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Volumn 167, Issue 2-4, 2010, Pages 279-287

Biochemical characterization of a Kunitz type inhibitor similar to dendrotoxins produced by Rhipicephalus (Boophilus) microplus (Acari: Ixodidae) hemocytes

Author keywords

Apoptosis; Chymotrypsin inhibitor; Cytotoxicity; Dendrotoxins; Ectoparasite; Hematophagous; Hemocytes; Kunitz BPTI domain

Indexed keywords

BOOPHILUS MICROPLUS CHYMOTRYPSIN INHIBITOR; CHYMOTRYPSIN INHIBITOR; DENDROTOXIN; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 74449089420     PISSN: 03044017     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vetpar.2009.09.030     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 0035863762 scopus 로고    scopus 로고
    • The estimation of statistical parameters for local alignment score distributions
    • Altschul S.F., Bundschuh R., Olsen R., and Hwa T. The estimation of statistical parameters for local alignment score distributions. Nucleic Acids Res. 29 (2001) 351-361
    • (2001) Nucleic Acids Res. , vol.29 , pp. 351-361
    • Altschul, S.F.1    Bundschuh, R.2    Olsen, R.3    Hwa, T.4
  • 2
    • 52549091895 scopus 로고    scopus 로고
    • Serine proteinase inhibitors from eggs and larvae of tick Boophilus microplus: purification and biochemical characterization
    • Andreotti R., Malavazi-Piza K.C., Sasaki S.D., Torquato R.J., Gomes A., and Tanaka A.S. Serine proteinase inhibitors from eggs and larvae of tick Boophilus microplus: purification and biochemical characterization. J. Protein Chem. 20 (2001) 337-343
    • (2001) J. Protein Chem. , vol.20 , pp. 337-343
    • Andreotti, R.1    Malavazi-Piza, K.C.2    Sasaki, S.D.3    Torquato, R.J.4    Gomes, A.5    Tanaka, A.S.6
  • 4
    • 38549161105 scopus 로고    scopus 로고
    • Programmed cell death
    • pp. 1-13
    • Conradt B., and Xue D. Programmed cell death. WormBook vol. 6 (2005) pp. 1-13
    • (2005) WormBook , vol.6
    • Conradt, B.1    Xue, D.2
  • 5
    • 0030692830 scopus 로고    scopus 로고
    • Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda)
    • Destoumieux D., Bulet P., Loew D., Van Dorsselaer A., Rodriguez J., and Bachère E. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda). J. Biol. Chem. 272 (1997) 28398-28406
    • (1997) J. Biol. Chem. , vol.272 , pp. 28398-28406
    • Destoumieux, D.1    Bulet, P.2    Loew, D.3    Van Dorsselaer, A.4    Rodriguez, J.5    Bachère, E.6
  • 6
    • 0024985345 scopus 로고
    • Peptide toxins and potassium channels
    • Dreyer F. Peptide toxins and potassium channels. Rev. Physiol. Biochem. Pharmacol. 115 (1990) 93-136
    • (1990) Rev. Physiol. Biochem. Pharmacol. , vol.115 , pp. 93-136
    • Dreyer, F.1
  • 7
    • 0024370356 scopus 로고
    • The long and the short of snake toxins
    • Dufton M.J., and Harvey A.L. The long and the short of snake toxins. Trends Pharmacol. Sci. 10 (1989) 258-259
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 258-259
    • Dufton, M.J.1    Harvey, A.L.2
  • 8
    • 33645414090 scopus 로고    scopus 로고
    • Ixodidin, a novel antimicrobial peptide from the hemocytes of the cattle tick Boophilus microplus with inhibitory activity against serine proteinases
    • Fogaça A.C., Almeida I.C., Eberlin M.N., Tanaka A.S., Bulet P., and Daffre S. Ixodidin, a novel antimicrobial peptide from the hemocytes of the cattle tick Boophilus microplus with inhibitory activity against serine proteinases. Peptides 27 (2006) 667-674
    • (2006) Peptides , vol.27 , pp. 667-674
    • Fogaça, A.C.1    Almeida, I.C.2    Eberlin, M.N.3    Tanaka, A.S.4    Bulet, P.5    Daffre, S.6
  • 9
    • 2442483514 scopus 로고    scopus 로고
    • Penthalaris, a novel recombinant five-Kunitz tissue factor pathway inhibitor (TFPI) from the salivary gland of the tick vector of Lyme disease, Ixodes scapularis
    • Francischetti I.M., Mather T.N., and Ribeiro J.M. Penthalaris, a novel recombinant five-Kunitz tissue factor pathway inhibitor (TFPI) from the salivary gland of the tick vector of Lyme disease, Ixodes scapularis. Thromb. Haemost. 91 (2004) 886-898
    • (2004) Thromb. Haemost. , vol.91 , pp. 886-898
    • Francischetti, I.M.1    Mather, T.N.2    Ribeiro, J.M.3
  • 10
    • 0037093065 scopus 로고    scopus 로고
    • Ixolaris, a novel recombinant tissue factor pathway inhibitor (TFPI) from the salivary gland of the tick, Ixodes scapularis: identification of factor X and factor Xa as scaffolds for the inhibition of factor VIIa/tissue factor complex
    • Francischetti I.M., Valenzuela J.G., Andersen J.F., Mather T.N., and Ribeiro J.M. Ixolaris, a novel recombinant tissue factor pathway inhibitor (TFPI) from the salivary gland of the tick, Ixodes scapularis: identification of factor X and factor Xa as scaffolds for the inhibition of factor VIIa/tissue factor complex. Blood 99 (2002) 3602-3612
    • (2002) Blood , vol.99 , pp. 3602-3612
    • Francischetti, I.M.1    Valenzuela, J.G.2    Andersen, J.F.3    Mather, T.N.4    Ribeiro, J.M.5
  • 12
    • 0022332269 scopus 로고
    • Dendrotoxins: snake toxins that block potassium channels and facilitate neurotransmitter release
    • Harvey A.L., and Anderson A.J. Dendrotoxins: snake toxins that block potassium channels and facilitate neurotransmitter release. Pharmacol. Ther. 31 (1985) 33-55
    • (1985) Pharmacol. Ther. , vol.31 , pp. 33-55
    • Harvey, A.L.1    Anderson, A.J.2
  • 13
    • 0036417225 scopus 로고    scopus 로고
    • Beta-bungarotoxin is a potent inducer of apoptosis in cultured rat neurons by receptor-mediated internalization
    • Herkert M., Shakhman O., Schweins E., and Becker C.M. Beta-bungarotoxin is a potent inducer of apoptosis in cultured rat neurons by receptor-mediated internalization. Eur. J. Neurosci. 14 (2001) 821-828
    • (2001) Eur. J. Neurosci. , vol.14 , pp. 821-828
    • Herkert, M.1    Shakhman, O.2    Schweins, E.3    Becker, C.M.4
  • 14
    • 0017196279 scopus 로고
    • Snake venom proteinase inhibitors. III. Isolation of five polypeptide inhibitors from the venoms of Hemachatus haemachatus (Ringhal's cobra) and Naja nivea (Cape cobra) and the complete amino acid sequences of two of them
    • Hokama Y., Iwanaga S., Tatsuki T., and Suzuki T. Snake venom proteinase inhibitors. III. Isolation of five polypeptide inhibitors from the venoms of Hemachatus haemachatus (Ringhal's cobra) and Naja nivea (Cape cobra) and the complete amino acid sequences of two of them. J. Biochem. 79 (1976) 559-578
    • (1976) J. Biochem. , vol.79 , pp. 559-578
    • Hokama, Y.1    Iwanaga, S.2    Tatsuki, T.3    Suzuki, T.4
  • 15
    • 0034628896 scopus 로고    scopus 로고
    • Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel
    • Imredy J.P., and MacKinnon R. Energetic and structural interactions between delta-dendrotoxin and a voltage-gated potassium channel. J. Mol. Biol. 296 (2000) 1283-1294
    • (2000) J. Mol. Biol. , vol.296 , pp. 1283-1294
    • Imredy, J.P.1    MacKinnon, R.2
  • 16
    • 33745600373 scopus 로고    scopus 로고
    • Molecular cloning of disintegrin-like transcript BA-5A from a Bitis arietans venom gland cDNA library: a putative intermediate in the evolution of the long-chain disintegrin bitistatin
    • Juarez P., Wagstaff S.C., Oliver J., Sanz L., Harrison R.A., and Calvete J.J. Molecular cloning of disintegrin-like transcript BA-5A from a Bitis arietans venom gland cDNA library: a putative intermediate in the evolution of the long-chain disintegrin bitistatin. J. Mol. Evol. 63 (2006) 142-152
    • (2006) J. Mol. Evol. , vol.63 , pp. 142-152
    • Juarez, P.1    Wagstaff, S.C.2    Oliver, J.3    Sanz, L.4    Harrison, R.A.5    Calvete, J.J.6
  • 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
    • 0038175546 scopus 로고    scopus 로고
    • Morphological evidence that salivary gland degeneration in the American dog tick, Dermacentor variabilis (Say), involves programmed cell death
    • L'Amoreaux W.J., Junaid L., and Trevidi S. Morphological evidence that salivary gland degeneration in the American dog tick, Dermacentor variabilis (Say), involves programmed cell death. Tissue Cell. 35 (2003) 95-99
    • (2003) Tissue Cell. , vol.35 , pp. 95-99
    • L'Amoreaux, W.J.1    Junaid, L.2    Trevidi, S.3
  • 21
    • 0036015625 scopus 로고    scopus 로고
    • Amino acid sequence and structure modeling of savignin, a thrombin inhibitor from the tick, Ornithodoros savignyi
    • Mans B.J., Louw A.I., and Neitz A.W. Amino acid sequence and structure modeling of savignin, a thrombin inhibitor from the tick, Ornithodoros savignyi. Insect Biochem. Mol. Biol. 32 (2002) 821-828
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 821-828
    • Mans, B.J.1    Louw, A.I.2    Neitz, A.W.3
  • 22
    • 0026908424 scopus 로고
    • Protease inhibitor homologues of dendrotoxin do not bind to dendrotoxin acceptors on synaptosomal membranes or facilitate neuromuscular transmission
    • Marshall D.L., and Harvey A.L. Protease inhibitor homologues of dendrotoxin do not bind to dendrotoxin acceptors on synaptosomal membranes or facilitate neuromuscular transmission. Biol. Chem. Hoppe Seyler 373 (1992) 707-714
    • (1992) Biol. Chem. Hoppe Seyler , vol.373 , pp. 707-714
    • Marshall, D.L.1    Harvey, A.L.2
  • 23
    • 0014454095 scopus 로고
    • Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
    • Morrison J.F. Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors. Biochim. Biophys. Acta 185 (1969) 269-286
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 269-286
    • Morrison, J.F.1
  • 24
    • 0037088658 scopus 로고    scopus 로고
    • Bax and Bak promote apoptosis by modulating endoplasmic reticular and mitochondrial Ca2+ store
    • Nutt L.K., Pataer A., Pahler J., Fang B., Roth J., McConkey D.J., and Swisher S.G. Bax and Bak promote apoptosis by modulating endoplasmic reticular and mitochondrial Ca2+ store. J. Biol. Chem. 277 (2002) 9219-9225
    • (2002) J. Biol. Chem. , vol.277 , pp. 9219-9225
    • Nutt, L.K.1    Pataer, A.2    Pahler, J.3    Fang, B.4    Roth, J.5    McConkey, D.J.6    Swisher, S.G.7
  • 25
    • 0035867078 scopus 로고    scopus 로고
    • Ticks and tickborne bacterial diseases in humans: an emerging infectious threat
    • Parola P., and Raoult D. Ticks and tickborne bacterial diseases in humans: an emerging infectious threat. Clin. Infect. Dis. 32 (2001) 897-928
    • (2001) Clin. Infect. Dis. , vol.32 , pp. 897-928
    • Parola, P.1    Raoult, D.2
  • 26
    • 0020955346 scopus 로고
    • Serine proteinase inhibitors from Vipera ammodytes venom. Isolation and kinetic studies
    • Ritonja A., Turk V., and Gubensek F. Serine proteinase inhibitors from Vipera ammodytes venom. Isolation and kinetic studies. Eur. J. Biochem. 133 (1983) 427-432
    • (1983) Eur. J. Biochem. , vol.133 , pp. 427-432
    • Ritonja, A.1    Turk, V.2    Gubensek, F.3
  • 27
    • 8844240690 scopus 로고    scopus 로고
    • Boophilus microplus tick larvae, a rich source of Kunitz type serine proteinase inhibitors
    • Sasaki S.D., Azzolini S.S., Hirata I.Y., Andreotti R., and Tanaka A.S. Boophilus microplus tick larvae, a rich source of Kunitz type serine proteinase inhibitors. Biochimie 86 (2004) 643-649
    • (2004) Biochimie , vol.86 , pp. 643-649
    • Sasaki, S.D.1    Azzolini, S.S.2    Hirata, I.Y.3    Andreotti, R.4    Tanaka, A.S.5
  • 28
    • 45549109409 scopus 로고    scopus 로고
    • rBmTI-6, a Kunitz-BPTI domain protease inhibitor from the tick Boophilus microplus, its cloning, expression and biochemical characterization
    • Sasaki S.D., and Tanaka A.S. rBmTI-6, a Kunitz-BPTI domain protease inhibitor from the tick Boophilus microplus, its cloning, expression and biochemical characterization. Vet. Parasitol. 155 (2008) 133-141
    • (2008) Vet. Parasitol. , vol.155 , pp. 133-141
    • Sasaki, S.D.1    Tanaka, A.S.2
  • 29
    • 0025080866 scopus 로고
    • Purification and characterization of a chymotrypsin Kunitz inhibitor type of polypeptide from the venom of cobra (Naja naja naja)
    • Shafqat J., Zaidi Z.H., and Jörnvall H. Purification and characterization of a chymotrypsin Kunitz inhibitor type of polypeptide from the venom of cobra (Naja naja naja). FIBS Lett. 275 (1990) 6-8
    • (1990) FIBS Lett. , vol.275 , pp. 6-8
    • Shafqat, J.1    Zaidi, Z.H.2    Jörnvall, H.3
  • 30
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I., and Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27 (1967) 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 31
    • 33644901042 scopus 로고    scopus 로고
    • Cytotoxicity of materials used in perforation repair tested using the V79 fibroblast cell line and the granulocyte-macrophage progenitor cells
    • Souza N.J.A., Justo G.Z., Oliveira C.R., Haun M., and Bincoletto C. Cytotoxicity of materials used in perforation repair tested using the V79 fibroblast cell line and the granulocyte-macrophage progenitor cells. Int. Endod. J. 39 (2006) 40-47
    • (2006) Int. Endod. J. , vol.39 , pp. 40-47
    • Souza, N.J.A.1    Justo, G.Z.2    Oliveira, C.R.3    Haun, M.4    Bincoletto, C.5
  • 32
    • 0032735453 scopus 로고    scopus 로고
    • A double headed serine proteinase inhibitor-human plasma kallikrein and elastase inhibitor-from Boophilus microplus larvae
    • Tanaka A.S., Andreotti R., Gomes A., Torquato R.J., Sampaio M.U., and Sampaio C.A. A double headed serine proteinase inhibitor-human plasma kallikrein and elastase inhibitor-from Boophilus microplus larvae. Immunopharmacology 45 (1999) 171-177
    • (1999) Immunopharmacology , vol.45 , pp. 171-177
    • Tanaka, A.S.1    Andreotti, R.2    Gomes, A.3    Torquato, R.J.4    Sampaio, M.U.5    Sampaio, C.A.6
  • 33
    • 33845628659 scopus 로고    scopus 로고
    • Changes in gap junction organization and decreased coupling during induced apoptosis in lens epithelial and NIH-3T3 cells
    • Theiss C., Mazur A., Mellerm K., and Mannherz H.G. Changes in gap junction organization and decreased coupling during induced apoptosis in lens epithelial and NIH-3T3 cells. Exp. Cell Res. 313 (2007) 38-52
    • (2007) Exp. Cell Res. , vol.313 , pp. 38-52
    • Theiss, C.1    Mazur, A.2    Mellerm, K.3    Mannherz, H.G.4
  • 35
    • 0025375504 scopus 로고
    • Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa
    • Waxman L., Smith D.E., Arcuri K.E., and Vlasuk G.P. Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science 248 (1990) 593-596
    • (1990) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3    Vlasuk, G.P.4
  • 36
    • 33846840838 scopus 로고    scopus 로고
    • Vaccination against ectoparasites
    • Willadsen P. Vaccination against ectoparasites. Parasitology 133 (2006) S9-S25
    • (2006) Parasitology , vol.133
    • Willadsen, P.1
  • 37
    • 15944416757 scopus 로고    scopus 로고
    • Mechanisms of steroid-triggered programmed cell death in Drosophila
    • Yin V.P., and Thummel C.S. Mechanisms of steroid-triggered programmed cell death in Drosophila. Semin. Cell Dev. Biol. 16 (2005) 237-243
    • (2005) Semin. Cell Dev. Biol. , vol.16 , pp. 237-243
    • Yin, V.P.1    Thummel, C.S.2
  • 38
    • 1342279424 scopus 로고    scopus 로고
    • Purification, characterization and primary structure of a chymotrypsin inhibitor from Naja atra venom
    • Zhou X.Z., Yan J., Lu Q., Li D., Zhu S., Wang W., and Xiong Y. Purification, characterization and primary structure of a chymotrypsin inhibitor from Naja atra venom. Comp. Biochem. Physiol. 137 (2004) 219-224
    • (2004) Comp. Biochem. Physiol. , vol.137 , pp. 219-224
    • Zhou, X.Z.1    Yan, J.2    Lu, Q.3    Li, D.4    Zhu, S.5    Wang, W.6    Xiong, Y.7


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