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Volumn 37, Issue 4, 1999, Pages 587-607

Oligosaccharide residues of Loxosceles intermedia (brown spider) venom proteins: Dependence on glycosylation for dermonecrotic activity

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSIDASE; MANNOSE; OLIGOSACCHARIDE; PROTEINASE K; SPIDER VENOM;

EID: 0033046829     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0041-0101(98)00198-6     Document Type: Article
Times cited : (27)

References (42)
  • 1
    • 0026348765 scopus 로고
    • A common precursor for a putative haemorrhagic protein and rhodostomin, a platelet aggregation inhibitor of the venom of Calloselasma rhoadostoma: Molecular cloning and sequence analysis
    • Au L.C., Huang Y.B., Huang T.F., Teh G.W., Lin H.H., Choo K.B. A common precursor for a putative haemorrhagic protein and rhodostomin, a platelet aggregation inhibitor of the venom of Calloselasma rhoadostoma: molecular cloning and sequence analysis. Biochem. Biophys. Res. Commun. 181:1991;585-593.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 585-593
    • Au, L.C.1    Huang, Y.B.2    Huang, T.F.3    Teh, G.W.4    Lin, H.H.5    Choo, K.B.6
  • 2
  • 3
    • 0026611689 scopus 로고
    • Dermonecrotic and lethal components of Loxosceles gaucho spider venom
    • Barbaro K.C., Cardoso J.L.C., Eickstedt V.R.D., Mota I. Dermonecrotic and lethal components of Loxosceles gaucho spider venom. Toxicon. 30:1992;331-338.
    • (1992) Toxicon , vol.30 , pp. 331-338
    • Barbaro, K.C.1    Cardoso, J.L.C.2    Eickstedt, V.R.D.3    Mota, I.4
  • 5
    • 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
  • 6
    • 0026583798 scopus 로고
    • Folding of intestinal brush border enzymes: Evidence that high-mannose glycosylation is an essential early event
    • Danielsen E.M. Folding of intestinal brush border enzymes: evidence that high-mannose glycosylation is an essential early event. Biochemistry. 31:1992;2266-2272.
    • (1992) Biochemistry , vol.31 , pp. 2266-2272
    • Danielsen, E.M.1
  • 7
    • 0017290721 scopus 로고
    • Electrophoretic behaviour of acidic mucopolysaccharides in dyamine buffers
    • Dietrich C.P., Dietrich S.M.C. Electrophoretic behaviour of acidic mucopolysaccharides in dyamine buffers. Anal. Biochem. 70:1976;645-647.
    • (1976) Anal. Biochem. , vol.70 , pp. 645-647
    • Dietrich, C.P.1    Dietrich, S.M.C.2
  • 9
    • 0017375736 scopus 로고
    • Binding of soluble form of fibroblast surface protein, fibronectin, to collagen
    • Engvall E., Ruoslahti E. Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int. J. Cancer. 20:1977;1-5.
    • (1977) Int. J. Cancer , vol.20 , pp. 1-5
    • Engvall, E.1    Ruoslahti, E.2
  • 10
    • 0026317511 scopus 로고
    • Glycosidase inhibitors: Inhibitors of N-linked oligosaccharide processing
    • Elbein A.D. Glycosidase inhibitors: inhibitors of N-linked oligosaccharide processing. FASEB J. 5:1991;3055-3063.
    • (1991) FASEB J. , vol.5 , pp. 3055-3063
    • Elbein, A.D.1
  • 11
    • 0032125173 scopus 로고    scopus 로고
    • Detection and characterization of metalloproteinases with gelatinolytic, fibronectinolytic and fibrinogenolytic activities in brown spider (Loxosceles intermedia) venom
    • Feitosa, L., Gremski, W., Veiga, S.S., Elias, M.C.Q.B., Graner, E., Mangili, O.C., Brentani, R.R., 1998. Detection and characterization of metalloproteinases with gelatinolytic, fibronectinolytic and fibrinogenolytic activities in brown spider (Loxosceles intermedia) venom. Toxicon, 36, 1039 - 1056.
    • (1998) Toxicon , vol.36 , pp. 1039-1056
    • Feitosa, L.1    Gremski, W.2    Veiga, S.S.3    Elias, M.C.Q.B.4    Graner, E.5    Mangili, O.C.6    Brentani, R.R.7
  • 12
    • 0029030882 scopus 로고
    • Atrolysins: Metalloproteinases from Crotalus atrox venom
    • Fox J.W., Bjarnason J.B. Atrolysins: metalloproteinases from Crotalus atrox venom. Methods Enzymol. 248:1995;368-387.
    • (1995) Methods Enzymol. , vol.248 , pp. 368-387
    • Fox, J.W.1    Bjarnason, J.B.2
  • 13
  • 14
    • 0017076670 scopus 로고
    • Isolation and characterization of toxins from brown recluse spider venom (Loxosceles reclusa)
    • Geren C.R., Chan T.K., Howell D.E., Odell G.V. Isolation and characterization of toxins from brown recluse spider venom (Loxosceles reclusa). Arch. Biochem. Biophys. 174:1976;90-99.
    • (1976) Arch. Biochem. Biophys. , vol.174 , pp. 90-99
    • Geren, C.R.1    Chan, T.K.2    Howell, D.E.3    Odell, G.V.4
  • 15
    • 0028365639 scopus 로고
    • Factor-X-activating glycoprotein of Russell's viper venom: Polypeptide composition and characterization of the carbohydrate moieties
    • Gowda D.C., Jackson C.M., Hensley P., Davidson E.A. Factor-X-activating glycoprotein of Russell's viper venom: polypeptide composition and characterization of the carbohydrate moieties. J. Biol. Chem. 269:1994;10644-10650.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10644-10650
    • Gowda, D.C.1    Jackson, C.M.2    Hensley, P.3    Davidson, E.A.4
  • 16
    • 0029971864 scopus 로고    scopus 로고
    • Core sugar residues of the N-linked oligosaccharides of Russell's viper venom factor X-activator maintain functionally active polypeptide structure
    • Gowda D.C., Jackson C.M., Kurzban G.P., McPhie P., Davidson E.A. Core sugar residues of the N-linked oligosaccharides of Russell's viper venom factor X-activator maintain functionally active polypeptide structure. Biochemistry. 35:1996;5833-5837.
    • (1996) Biochemistry , vol.35 , pp. 5833-5837
    • Gowda, D.C.1    Jackson, C.M.2    Kurzban, G.P.3    McPhie, P.4    Davidson, E.A.5
  • 18
    • 0026507880 scopus 로고
    • Proteoglycans: Many forms and many functions
    • Hardingham T.E., Fosang A.J. Proteoglycans: many forms and many functions. FASEB J. 6:1992;861-870.
    • (1992) FASEB J. , vol.6 , pp. 861-870
    • Hardingham, T.E.1    Fosang, A.J.2
  • 19
    • 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., Fox J.W. cDNA sequences for four snake venom metalloproteinases: structure, classification, and their relationship to mammalian reproductive proteins. Arch. Biochem. Biophys. 308:1994;182-191.
    • (1994) Arch. Biochem. Biophys. , vol.308 , pp. 182-191
    • Hite, L.A.1    Jia, L.G.2    Bjarnason, J.B.3    Fox, J.W.4
  • 20
    • 14744273042 scopus 로고
    • Carbohydrate-based therapeutics
    • Hodgson J. Carbohydrate-based therapeutics. Biotechnology. 9:1991;609-613.
    • (1991) Biotechnology , vol.9 , pp. 609-613
    • Hodgson, J.1
  • 21
    • 0025945169 scopus 로고
    • Oligosaccharides at each glycosylation site make structure-dependent contribuitions to biological properties of human tissue plasminogen activator
    • Howard S.C., Wittwer A.J., Welphy J.K. Oligosaccharides at each glycosylation site make structure-dependent contribuitions to biological properties of human tissue plasminogen activator. Glycobiology. 1:1991;411-417.
    • (1991) Glycobiology , vol.1 , pp. 411-417
    • Howard, S.C.1    Wittwer, A.J.2    Welphy, J.K.3
  • 22
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interations
    • Kjellén L., Lindahl U. Proteoglycans: structures and interations. Ann. Rev. Biochem. 60:1991;443-475.
    • (1991) Ann. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellén, L.1    Lindahl, U.2
  • 23
    • 0021891884 scopus 로고
    • Assembly of asparagine-linked oligosaccharides
    • Kornfeld R., Kornfeld S. Assembly of asparagine-linked oligosaccharides. Ann. Rev. Biochem. 54:1985;631-664.
    • (1985) Ann. Rev. Biochem. , vol.54 , pp. 631-664
    • Kornfeld, R.1    Kornfeld, S.2
  • 24
    • 0019767846 scopus 로고
    • Platelet aggregation and sphingomyelinase D activity of a purified toxin from the venom of Loxosceles reclusa
    • Kurpiewski G., Forrester L.J., Barrett J.T., Campbell B.J. Platelet aggregation and sphingomyelinase D activity of a purified toxin from the venom of Loxosceles reclusa. Biochem. Biophys. Acta. 678:1981;467-476.
    • (1981) Biochem. Biophys. Acta , vol.678 , pp. 467-476
    • Kurpiewski, G.1    Forrester, L.J.2    Barrett, J.T.3    Campbell, B.J.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0028905147 scopus 로고
    • Carbohydrate structure analysis of batroxobin a thrombin-like serine protease from Bothrops moojeni venom
    • Lochnit G., Geyer R. Carbohydrate structure analysis of batroxobin a thrombin-like serine protease from Bothrops moojeni venom. Eur. J. Biochem. 228:1995;805-816.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 805-816
    • Lochnit, G.1    Geyer, R.2
  • 27
    • 0024344059 scopus 로고
    • Primary structure of haemorrhagic protein, HR2a, isolated from the venom of Trimeresurus flavoviridis
    • Miyata T., Takeya H., Ozeki Y., Arakawa M., Tokunaga F., Iwanaga S., Satoh T.O. Primary structure of haemorrhagic protein, HR2a, isolated from the venom of Trimeresurus flavoviridis. J. Biochem. 105:1989;847-853.
    • (1989) J. Biochem. , vol.105 , pp. 847-853
    • Miyata, T.1    Takeya, H.2    Ozeki, Y.3    Arakawa, M.4    Tokunaga, F.5    Iwanaga, S.6    Satoh, T.O.7
  • 28
    • 0028947353 scopus 로고
    • Primary structure of a coagulant enzyme, bilineobin, from Agkistrodon bilineatus venom
    • Nikai T., Ohara A., Komori Y., Fox J.W., Sugihara H. Primary structure of a coagulant enzyme, bilineobin, from Agkistrodon bilineatus venom. Arch. Biochem. Biophys. 318:1995;89-96.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 89-96
    • Nikai, T.1    Ohara, A.2    Komori, Y.3    Fox, J.W.4    Sugihara, H.5
  • 29
    • 0018608598 scopus 로고
    • Separation and characterization of venom components in Loxosceles reclusa, III. Hydrolic enzyme activity
    • Norment B.R., Jong Y.S., Heitz J.R. Separation and characterization of venom components in Loxosceles reclusa, III. Hydrolic enzyme activity. Toxicon. 17:1979;539-548.
    • (1979) Toxicon , vol.17 , pp. 539-548
    • Norment, B.R.1    Jong, Y.S.2    Heitz, J.R.3
  • 30
    • 0026495409 scopus 로고
    • Purification, cloning, and molecular characterization of a high molecular weight haemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom
    • Paine M.J.I., Desmond H.P., Theakston R.D.G., Crampton J.M. Purification, cloning, and molecular characterization of a high molecular weight haemorrhagic metalloprotease, jararhagin, from Bothrops jararaca venom. J. Biol. Chem. 267:1992;22869-22876.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22869-22876
    • Paine, M.J.I.1    Desmond, H.P.2    Theakston, R.D.G.3    Crampton, J.M.4
  • 32
    • 0345518379 scopus 로고
    • The effect of arg-gly-asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets
    • Plow E.F., Pierschbacher M.D., Ruoslahti E., Marguerie G.A. The effect of arg-gly-asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets. Proc. Natl. Acad. Sci. USA. 82:1985;8057-8061.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8057-8061
    • Plow, E.F.1    Pierschbacher, M.D.2    Ruoslahti, E.3    Marguerie, G.A.4
  • 33
    • 0025891131 scopus 로고
    • The complete amino acid sequence of the haemorrhagic factor LHFII, a metalloproteinase isolated from the venom of the bushmaster snake (Lachesis muta muta)
    • Sanchez E.F., Diniz C.R., Richardson M. The complete amino acid sequence of the haemorrhagic factor LHFII, a metalloproteinase isolated from the venom of the bushmaster snake (Lachesis muta muta). FEBS Lett. 282:1991;178-182.
    • (1991) FEBS Lett. , vol.282 , pp. 178-182
    • Sanchez, E.F.1    Diniz, C.R.2    Richardson, M.3
  • 34
    • 0028791068 scopus 로고
    • Incorporation of a 35-kilodalton purified protein from Loxosceles intermedia spider venom transforms human erythrocytes into activators of autologous complement alternative pathway
    • Tambourgi D.V., Magnoli F.C., Eickstedt V.R.D., Benedetti Z.C., Petricevich V.L., Silva W.D. Incorporation of a 35-kilodalton purified protein from Loxosceles intermedia spider venom transforms human erythrocytes into activators of autologous complement alternative pathway. J. Immunol. 155:1995;4459-4466.
    • (1995) J. Immunol. , vol.155 , pp. 4459-4466
    • Tambourgi, D.V.1    Magnoli, F.C.2    Eickstedt, V.R.D.3    Benedetti, Z.C.4    Petricevich, V.L.5    Silva, W.D.6
  • 35
    • 0024690967 scopus 로고
    • 2-proteinase, a non-haemorrhagic metalloproteinase, isolated from venom of the Habu snake, Trimeresurus flavoviridis
    • 2-proteinase, a non-haemorrhagic metalloproteinase, isolated from venom of the Habu snake, Trimeresurus flavoviridis. J. Biochem. 106:1989;151-157.
    • (1989) J. Biochem. , vol.106 , pp. 151-157
    • Takeya, H.1    Arakawa, M.2    Miyata, T.3    Iwanaga, S.4    Omori-Satoh, T.5
  • 36
    • 0024997837 scopus 로고
    • The complete amino acid sequence of the high molecular mass haemorhagic protein HR1B isolated from the venom of Trimeresurus flavoviridis
    • Takeya H., Oda K., Miyata T., Omori-Satoh T., Iwanaga S. The complete amino acid sequence of the high molecular mass haemorhagic 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
  • 37
    • 0025918707 scopus 로고
    • Structures and functional roles of the sugar chains of human erythropoietins
    • Takeuchi M., Kobata A. Structures and functional roles of the sugar chains of human erythropoietins. Glycobiology. 1:1991;337-346.
    • (1991) Glycobiology , vol.1 , pp. 337-346
    • Takeuchi, M.1    Kobata, A.2
  • 38
    • 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. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 39
    • 0028988148 scopus 로고
    • Glycosylation of β-1 integrins in B16-F10 mouse melanoma cells as determinant of differential binding and acquisition of biological activity
    • Veiga S.S., Chammas R., Cella N., Brentani R.R. Glycosylation of β-1 integrins in B16-F10 mouse melanoma cells as determinant of differential binding and acquisition of biological activity. Int. J. Cancer. 61:1995;420-424.
    • (1995) Int. J. Cancer , vol.61 , pp. 420-424
    • Veiga, S.S.1    Chammas, R.2    Cella, N.3    Brentani, R.R.4
  • 42
    • 0026326839 scopus 로고
    • Will complex carbohydrate ligands of vascular selectins be the next generation of non-steroidal anti-inflamatory drugs?
    • Winkelhake J.L. Will complex carbohydrate ligands of vascular selectins be the next generation of non-steroidal anti-inflamatory drugs? Glycoconjugate J. 8:1991;381-386.
    • (1991) Glycoconjugate J. , vol.8 , pp. 381-386
    • Winkelhake, J.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.