorrhagic toxins from Western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in haemorrhagic toxin e. Biochemistry 17 (1978) 3395-3404
    • (1978) Biochemistry , vol.17 , pp. 3395-3404
    • Bjarnason, J.B.1    Tu, A.T.2
  • 3
    • 0027291266 scopus 로고
    • Isolation and characterization of synergistic hemorrhagins from the venom of the snake Bothrops asper
    • Borkow G., Gutiérrez J.M., and Ovadia M. Isolation and characterization of synergistic hemorrhagins from the venom of the snake Bothrops asper. Toxicon 31 (1993) 1137-1150
    • (1993) Toxicon , vol.31 , pp. 1137-1150
    • Borkow, G.1    Gutiérrez, J.M.2    Ovadia, M.3
  • 4
    • 0031172832 scopus 로고    scopus 로고
    • Inhibition of the hemorrhagic activity of Bothrops asper venom by a novel neutralizing mixture
    • Borkow G., Gutiérrez J.M., and Ovadia M. Inhibition of the hemorrhagic activity of Bothrops asper venom by a novel neutralizing mixture. Toxicon 35 (1997) 865-877
    • (1997) Toxicon , vol.35 , pp. 865-877
    • Borkow, G.1    Gutiérrez, J.M.2    Ovadia, M.3
  • 5
    • 0037320124 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors-an emphasis on gastrointestinal malignancies
    • Chau I., Rigg A., and Cunningham D. Matrix metalloproteinase inhibitors-an emphasis on gastrointestinal malignancies. Crit. Rev. Oncol. Hematol. 45 (2003) 151-176
    • (2003) Crit. Rev. Oncol. Hematol. , vol.45 , pp. 151-176
    • Chau, I.1    Rigg, A.2    Cunningham, D.3
  • 7
    • 20444464925 scopus 로고    scopus 로고
    • Report of the 2nd International Conference on Envenomations in Africa (Deuxieme Colloque International sur les envenomations en Afrique)
    • Chippaux J.P., Stock R.P., and Alagon A. Report of the 2nd International Conference on Envenomations in Africa (Deuxieme Colloque International sur les envenomations en Afrique). Toxicon 46 (2005) 115-118
    • (2005) Toxicon , vol.46 , pp. 115-118
    • Chippaux, J.P.1    Stock, R.P.2    Alagon, A.3
  • 8
    • 0034662380 scopus 로고    scopus 로고
    • Effectiveness of batimastat, a synthetic inhibitor of matrix metalloproteinases, in neutralizing local tissue damage induced by BaP1, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper
    • Escalante T., Franceschi A., Rucavado A., and Gutierrez J.M. Effectiveness of batimastat, a synthetic inhibitor of matrix metalloproteinases, in neutralizing local tissue damage induced by BaP1, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper. Biochem. Pharmacol. 60 (2000) 269-274
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 269-274
    • Escalante, T.1    Franceschi, A.2    Rucavado, A.3    Gutierrez, J.M.4
  • 9
    • 0037155057 scopus 로고    scopus 로고
    • Matrix metalloproteinases in vascular remodelling and atherogenesis: the good, the bad, and the ugly
    • Galis Z.S., and Khatri J.J. Matrix metalloproteinases in vascular remodelling and atherogenesis: the good, the bad, and the ugly. Circ. Res. 90 (2002) 251-262
    • (2002) Circ. Res. , vol.90 , pp. 251-262
    • Galis, Z.S.1    Khatri, J.J.2
  • 10
    • 24344481759 scopus 로고    scopus 로고
    • Proteolytic, edematogenic and myotoxic activities of a hemorrhagic metalloproteinase isolated from Bothrops alternatus venom
    • Gay C.C., Leiva L.C., Marunak S., Teibler P., and Acosta de Perez O. Proteolytic, edematogenic and myotoxic activities of a hemorrhagic metalloproteinase isolated from Bothrops alternatus venom. Toxicon 46 (2005) 546-554
    • (2005) Toxicon , vol.46 , pp. 546-554
    • Gay, C.C.1    Leiva, L.C.2    Marunak, S.3    Teibler, P.4    Acosta de Perez, O.5
  • 11
    • 0032582674 scopus 로고    scopus 로고
    • Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus
    • Gong W., Zhu X., Liu S., Teng M., and Niu L. Crystal structures of acutolysin A, a three-disulfide hemorrhagic zinc metalloproteinase from the snake venom of Agkistrodon acutus. J. Mol. Biol. 283 (1998) 657-668
    • (1998) J. Mol. Biol. , vol.283 , pp. 657-668
    • Gong, W.1    Zhu, X.2    Liu, S.3    Teng, M.4    Niu, L.5
  • 12
    • 0033731921 scopus 로고    scopus 로고
    • Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage
    • Gutiérrez J.M., and Rucavado A. Snake venom metalloproteinases: their role in the pathogenesis of local tissue damage. Biochimie 82 (2000) 841-850
    • (2000) Biochimie , vol.82 , pp. 841-850
    • Gutiérrez, J.M.1    Rucavado, A.2
  • 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., Diaz C., Borkow G., and Ovadia M. Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo). Toxicon 33 (1995) 19-29
    • (1995) Toxicon , vol.33 , pp. 19-29
    • Gutiérrez, J.M.1    Romero, M.2    Diaz, C.3    Borkow, G.4    Ovadia, M.5
  • 14
    • 0344447110 scopus 로고    scopus 로고
    • Neutralization of local tissue damage induced by Bothrops asper (terciopelo) snake venom
    • Gutiérrez J.M., Leon G., Rojas G., Lomonte B., Rucavado A., and Chaves F. Neutralization of local tissue damage induced by Bothrops asper (terciopelo) snake venom. Toxicon 36 (1998) 1529-1538
    • (1998) Toxicon , vol.36 , pp. 1529-1538
    • Gutiérrez, J.M.1    Leon, G.2    Rojas, G.3    Lomonte, B.4    Rucavado, A.5    Chaves, F.6
  • 16
    • 0141594743 scopus 로고    scopus 로고
    • Novel sequences encoding venom C-type lectins are conserved in phylogenetically and geographically distinct Echis and Bitis viper species
    • Harrison R.A., Oliver J., Hasson S.S., Bharati K., and Theakston R.D.G. Novel sequences encoding venom C-type lectins are conserved in phylogenetically and geographically distinct Echis and Bitis viper species. Gene 315 (2003) 95-102
    • (2003) Gene , vol.315 , pp. 95-102
    • Harrison, R.A.1    Oliver, J.2    Hasson, S.S.3    Bharati, K.4    Theakston, R.D.G.5
  • 17
    • 0037376318 scopus 로고    scopus 로고
    • The conserved structure of snake venom toxins confers extensive immunological cross-reactivity to toxin-specific antibody
    • Harrison R.A., Wuster W., and Theakston R.D.G. The conserved structure of snake venom toxins confers extensive immunological cross-reactivity to toxin-specific antibody. Toxicon 41 (2003) 441-449
    • (2003) Toxicon , vol.41 , pp. 441-449
    • Harrison, R.A.1    Wuster, W.2    Theakston, R.D.G.3
  • 18
    • 1842584426 scopus 로고    scopus 로고
    • Development of venom toxin-specific antibodies by DNA immunisation: rationale and strategies to improve therapy of viper envenoming
    • Harrison R.A. Development of venom toxin-specific antibodies by DNA immunisation: rationale and strategies to improve therapy of viper envenoming. Vaccine 22 (2004) 1648-1655
    • (2004) Vaccine , vol.22 , pp. 1648-1655
    • Harrison, R.A.1
  • 19
    • 0034036315 scopus 로고    scopus 로고
    • Clinical potential of matrix metalloprotease inhibitors in cancer therapy
    • Heath E.I., and Grochow L.B. Clinical potential of matrix metalloprotease inhibitors in cancer therapy. Drugs 59 (2000) 1043-1055
    • (2000) Drugs , vol.59 , pp. 1043-1055
    • Heath, E.I.1    Grochow, L.B.2
  • 20
    • 0035819527 scopus 로고    scopus 로고
    • Development of matrix metalloproteinase inhibitors in cancer therapy
    • Hidalgo M., and Eckhardt S.G. Development of matrix metalloproteinase inhibitors in cancer therapy. J. Natl. Cancer Instrum. 93 (2001) 178-193
    • (2001) J. Natl. Cancer Instrum. , vol.93 , pp. 178-193
    • Hidalgo, M.1    Eckhardt, S.G.2
  • 21
    • 0141767106 scopus 로고    scopus 로고
    • The purification and partial characterisation of two novel metalloproteinases from the venom of the West African carpet viper, Echis ocellatus
    • Howes J.-M., Wilkinson M.C., Theakston R.D.G., and Laing G.D. The purification and partial characterisation of two novel metalloproteinases from the venom of the West African carpet viper, Echis ocellatus. Toxicon 42 (2003) 21-27
    • (2003) Toxicon , vol.42 , pp. 21-27
    • Howes, J.-M.1    Wilkinson, M.C.2    Theakston, R.D.G.3    Laing, G.D.4
  • 22
    • 20444415636 scopus 로고    scopus 로고
    • Effects of three novel metalloproteinases from the venom of the West African saw-scaled viper, Echis carinatus on blood coagulation and platelets
    • Howes J.-M., Kamiguti A.S., Theakston R.D.G., Wilkinson M.C., and Laing G.D. Effects of three novel metalloproteinases from the venom of the West African saw-scaled viper, Echis carinatus on blood coagulation and platelets. Biochim. Biophys. Act. Gen. Sub. 1724 (2005) 194-202
    • (2005) Biochim. Biophys. Act. Gen. Sub. , vol.1724 , pp. 194-202
    • Howes, J.-M.1    Kamiguti, A.S.2    Theakston, R.D.G.3    Wilkinson, M.C.4    Laing, G.D.5
  • 23
    • 0023607649 scopus 로고
    • A study of local necrosis induced by Naja nigricollis (spitting cobra) venom using simple histological staining techniques
    • Iddon D., Theakston R.D.G., and Ownby C.L. A study of local necrosis induced by Naja nigricollis (spitting cobra) venom using simple histological staining techniques. Toxicon 25 (1987) 665-672
    • (1987) Toxicon , vol.25 , pp. 665-672
    • Iddon, D.1    Theakston, R.D.G.2    Ownby, C.L.3
  • 24
    • 0036232455 scopus 로고    scopus 로고
    • A non-toxic anticoagulant metalloprotease: purification and characterization from Indian cobra (Naja naja naja) venom
    • Jagadeesha D.K., Shashidhara murthy R., Girish K.S., and Kemparaju K. A non-toxic anticoagulant metalloprotease: purification and characterization from Indian cobra (Naja naja naja) venom. Toxicon 40 (2002) 667-675
    • (2002) Toxicon , vol.40 , pp. 667-675
    • Jagadeesha, D.K.1    Shashidhara murthy, R.2    Girish, K.S.3    Kemparaju, K.4
  • 25
    • 0030976889 scopus 로고    scopus 로고
    • Function of disintegrin-like/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists
    • Jia L.G., Wang X.M., Shannon J.D., Bjarnason J.B., and Fox J.W. Function of disintegrin-like/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists. J. Biol. Chem. 272 (1997) 13094-13102
    • (1997) J. Biol. Chem. , vol.272 , pp. 13094-13102
    • Jia, L.G.1    Wang, X.M.2    Shannon, J.D.3    Bjarnason, J.B.4    Fox, J.W.5
  • 28
    • 0031596131 scopus 로고    scopus 로고
    • Inhibition by CaNa2EDTA of local tissue damage induced by Bothrops asper (terciopelo) venom: application in horse immunization for antivenom production
    • Leon G., Estrada R., Chaves F., Rojas G., Ovadia M., and Gutierrez J.M. Inhibition by CaNa2EDTA of local tissue damage induced by Bothrops asper (terciopelo) venom: application in horse immunization for antivenom production. Toxicon 36 (1998) 321-331
    • (1998) Toxicon , vol.36 , pp. 321-331
    • Leon, G.1    Estrada, R.2    Chaves, F.3    Rojas, G.4    Ovadia, M.5    Gutierrez, J.M.6
  • 31
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H., and Woessner Jr. J.F. Matrix metalloproteinases. J. Biol. Chem, 274 (1999) 21491-21494
    • (1999) J. Biol. Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner Jr., J.F.2
  • 33
    • 0034438185 scopus 로고    scopus 로고
    • Inhibition of local hemorrhage and dermonecrosis induced by Bothrops asper snake venom: effectiveness of early in situ administration of the peptidomimetic metalloproteinase inhibitor batimastat and the chelating agent CaNa2EDTA
    • Rucavado A., Escalante T., Franceschi A., Chaves F., Leon G., Cury Y., Ovadia M., and Gutiérrez J.M. Inhibition of local hemorrhage and dermonecrosis induced by Bothrops asper snake venom: effectiveness of early in situ administration of the peptidomimetic metalloproteinase inhibitor batimastat and the chelating agent CaNa2EDTA. Am. J. Trop. Med. Hyg. 63 (2000) 313-319
    • (2000) Am. J. Trop. Med. Hyg. , vol.63 , pp. 313-319
    • Rucavado, A.1    Escalante, T.2    Franceschi, A.3    Chaves, F.4    Leon, G.5    Cury, Y.6    Ovadia, M.7    Gutiérrez, J.M.8
  • 34
    • 1642462834 scopus 로고    scopus 로고
    • Effect of the metalloproteinase inhibitor batimastat in the systemic toxicity induced by Bothrops asper snake venom: understanding the role of metalloproteinases in envenomation
    • Rucavado A., Escalante T., and Gutiérrez J.M. Effect of the metalloproteinase inhibitor batimastat in the systemic toxicity induced by Bothrops asper snake venom: understanding the role of metalloproteinases in envenomation. Toxicon 43 (2004) 417-424
    • (2004) Toxicon , vol.43 , pp. 417-424
    • Rucavado, A.1    Escalante, T.2    Gutiérrez, J.M.3
  • 35
    • 0032895433 scopus 로고    scopus 로고
    • Recent advances in inhibitors of matrix metalloproteinases for cancer therapy
    • Sugita K. Recent advances in inhibitors of matrix metalloproteinases for cancer therapy. IDrugs 2 (1999) 327-339
    • (1999) IDrugs , vol.2 , pp. 327-339
    • Sugita, K.1
  • 36
    • 0026792603 scopus 로고
    • A comparative study of the biological properties of venoms of some old world vipers (subfamily viperinae)
    • Tan N.-H., and Ponnudurai G. A comparative study of the biological properties of venoms of some old world vipers (subfamily viperinae). Int. J. Biochem. 24 (1992) 331-336
    • (1992) Int. J. Biochem. , vol.24 , pp. 331-336
    • Tan, N.-H.1    Ponnudurai, G.2
  • 37
    • 0021061641 scopus 로고
    • Development of simple assay procedures for the characterisation of snake venoms
    • Theakston R.D.G., and Reid H.A. Development of simple assay procedures for the characterisation of snake venoms. Bull. WHO 61 (1983) 949-956
    • (1983) Bull. WHO , vol.61 , pp. 949-956
    • Theakston, R.D.G.1    Reid, H.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.