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Volumn 47, Issue 5, 2006, Pages 549-559

Inflammatory effects of BaP1 a metalloproteinase isolated from Bothrops asper snake venom: Leukocyte recruitment and release of cytokines

Author keywords

Adhesion molecules; Cytokines; Leukocytes; Metalloproteinase; Snake venom

Indexed keywords

ANTIBODY; CD18 ANTIGEN; CD31 ANTIGEN; CELL ADHESION MOLECULE; CYTOKINE; EDETIC ACID; INTERCELLULAR ADHESION MOLECULE 1; INTERLEUKIN 1; L SELECTIN; LEUKOTRIENE B4; LYMPHOCYTE FUNCTION ASSOCIATED ANTIGEN 1; METALLOPROTEINASE; PROTEIN BAP1; SNAKE VENOM; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 33645963111     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2006.01.009     Document Type: Article
Times cited : (70)

References (69)
  • 1
    • 0031134090 scopus 로고    scopus 로고
    • L-selectin shedding does not regulate human neutrophil attachment, rolling, or transmigration across human vascular endothelium in vitro
    • Allport J.R., Ding H.T., Ager A., Steeber D.A., Tedder T.F., and Luscinskas F.W. L-selectin shedding does not regulate human neutrophil attachment, rolling, or transmigration across human vascular endothelium in vitro. J. Immunol. 158 (1997) 4365-4372
    • (1997) J. Immunol. , vol.158 , pp. 4365-4372
    • Allport, J.R.1    Ding, H.T.2    Ager, A.3    Steeber, D.A.4    Tedder, T.F.5    Luscinskas, F.W.6
  • 3
    • 0023118407 scopus 로고
    • Cachectin: more than a tumor necrosis factor
    • Beutler B., and Cerami A. Cachectin: more than a tumor necrosis factor. N. Engl. J. Med. 316 (1987) 379-385
    • (1987) N. Engl. J. Med. , vol.316 , pp. 379-385
    • Beutler, B.1    Cerami, A.2
  • 5
    • 0028146808 scopus 로고
    • Hemorrhagic metalloproteinases from snake venoms
    • Bjarnason J.B., and Fox J.W. Hemorrhagic metalloproteinases from snake venoms. Pharmacol. Ther. 62 (1994) 325-372
    • (1994) Pharmacol. Ther. , vol.62 , pp. 325-372
    • Bjarnason, J.B.1    Fox, J.W.2
  • 6
    • 0029055393 scopus 로고
    • Snake venom metalloendopeptidases: reprolysins
    • Bjarnason J.B., and 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
  • 7
    • 0017883906 scopus 로고
    • Hemorrhagic toxins from western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin
    • Bjarnason J.B., and Tu A.T. Hemorrhagic toxins from western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin. Biochemistry 17 (1978) 3395-3404
    • (1978) Biochemistry , vol.17 , pp. 3395-3404
    • Bjarnason, J.B.1    Tu, A.T.2
  • 9
    • 0030834283 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF-alpha and notch
    • (Review)
    • Blobel C.P. Metalloprotease-disintegrins: links to cell adhesion and cleavage of TNF-alpha and notch. Cell 90 (1997) 589-592 (Review)
    • (1997) Cell , vol.90 , pp. 589-592
    • Blobel, C.P.1
  • 10
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'
    • Bode W., Gomis-Ruth F., and Stockler W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett. 331 (1993) 134-140
    • (1993) FEBS Lett. , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Ruth, F.2    Stockler, W.3
  • 11
    • 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
  • 12
    • 0033613949 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-3 inhibits shedding of L-selectin from leukocytes
    • Borland G., Murphy G., and Ager A. Tissue inhibitor of metalloproteinases-3 inhibits shedding of L-selectin from leukocytes. J. Biol. Chem. 274 (1999) 2810-2815
    • (1999) J. Biol. Chem. , vol.274 , pp. 2810-2815
    • Borland, G.1    Murphy, G.2    Ager, A.3
  • 13
    • 0029766216 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors and the prevention of connective tissue breakdown
    • (Review)
    • Cawston T.E. Metalloproteinase inhibitors and the prevention of connective tissue breakdown. Pharmacol. Ther. 70 (1996) 163-182 (Review)
    • (1996) Pharmacol. Ther. , vol.70 , pp. 163-182
    • Cawston, T.E.1
  • 14
    • 0030255831 scopus 로고    scopus 로고
    • Metalloproteinases in the rheumatic diseases
    • Cawston T.E., and Billington C. Metalloproteinases in the rheumatic diseases. J. Pathol. 180 (1996) 115-117
    • (1996) J. Pathol. , vol.180 , pp. 115-117
    • Cawston, T.E.1    Billington, C.2
  • 15
    • 0032428679 scopus 로고    scopus 로고
    • Snake-bites: appraisal of the global situation
    • Chippaux J.P. Snake-bites: appraisal of the global situation. Bull. World Health Organ. 76 (1998) 515-524
    • (1998) Bull. World Health Organ. , vol.76 , pp. 515-524
    • Chippaux, J.P.1
  • 16
    • 0034898736 scopus 로고    scopus 로고
    • The effect of jararhagin, a metalloproteinase from Bothrops jararaca venom, on pro-inflammatory cytokines released by murine peritoneal adherent cells
    • Clissa P.B., Laing G.D., Theakston R.D.G., Mota I., Taylor M.J., and Moura-Da-Silva A.M. The effect of jararhagin, a metalloproteinase from Bothrops jararaca venom, on pro-inflammatory cytokines released by murine peritoneal adherent cells. Toxicon 39 (2001) 1567-1573
    • (2001) Toxicon , vol.39 , pp. 1567-1573
    • Clissa, P.B.1    Laing, G.D.2    Theakston, R.D.G.3    Mota, I.4    Taylor, M.J.5    Moura-Da-Silva, A.M.6
  • 17
    • 0036126314 scopus 로고    scopus 로고
    • Importance of metalloproteinases and macrophages in viper venoms induced local inflammation
    • Costa E.P., Clissa P.B., Teixeira C.F.P., and Moura-Da-Silva A.M. Importance of metalloproteinases and macrophages in viper venoms induced local inflammation. Inflammation 26 (2002) 13-17
    • (2002) Inflammation , vol.26 , pp. 13-17
    • Costa, E.P.1    Clissa, P.B.2    Teixeira, C.F.P.3    Moura-Da-Silva, A.M.4
  • 18
    • 0016772348 scopus 로고
    • Comparison of agents producing a neutrophilic leukocytosis in man
    • Dale D.C., Fauci A.S., Guerry D.P., and Wolff S.M. Comparison of agents producing a neutrophilic leukocytosis in man. J. Clin. Invest. 56 (1957) 808-813
    • (1957) J. Clin. Invest. , vol.56 , pp. 808-813
    • Dale, D.C.1    Fauci, A.S.2    Guerry, D.P.3    Wolff, S.M.4
  • 19
    • 0030094287 scopus 로고    scopus 로고
    • Role of gelatinase B and elastase in human polymorphonuclear neutrophil migration across basement membrane
    • Delclaux C., Delacourt C., D'ortho M.P., Boyer V., Lafuma C., and Harf A. Role of gelatinase B and elastase in human polymorphonuclear neutrophil migration across basement membrane. Am. J. Respir. Cell Mol. Biol. 14 (1996) 288-295
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.14 , pp. 288-295
    • Delclaux, C.1    Delacourt, C.2    D'ortho, M.P.3    Boyer, V.4    Lafuma, C.5    Harf, A.6
  • 20
    • 0023953471 scopus 로고
    • Biology of interleukin-1
    • Dinarello C.A. Biology of interleukin-1. FASEB J. 2 (1988) 108-115
    • (1988) FASEB J. , vol.2 , pp. 108-115
    • Dinarello, C.A.1
  • 21
    • 0032764894 scopus 로고    scopus 로고
    • Molecular mechanisms that control leukocyte extravasation: the selections and the chemokines
    • Ebnet K., and Vestweber D. Molecular mechanisms that control leukocyte extravasation: the selections and the chemokines. Histochem. Cell Biol. 112 (1999) 1-23
    • (1999) Histochem. Cell Biol. , vol.112 , pp. 1-23
    • Ebnet, K.1    Vestweber, D.2
  • 22
    • 85063445768 scopus 로고
    • Clinical toxicology of snakebite in north América
    • Meier J., and White J. (Eds), CRC Press, Boca Raton, FL
    • Fan W.H., and Cardoso J.L. Clinical toxicology of snakebite in north América. In: Meier J., and White J. (Eds). Handbook of Clinical Toxicology of Animal Venoms and Poisons (1995), CRC Press, Boca Raton, FL 667-688
    • (1995) Handbook of Clinical Toxicology of Animal Venoms and Poisons , pp. 667-688
    • Fan, W.H.1    Cardoso, J.L.2
  • 24
    • 0034101628 scopus 로고    scopus 로고
    • The role of metalloproteinase and adhesion molecules in interleukin-8-induced stem-cell mobilization
    • Fibbe W.E., Pruijt J.F., Van Kooyk Y., Figdor C.G., Opdenakker G., and Willemze R. The role of metalloproteinase and adhesion molecules in interleukin-8-induced stem-cell mobilization. Semin. Hematol. 37 (2000) 19-24
    • (2000) Semin. Hematol. , vol.37 , pp. 19-24
    • Fibbe, W.E.1    Pruijt, J.F.2    Van Kooyk, Y.3    Figdor, C.G.4    Opdenakker, G.5    Willemze, R.6
  • 25
    • 0002655721 scopus 로고    scopus 로고
    • ADAMs / MDC family of proteins and their relationships to the snake venom metalloproteinases
    • Bayley G.S. (Ed), Alaken, Fort Colli, CO
    • Fox J.W., and Long C. ADAMs / MDC family of proteins and their relationships to the snake venom metalloproteinases. In: Bayley G.S. (Ed). Enzymes from Snake Venom (1998), Alaken, Fort Colli, CO 151-178
    • (1998) Enzymes from Snake Venom , pp. 151-178
    • Fox, J.W.1    Long, C.2
  • 26
    • 0033991114 scopus 로고    scopus 로고
    • Purification and characterization of BaH4, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper
    • Franceschi A., Rucavado A., Mora N., and Gutiérrez J.M. Purification and characterization of BaH4, a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper. Toxicon 38 (2000) 63-77
    • (2000) Toxicon , vol.38 , pp. 63-77
    • Franceschi, A.1    Rucavado, A.2    Mora, N.3    Gutiérrez, J.M.4
  • 28
    • 85063475698 scopus 로고
    • Clinical toxicology of snakebite in north América
    • Meier J., and White J. (Eds), CRC Press, Boca Raton, FL
    • Gómez H., and Dart R.C. Clinical toxicology of snakebite in north América. In: Meier J., and White J. (Eds). Handbook of Clinical Toxicology of Animal Venoms and Poisons (1995), CRC Press, Boca Raton, FL 619-644
    • (1995) Handbook of Clinical Toxicology of Animal Venoms and Poisons , pp. 619-644
    • Gómez, H.1    Dart, R.C.2
  • 29
    • 0002852055 scopus 로고
    • Clinical toxicology of snakebite in central America
    • Meier J., and White J. (Eds), CRC Press, Boca Raton FL
    • Gutiérrez J.M. Clinical toxicology of snakebite in central America. In: Meier J., and White J. (Eds). Handbook of Clinical Toxicology of Animal Venoms and Poisons (1995), CRC Press, Boca Raton FL 667-668
    • (1995) Handbook of Clinical Toxicology of Animal Venoms and Poisons , pp. 667-668
    • Gutiérrez, J.M.1
  • 30
    • 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., 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    Díaz, C.3    Borkow, G.4    Ovadia, M.5
  • 31
    • 19544381172 scopus 로고    scopus 로고
    • Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage
    • Gutiérrez J.M., Rucavado A., Escalante T., and Díaz C. Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage. Toxicon 45 (2005) 997-1011
    • (2005) Toxicon , vol.45 , pp. 997-1011
    • Gutiérrez, J.M.1    Rucavado, A.2    Escalante, T.3    Díaz, C.4
  • 33
    • 0026886317 scopus 로고
    • A new family of proteinases is defined by several snake venom metalloproteinases
    • Hite L.A., Fox J.W., and Bjarnason J.B. A new family of proteinases is defined by several snake venom metalloproteinases. Biol. Chem. Hoppe-Seyler 373 (1992) 381-385
    • (1992) Biol. Chem. Hoppe-Seyler , vol.373 , pp. 381-385
    • Hite, L.A.1    Fox, J.W.2    Bjarnason, J.B.3
  • 34
    • 0028337108 scopus 로고
    • cDNA sequences for four snake venom metalloproteinases: structure, classification and their relationship to mammalian reproductive proteins
    • Hite L.A., Jia L.G., Bjarnason J.B., and Fox J.W. cDNA sequences for four snake venom metalloproteinases: structure, classification and their relationship to mammalian reproductive proteins. Arch. Biophys. 308 (1994) 182-191
    • (1994) Arch. Biophys. , vol.308 , pp. 182-191
    • Hite, L.A.1    Jia, L.G.2    Bjarnason, J.B.3    Fox, J.W.4
  • 35
    • 0034190238 scopus 로고    scopus 로고
    • Intercellular adhesion molecule-1 (ICAM-1) expression and cell signaling cascades
    • Hubbard A., and Rothlein R. Intercellular adhesion molecule-1 (ICAM-1) expression and cell signaling cascades. Free Radical Biol. Med. 28 (2000) 1379-1386
    • (2000) Free Radical Biol. Med. , vol.28 , pp. 1379-1386
    • Hubbard, A.1    Rothlein, R.2
  • 36
    • 0035259951 scopus 로고    scopus 로고
    • Role of interleukin-1 in induction of matrix metalloproteinases synthesized by rat temporomandibular joint chondrocytes and disc cells
    • Ijima Y., Kobayashi M., and Kubota E. Role of interleukin-1 in induction of matrix metalloproteinases synthesized by rat temporomandibular joint chondrocytes and disc cells. Eur. J. Oral Sci. 109 (2001) 50-59
    • (2001) Eur. J. Oral Sci. , vol.109 , pp. 50-59
    • Ijima, Y.1    Kobayashi, M.2    Kubota, E.3
  • 37
    • 0032932566 scopus 로고    scopus 로고
    • Role of ICAM-1 and ICAM-2 and alternate CD11/CD18 ligands in neutrophil transendothelial migration
    • Issekutz A.C., Rowter D., and Springer T.A. Role of ICAM-1 and ICAM-2 and alternate CD11/CD18 ligands in neutrophil transendothelial migration. J. Leukoc. Biol. 65 (1999) 117-126
    • (1999) J. Leukoc. Biol. , vol.65 , pp. 117-126
    • Issekutz, A.C.1    Rowter, D.2    Springer, T.A.3
  • 38
    • 0031847147 scopus 로고    scopus 로고
    • Snake venom metalloproteinases and disintegrins: interactions with cells
    • Kamiguti A.S., Zuzel M., and Theakston R.D.G. Snake venom metalloproteinases and disintegrins: interactions with cells. Braz. J. Med. Biol. Res. 31 (1998) 853-862
    • (1998) Braz. J. Med. Biol. Res. , vol.31 , pp. 853-862
    • Kamiguti, A.S.1    Zuzel, M.2    Theakston, R.D.G.3
  • 39
    • 0037213682 scopus 로고    scopus 로고
    • IL-6: a regulator of the transition from neutrophil to monocyte recruitment during inflammation
    • Kaplanski G., Marin V., Montero-Julian F., Mantovani A., and Farnarier C. IL-6: a regulator of the transition from neutrophil to monocyte recruitment during inflammation. Trends Immunol. 24 (2003) 25-29
    • (2003) Trends Immunol. , vol.24 , pp. 25-29
    • Kaplanski, G.1    Marin, V.2    Montero-Julian, F.3    Mantovani, A.4    Farnarier, C.5
  • 40
    • 12344299684 scopus 로고    scopus 로고
    • Interleukin-1 stimulates cytokines, prostaglandin E2 and matrix metalloproteinase-1 production via activation of MAPK/AP-1 and NF-kappaB in human gingival fibroblasts
    • Kida Y., Kobayashi M., Suzuki T., Takeshita A., Okamatsu Y., Hanazawa S., Yasui T., and Hasegawa K. Interleukin-1 stimulates cytokines, prostaglandin E2 and matrix metalloproteinase-1 production via activation of MAPK/AP-1 and NF-kappaB in human gingival fibroblasts. Cytokine 29 (2005) 159-168
    • (2005) Cytokine , vol.29 , pp. 159-168
    • Kida, Y.1    Kobayashi, M.2    Suzuki, T.3    Takeshita, A.4    Okamatsu, Y.5    Hanazawa, S.6    Yasui, T.7    Hasegawa, K.8
  • 41
    • 0025854524 scopus 로고
    • Leukocytes roll on a selectin at physiologic flow rates: distinction from and prerequisite for adhesion through integrins
    • Lawrence M.B., and Springer T.A. Leukocytes roll on a selectin at physiologic flow rates: distinction from and prerequisite for adhesion through integrins. Cell 65 (1991) 859-873
    • (1991) Cell , vol.65 , pp. 859-873
    • Lawrence, M.B.1    Springer, T.A.2
  • 42
    • 0032402107 scopus 로고    scopus 로고
    • Snake venoms and the hemostatic system
    • Markland F.S. Snake venoms and the hemostatic system. Toxicon 36 (1998) 1749-1756
    • (1998) Toxicon , vol.36 , pp. 1749-1756
    • Markland, F.S.1
  • 44
    • 0034113347 scopus 로고    scopus 로고
    • Increments in serum cytokine and nitric oxide levels in mice injected with Bothrops asper and Bothrops jararaca snake venoms
    • Petricevich V.L., Teixeira C.F.P., Tambourgi D.V., and Gutiérrez J.M. Increments in serum cytokine and nitric oxide levels in mice injected with Bothrops asper and Bothrops jararaca snake venoms. Toxicon 38 (2000) 1253-1266
    • (2000) Toxicon , vol.38 , pp. 1253-1266
    • Petricevich, V.L.1    Teixeira, C.F.P.2    Tambourgi, D.V.3    Gutiérrez, J.M.4
  • 45
    • 0022074792 scopus 로고
    • Enzyme immunoassays of eicosanoids using acetylcholine esterase as label: an alternative to radioimmunoassay
    • Pradelles P., Grassi J., and Mac Louf J. Enzyme immunoassays of eicosanoids using acetylcholine esterase as label: an alternative to radioimmunoassay. Anal. Chem. 57 (1985) 1170-1173
    • (1985) Anal. Chem. , vol.57 , pp. 1170-1173
    • Pradelles, P.1    Grassi, J.2    Mac Louf, J.3
  • 46
    • 0031148627 scopus 로고    scopus 로고
    • Cross-talk between cell adhesion molecules regulates the migration velocity of neutrophils
    • Rainger G.E., Buckley C., Simmons D.L., and Nash G.B. Cross-talk between cell adhesion molecules regulates the migration velocity of neutrophils. Curr. Biol. 7 (1997) 316-325
    • (1997) Curr. Biol. , vol.7 , pp. 316-325
    • Rainger, G.E.1    Buckley, C.2    Simmons, D.L.3    Nash, G.B.4
  • 47
    • 4644372665 scopus 로고    scopus 로고
    • Comparative analysis of the catalytic domain of hemorrhagic and non-hemorrhagic snake venom metallopeptidases using bioinformatic tools
    • Ramos O.H., and Selistre-De-Araújo H.S. Comparative analysis of the catalytic domain of hemorrhagic and non-hemorrhagic snake venom metallopeptidases using bioinformatic tools. Toxicon 44 (2004) 529-538
    • (2004) Toxicon , vol.44 , pp. 529-538
    • Ramos, O.H.1    Selistre-De-Araújo, H.S.2
  • 48
    • 3042777503 scopus 로고    scopus 로고
    • Production of matrix metalloproteinase-9 by cord blood CD34+ cells and its role in migration
    • Rao Q., Zheng G.G., Lin Y.M., and Wu K.F. Production of matrix metalloproteinase-9 by cord blood CD34+ cells and its role in migration. Ann. Hematol. 83 (2004) 409-413
    • (2004) Ann. Hematol. , vol.83 , pp. 409-413
    • Rao, Q.1    Zheng, G.G.2    Lin, Y.M.3    Wu, K.F.4
  • 50
    • 0001495821 scopus 로고
    • Symptomatology, pathology and treatment of snake bites in south América
    • Venomous Animals and their Venoms. Bucherl W., and Buckley E. (Eds), Academic Press, New York
    • Rosenfeld G. Symptomatology, pathology and treatment of snake bites in south América. In: Bucherl W., and Buckley E. (Eds). Venomous Animals and their Venoms. Venomous Vertebrates vol. II (1971), Academic Press, New York 345-384
    • (1971) Venomous Vertebrates , vol.II , pp. 345-384
    • Rosenfeld, G.1
  • 51
    • 0029432140 scopus 로고
    • Local tissue damage induced by BaP1, a metalloproteinase isolated from Bothrops asper (terciopelo) snake venom
    • Rucavado A., Lomonte B., Ovadia M., and Gutiérrez J.M. Local tissue damage induced by BaP1, a metalloproteinase isolated from Bothrops asper (terciopelo) snake venom. Exp. Mol. Pathol. 63 (1995) 186-199
    • (1995) Exp. Mol. Pathol. , vol.63 , pp. 186-199
    • Rucavado, A.1    Lomonte, B.2    Ovadia, M.3    Gutiérrez, J.M.4
  • 52
    • 0031661318 scopus 로고    scopus 로고
    • Blister formation and skin damage induced by BaP1, a haemorrhagic metalloproteinase from the venom of the snake Bothrops asper
    • Rucavado A., Núnez J., and Gutiérrez J.M. Blister formation and skin damage induced by BaP1, a haemorrhagic metalloproteinase from the venom of the snake Bothrops asper. Int. J. Exp. Path. 79 (1998) 245-254
    • (1998) Int. J. Exp. Path. , vol.79 , pp. 245-254
    • Rucavado, A.1    Núnez, J.2    Gutiérrez, J.M.3
  • 53
    • 0036096413 scopus 로고    scopus 로고
    • Local production of cytokines and matrix metalloproteinases after intramuscular injection of a myotoxic phospholipase A2 and a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper
    • Rucavado A., Escalante T., Teixeira C.F.P., Fernandes C.M., Moura-Da-Silva A.M., Díaz C., and Gutiérrez J.M. Local production of cytokines and matrix metalloproteinases after intramuscular injection of a myotoxic phospholipase A2 and a hemorrhagic metalloproteinase from the venom of the snake Bothrops asper. Med. Inflamm. 11 (2002) 121-128
    • (2002) Med. Inflamm. , vol.11 , pp. 121-128
    • Rucavado, A.1    Escalante, T.2    Teixeira, C.F.P.3    Fernandes, C.M.4    Moura-Da-Silva, A.M.5    Díaz, C.6    Gutiérrez, J.M.7
  • 54
    • 0019523161 scopus 로고
    • Rabbit tumor necrosis factor: machanism of action
    • Ruff M.R., and Gifford G.E. Rabbit tumor necrosis factor: machanism of action. Infect. Immun. 31 (1981) 380-385
    • (1981) Infect. Immun. , vol.31 , pp. 380-385
    • Ruff, M.R.1    Gifford, G.E.2
  • 55
    • 0017581660 scopus 로고
    • Acute inflammation
    • Ryan G.B., and Majno G. Acute inflammation. Am. J. Pathol. 86 (1977) 185-274
    • (1977) Am. J. Pathol. , vol.86 , pp. 185-274
    • Ryan, G.B.1    Majno, G.2
  • 56
    • 0023693868 scopus 로고
    • The characterization of four monoclonal antibodies specific for mouse IL-5 and development of mouse and human IL-5 ELISA
    • Schumaker J.H., O'Garra A., Schrader B., Van Kimmeenade A., Bond M.W., Mosmann T.R., and Coffman R.L. The characterization of four monoclonal antibodies specific for mouse IL-5 and development of mouse and human IL-5 ELISA. J. Immunol. 141 (1988) 1576-1581
    • (1988) J. Immunol. , vol.141 , pp. 1576-1581
    • Schumaker, J.H.1    O'Garra, A.2    Schrader, B.3    Van Kimmeenade, A.4    Bond, M.W.5    Mosmann, T.R.6    Coffman, R.L.7
  • 59
    • 0024997837 scopus 로고
    • The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis
    • Takeya H., Oda K., Miyata T., Omori-Satoh T., and Iwanaga S. The complete amino acid sequence of the high molecular mass hemorrhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis. J. Biol. Chem. 265 (1990) 16068-16073
    • (1990) J. Biol. Chem. , vol.265 , pp. 16068-16073
    • Takeya, H.1    Oda, K.2    Miyata, T.3    Omori-Satoh, T.4    Iwanaga, S.5
  • 60
    • 0035071646 scopus 로고    scopus 로고
    • Transforming growth factor-β suppresses tumor necrosis factor α-induced matrix metalloproteinase-9 expression in monocytes
    • Vaday G.G., Schor H., Rahat M.A., Lahat N., and Lider O. Transforming growth factor-β suppresses tumor necrosis factor α-induced matrix metalloproteinase-9 expression in monocytes. J. Leukoc. Biol. 69 (2001) 613-621
    • (2001) J. Leukoc. Biol. , vol.69 , pp. 613-621
    • Vaday, G.G.1    Schor, H.2    Rahat, M.A.3    Lahat, N.4    Lider, O.5
  • 61
    • 0026717674 scopus 로고
    • The pathophysiology of tumor necrosis factors
    • Vassalli P. The pathophysiology of tumor necrosis factors. Annu. Rev. Immunol. 10 (1992) 411-452
    • (1992) Annu. Rev. Immunol. , vol.10 , pp. 411-452
    • Vassalli, P.1
  • 64
    • 0002414874 scopus 로고    scopus 로고
    • Clinical features of envenoming from snake bites
    • Bon C., and Goyffon M. (Eds), Editions Foundation Marcel Mérieux, Lyon
    • Warrel D.A. Clinical features of envenoming from snake bites. In: Bon C., and Goyffon M. (Eds). Envenomings and their Treatments (1996), Editions Foundation Marcel Mérieux, Lyon 63-76
    • (1996) Envenomings and their Treatments , pp. 63-76
    • Warrel, D.A.1
  • 66
    • 0029769940 scopus 로고    scopus 로고
    • Cytokine receptor signal transduction and the control of hematopoietic stem cell development
    • Watowich S.S., Wu H., and Socolovsky M. Cytokine receptor signal transduction and the control of hematopoietic stem cell development. Annu. Rev. Cell Dev. Biol. 12 (1996) 91-128
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 91-128
    • Watowich, S.S.1    Wu, H.2    Socolovsky, M.3
  • 67
    • 0024298861 scopus 로고
    • Purification and biochemical characterization of atroxase, a nonhemorrhagic fibrinolytic protease from western diamondback rattlesnake venom
    • Willis T.W., and 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
  • 68
    • 0034894386 scopus 로고    scopus 로고
    • Bothrops asper and Bothrops jararaca snake venoms trigger microbicidal functions of peritoneal leukocytes in vivo
    • Zamuner S., Gutiérrez J.M., Muscará M.N., Teixeira S.A., and Teixeira C.F.P. Bothrops asper and Bothrops jararaca snake venoms trigger microbicidal functions of peritoneal leukocytes in vivo. Toxicon 39 (2001) 1505-1513
    • (2001) Toxicon , vol.39 , pp. 1505-1513
    • Zamuner, S.1    Gutiérrez, J.M.2    Muscará, M.N.3    Teixeira, S.A.4    Teixeira, C.F.P.5
  • 69
    • 0026499960 scopus 로고
    • Endothelial cell interactions with granulocytes: tethering and signaling molecules
    • Zimmerman G.A., Prescott S.M., and Mcintyre T.M. Endothelial cell interactions with granulocytes: tethering and signaling molecules. Immunol. Today 13 (1992) 93-100
    • (1992) Immunol. Today , vol.13 , pp. 93-100
    • Zimmerman, G.A.1    Prescott, S.M.2    Mcintyre, T.M.3


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