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Volumn 279, Issue 21, 2012, Pages 4025-4038

Subtype specificity interaction of bactridines with mammalian, insect and bacterial sodium channels under voltage clamp conditions

Author keywords

bactridines; NaV channels; scorpion; sequence; Tityus discrepans

Indexed keywords

BACTRIDINE 1; BACTRIDINE 2; BACTRIDINE 3; BACTRIDINE 4; BACTRIDINE 5; BACTRIDINE 6; SCORPION VENOM; SODIUM CHANNEL NAV1.2; SODIUM CHANNEL NAV1.3; SODIUM CHANNEL NAV1.4; SODIUM CHANNEL NAV1.5; SODIUM CHANNEL NAV1.6; SODIUM CHANNEL NAV1.7; SODIUM CHANNEL NAV1.8; UNCLASSIFIED DRUG;

EID: 84867576405     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08808.x     Document Type: Article
Times cited : (18)

References (62)
  • 1
    • 68949146850 scopus 로고    scopus 로고
    • Antibacterial activity of six novel peptides from Tityus discrepans scorpion venom. A fluorescent probe study of microbial membrane Na+ permeability changes
    • Díaz P, D'Suze G, Salazar V, Sevcik C, Shannon JD, Sherman NE, &, Fox JW, (2009) Antibacterial activity of six novel peptides from Tityus discrepans scorpion venom. A fluorescent probe study of microbial membrane Na+ permeability changes. Toxicon 54, 802-817.
    • (2009) Toxicon , vol.54 , pp. 802-817
    • Díaz, P.1    D'Suze, G.2    Salazar, V.3    Sevcik, C.4    Shannon, J.D.5    Sherman, N.E.6    Fox, J.W.7
  • 3
    • 0028233375 scopus 로고
    • Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 Å resolution
    • Housset D, Habersetzer-Rochat C, Astier JP, &, Fontecilla-Camps JC, (1994) Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 Å resolution. J Mol Biol 238, 88-103.
    • (1994) J Mol Biol , vol.238 , pp. 88-103
    • Housset, D.1    Habersetzer-Rochat, C.2    Astier, J.P.3    Fontecilla-Camps, J.C.4
  • 4
    • 0028927315 scopus 로고
    • NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels
    • Lippens G, Najib J, Wodak SJ, &, Tartar A, (1995) NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels. Biochemistry 34, 13-21.
    • (1995) Biochemistry , vol.34 , pp. 13-21
    • Lippens, G.1    Najib, J.2    Wodak, S.J.3    Tartar, A.4
  • 6
    • 29244468286 scopus 로고    scopus 로고
    • Structure-activity relationship of an α-toxin Bs-Tx28 from scorpion (Buthus sindicus) venom suggests a new α-toxin subfamily
    • Ali SA, Wang B, Alam M, Beck A, Stoeva S, Voelter W, Abbasi A, &, Duszenko M, (2006) Structure-activity relationship of an α-toxin Bs-Tx28 from scorpion (Buthus sindicus) venom suggests a new α-toxin subfamily. Arch Biochem Biophys 445, 81-94.
    • (2006) Arch Biochem Biophys , vol.445 , pp. 81-94
    • Ali, S.A.1    Wang, B.2    Alam, M.3    Beck, A.4    Stoeva, S.5    Voelter, W.6    Abbasi, A.7    Duszenko, M.8
  • 7
    • 33846424926 scopus 로고    scopus 로고
    • Novel paradigms on scorpion toxins that affects the activating mechanism of sodium channels
    • Rodríguez de la Vega RC, &, Possani LD, (2007) Novel paradigms on scorpion toxins that affects the activating mechanism of sodium channels. Toxicon 49, 171-180.
    • (2007) Toxicon , vol.49 , pp. 171-180
    • Rodríguez De La Vega, R.C.1    Possani, L.D.2
  • 8
    • 0003017338 scopus 로고
    • Scorpion neurotoxins: Effects and mechanisms
    • In (Chang L.W. & Dyer R.S. eds), Marcel Dekker, New York.
    • Martin-Eauclaire MF, &, Couraud F, (1995) Scorpion neurotoxins: effects and mechanisms. In Handbook of Neurotoxicology (, Chang LW, &, Dyer RS, eds), pp. 683-716. Marcel Dekker, New York.
    • (1995) Handbook of Neurotoxicology , pp. 683-716
    • Martin-Eauclaire, M.F.1    Couraud, F.2
  • 11
    • 15244363044 scopus 로고    scopus 로고
    • Molecular mechanism of scorpion neurotoxins acting on sodium channels
    • Zuo XP, &, Ji YH, (2004) Molecular mechanism of scorpion neurotoxins acting on sodium channels. Mol Neurobiol 30, 265-278.
    • (2004) Mol Neurobiol , vol.30 , pp. 265-278
    • Zuo, X.P.1    Ji, Y.H.2
  • 12
    • 1542391730 scopus 로고    scopus 로고
    • New insight on scorpion divergence inferred from comparative analysis of toxin structure, pharmacology and distribution
    • Froy O, &, Gurevitz M, (2003) New insight on scorpion divergence inferred from comparative analysis of toxin structure, pharmacology and distribution. Toxicon 42, 549-555.
    • (2003) Toxicon , vol.42 , pp. 549-555
    • Froy, O.1    Gurevitz, M.2
  • 13
    • 0842312524 scopus 로고    scopus 로고
    • Adaptive evolution of scorpion sodium channel toxins
    • Zhu S, Bosmans F, &, Tytgat J, (2004) Adaptive evolution of scorpion sodium channel toxins. J Mol Evol 58, 145-153.
    • (2004) J Mol Evol , vol.58 , pp. 145-153
    • Zhu, S.1    Bosmans, F.2    Tytgat, J.3
  • 14
    • 33846474874 scopus 로고    scopus 로고
    • Voltage-gated sodium channel modulation by scorpion α-toxins
    • Bosmans F, &, Tytgat J, (2007) Voltage-gated sodium channel modulation by scorpion α-toxins. Toxicon 49, 142-158.
    • (2007) Toxicon , vol.49 , pp. 142-158
    • Bosmans, F.1    Tytgat, J.2
  • 15
    • 0029026638 scopus 로고
    • Structure and function of voltage-gated ion channels
    • Catterall WA, (1995) Structure and function of voltage-gated ion channels. Annu Rev Biochem 64, 493-531.
    • (1995) Annu Rev Biochem , vol.64 , pp. 493-531
    • Catterall, W.A.1
  • 16
    • 0001456758 scopus 로고    scopus 로고
    • Sodium channels as targets for neurotoxins: Mode of action and interaction of neurotoxins with receptor sites on sodium channels
    • In (Gutman Y. & Lazarowici P. eds), Harwood Academic Publishers, Amsterdam, Netherlands.
    • Gordon D, (1997) Sodium channels as targets for neurotoxins: mode of action and interaction of neurotoxins with receptor sites on sodium channels. In Toxins and Signal Transduction (, Gutman Y, &, Lazarowici P, eds), pp. 119-149. Harwood Academic Publishers, Amsterdam, Netherlands.
    • (1997) Toxins and Signal Transduction , pp. 119-149
    • Gordon, D.1
  • 18
    • 0032191111 scopus 로고    scopus 로고
    • Voltage sensor-trapping: Enhanced activation of sodium channels by β-scorpion toxin bound to the S3-S4 loop in domain II
    • Cèstele S, Qu Y, Rogers JC, Rochat H, Scheuer T, &, Catterall WA, (1998) Voltage sensor-trapping: enhanced activation of sodium channels by β-scorpion toxin bound to the S3-S4 loop in domain II. Neuron 21, 919-931.
    • (1998) Neuron , vol.21 , pp. 919-931
    • Cèstele, S.1    Qu, Y.2    Rogers, J.C.3    Rochat, H.4    Scheuer, T.5    Catterall, W.A.6
  • 20
    • 33745228127 scopus 로고    scopus 로고
    • Subtype specificity of scorpion β-toxin tz1 interaction with voltage-gated sodium channels is determined by the pore loop of domain 3
    • Leipold E, Hansel A, Borges A, &, Heinemann SH, (2006) Subtype specificity of scorpion β-toxin tz1 interaction with voltage-gated sodium channels is determined by the pore loop of domain 3. Mol Pharmacol 70, 340-347.
    • (2006) Mol Pharmacol , vol.70 , pp. 340-347
    • Leipold, E.1    Hansel, A.2    Borges, A.3    Heinemann, S.H.4
  • 22
    • 0033661482 scopus 로고    scopus 로고
    • Structure, function and pharmacology of voltage-gated sodium channels
    • Denac H, Mevissen M, &, Scholtysik G, (2000) Structure, function and pharmacology of voltage-gated sodium channels. Naun-Schmied Arch Pharmacol 362, 453-479.
    • (2000) Naun-Schmied Arch Pharmacol , vol.362 , pp. 453-479
    • Denac, H.1    Mevissen, M.2    Scholtysik, G.3
  • 23
    • 0035050571 scopus 로고    scopus 로고
    • Resurgence of sodium channel research
    • Goldin AL, (2001) Resurgence of sodium channel research. Annu Rev Physiol 63, 871-894.
    • (2001) Annu Rev Physiol , vol.63 , pp. 871-894
    • Goldin, A.L.1
  • 24
    • 0034843175 scopus 로고    scopus 로고
    • Neutralization of gating charges in domain II of the sodium channel a subunit enhances voltage-sensor trapping by a β-scorpion toxin
    • Cestele S, Scheuer T, Mantegazza M, Rochat H, &, Catterall WA, (2001) Neutralization of gating charges in domain II of the sodium channel a subunit enhances voltage-sensor trapping by a β-scorpion toxin. J Gen Physiol 118, 291-301.
    • (2001) J Gen Physiol , vol.118 , pp. 291-301
    • Cestele, S.1    Scheuer, T.2    Mantegazza, M.3    Rochat, H.4    Catterall, W.A.5
  • 25
    • 84861220344 scopus 로고    scopus 로고
    • V channel voltage sensor gives rise to excitatory and depressant modes
    • V channel voltage sensor gives rise to excitatory and depressant modes. J Gen Physiol 139, 305-319.
    • (2012) J Gen Physiol , vol.139 , pp. 305-319
    • Leipold, E.1    Borges, A.2    Heinemann, S.H.3
  • 27
    • 0033735270 scopus 로고    scopus 로고
    • The binding of BmK IT2, a depressant insect-selective scorpion toxin on mammal and insect sodium channels
    • Li YJ, Tan ZY, &, Ji YH, (2000) The binding of BmK IT2, a depressant insect-selective scorpion toxin on mammal and insect sodium channels. Neurosci Res 38, 257-264.
    • (2000) Neurosci Res , vol.38 , pp. 257-264
    • Li, Y.J.1    Tan, Z.Y.2    Ji, Y.H.3
  • 28
    • 0033663936 scopus 로고    scopus 로고
    • Antihyperalgesia effect of BmK IT2, a depressant insect-selective scorpion toxin in rat by peripheral administration
    • Wang CY, Tan ZY, Chen B, Zhao ZQ, &, Ji YH, (2000) Antihyperalgesia effect of BmK IT2, a depressant insect-selective scorpion toxin in rat by peripheral administration. Brain Res Bull 53, 335-338.
    • (2000) Brain Res Bull , vol.53 , pp. 335-338
    • Wang, C.Y.1    Tan, Z.Y.2    Chen, B.3    Zhao, Z.Q.4    Ji, Y.H.5
  • 30
    • 0141646281 scopus 로고    scopus 로고
    • Suppressive effects of BmK IT2 on nociceptive behavior and c-Fos expression in spinal cord induced by formalin
    • Zhang XY, Bai ZT, Chai ZF, Zhang JW, Liu Y, &, Ji YH, (2003) Suppressive effects of BmK IT2 on nociceptive behavior and c-Fos expression in spinal cord induced by formalin. J Neurosci Res 74, 167-173.
    • (2003) J Neurosci Res , vol.74 , pp. 167-173
    • Zhang, X.Y.1    Bai, Z.T.2    Chai, Z.F.3    Zhang, J.W.4    Liu, Y.5    Ji, Y.H.6
  • 31
    • 34250019655 scopus 로고    scopus 로고
    • Suppression by intrathecal BmK IT2 on rat spontaneous pain behaviors and spinal c-Fos expression induced by formalin
    • Bai ZT, Liu T, Pang XY, Chai ZF, &, Ji YH, (2007) Suppression by intrathecal BmK IT2 on rat spontaneous pain behaviors and spinal c-Fos expression induced by formalin. Brain Res Bull 73, 248-253.
    • (2007) Brain Res Bull , vol.73 , pp. 248-253
    • Bai, Z.T.1    Liu, T.2    Pang, X.Y.3    Chai, Z.F.4    Ji, Y.H.5
  • 33
    • 0032935518 scopus 로고    scopus 로고
    • Inactivated state dependence of sodium channel modulation by beta-scorpion toxin
    • Tsushima RG, Borges A, &, Backx PH, (1999) Inactivated state dependence of sodium channel modulation by beta-scorpion toxin. Pflüg Arch 437, 661-668.
    • (1999) Pflüg Arch , vol.437 , pp. 661-668
    • Tsushima, R.G.1    Borges, A.2    Backx, P.H.3
  • 34
    • 67649450453 scopus 로고    scopus 로고
    • Molecular cloning and nucleotide sequence analysis of genes from a cDNA library of the scorpion Tityus discrepans
    • D'Suze G, Schwartz EF, García-Gomez BI, Sevcik C, &, Possani LD, (2009) Molecular cloning and nucleotide sequence analysis of genes from a cDNA library of the scorpion Tityus discrepans. Biochimie 91, 1010-1019.
    • (2009) Biochimie , vol.91 , pp. 1010-1019
    • D'Suze, G.1    Schwartz, E.F.2    García-Gomez, B.I.3    Sevcik, C.4    Possani, L.D.5
  • 35
    • 33644994074 scopus 로고    scopus 로고
    • Diversity of long-chain toxins in Tityus zulianus and Tityus discrepans venoms (Scorpiones, Buthidae): Molecular, immunological, and mass spectral analyses
    • Borges A, García CC, Lugo E, Alfonzo MJ, Jowers MJ, &, op den Camp HJ, (2006) Diversity of long-chain toxins in Tityus zulianus and Tityus discrepans venoms (Scorpiones, Buthidae): molecular, immunological, and mass spectral analyses. Comp Biochem Physiol C Toxicol Pharmacol 142, 240-252.
    • (2006) Comp Biochem Physiol C Toxicol Pharmacol , vol.142 , pp. 240-252
    • Borges, A.1    García, C.C.2    Lugo, E.3    Alfonzo, M.J.4    Jowers, M.J.5    Op Den Camp, H.J.6
  • 36
    • 0032900897 scopus 로고    scopus 로고
    • Dynamic diversification from a putative common ancestor of scorpion toxins affecting sodium, potassium and chloride channels
    • Froy O, Sagiv T, Poreh M, Urbach D, Zilberberg N, &, Gurevitz M, (1999) Dynamic diversification from a putative common ancestor of scorpion toxins affecting sodium, potassium and chloride channels. J Mol Evol 48, 187-196.
    • (1999) J Mol Evol , vol.48 , pp. 187-196
    • Froy, O.1    Sagiv, T.2    Poreh, M.3    Urbach, D.4    Zilberberg, N.5    Gurevitz, M.6
  • 38
    • 14244265321 scopus 로고    scopus 로고
    • Common features in the functional surface of scorpion β-toxins and elements that confer specificity for insect and mammalian voltage-gated sodium channels
    • Cohen L, Karbat I, Gilles N, Ilan N, Benveniste N, Gordon D, &, Gurevitz M, (2005) Common features in the functional surface of scorpion β-toxins and elements that confer specificity for insect and mammalian voltage-gated sodium channels. J Biol Chem 280, 5045-5053.
    • (2005) J Biol Chem , vol.280 , pp. 5045-5053
    • Cohen, L.1    Karbat, I.2    Gilles, N.3    Ilan, N.4    Benveniste, N.5    Gordon, D.6    Gurevitz, M.7
  • 40
    • 0020004282 scopus 로고
    • Temperature dependence of tetrodotoxin effect in squid giant axons
    • Sevcik C, (1982) Temperature dependence of tetrodotoxin effect in squid giant axons. J Physiol 325, 187-194.
    • (1982) J Physiol , vol.325 , pp. 187-194
    • Sevcik, C.1
  • 41
    • 0026080931 scopus 로고
    • An anti-insect toxin purified from the scorpion Androctonus australis Hector also acts on the α- And β-sites of the mammalian sodium channel: Sequence and circular dichroism study
    • Loret EP, Martin-Eauclaire MF, Mansuelle P, Sampieri F, Granier C, &, Rochat H, (1991) An anti-insect toxin purified from the scorpion Androctonus australis Hector also acts on the α- and β-sites of the mammalian sodium channel: sequence and circular dichroism study. Biochemistry 30, 633-640.
    • (1991) Biochemistry , vol.30 , pp. 633-640
    • Loret, E.P.1    Martin-Eauclaire, M.F.2    Mansuelle, P.3    Sampieri, F.4    Granier, C.5    Rochat, H.6
  • 43
    • 13944258544 scopus 로고    scopus 로고
    • The depressant scorpion neurotoxin LqqIT2 selectively modulates the insect voltage-gated sodium channel
    • Bosmans F, Martin-Eauclaire MF, &, Tytgat J, (2005) The depressant scorpion neurotoxin LqqIT2 selectively modulates the insect voltage-gated sodium channel. Toxicon 45, 501-507.
    • (2005) Toxicon , vol.45 , pp. 501-507
    • Bosmans, F.1    Martin-Eauclaire, M.F.2    Tytgat, J.3
  • 44
    • 84859606337 scopus 로고    scopus 로고
    • Investigation of the relationship between the structure and function of Ts2, a neurotoxin from Tityus serrulatus venom
    • Cologna CT, Peigneur S, Rustiguel JK, Nonato MC, Tytgat J, &, Arantes EC, (2012) Investigation of the relationship between the structure and function of Ts2, a neurotoxin from Tityus serrulatus venom. FEBS J 279, 1495-1504.
    • (2012) FEBS J , vol.279 , pp. 1495-1504
    • Cologna, C.T.1    Peigneur, S.2    Rustiguel, J.K.3    Nonato, M.C.4    Tytgat, J.5    Arantes, E.C.6
  • 49
    • 55949108402 scopus 로고    scopus 로고
    • Ion channels in microbes
    • Martinac B, Saimi Y, &, Kung C, (2008) Ion channels in microbes. Physiol Rev 88, 1449-1490.
    • (2008) Physiol Rev , vol.88 , pp. 1449-1490
    • Martinac, B.1    Saimi, Y.2    Kung, C.3
  • 50
    • 0028948580 scopus 로고
    • Presence of curarizing polypeptides and a pancreatitisinducing fraction without muscarinic effects in the venom of the Venezuelan scorpion Tityus discrepans (Karsch)
    • D'Suze G, Sevcik C, &, Ramos M, (1995) Presence of curarizing polypeptides and a pancreatitisinducing fraction without muscarinic effects in the venom of the Venezuelan scorpion Tityus discrepans (Karsch). Toxicon 33, 333-345.
    • (1995) Toxicon , vol.33 , pp. 333-345
    • D'Suze, G.1    Sevcik, C.2    Ramos, M.3
  • 54
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex N, &, Peitsch MC, (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 55
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, &, Peitsch MC, (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31, 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 56
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • Arnold K, Bordoli L, Kopp J, &, Schwede T, (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201.
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 57
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia C, &, Lesk AM, (1986) The relation between the divergence of sequence and structure in proteins. EMBO J 5, 823-836.
    • (1986) EMBO J , vol.5 , pp. 823-836
    • Chothia, C.1    Lesk, A.M.2
  • 58
    • 0026030641 scopus 로고
    • Database of homology-derived protein structures and the structural meaning of sequence alignment
    • Sander C, &, Schneider R, (1991) Database of homology-derived protein structures and the structural meaning of sequence alignment. Proteins 9, 56-68.
    • (1991) Proteins , vol.9 , pp. 56-68
    • Sander, C.1    Schneider, R.2
  • 59
    • 0032962457 scopus 로고    scopus 로고
    • Twilight zone of protein sequence alignments
    • Rost B, (1999) Twilight zone of protein sequence alignments. Protein Eng 12, 85-94.
    • (1999) Protein Eng , vol.12 , pp. 85-94
    • Rost, B.1
  • 60
    • 33747866099 scopus 로고    scopus 로고
    • DISULFIND: A disulfide bonding state and cysteine connectivity prediction server
    • Ceroni A, Passerini A, Vullo A, &, Frasconi P, (2006) DISULFIND: a disulfide bonding state and cysteine connectivity prediction server. Nucleic Acids Res 34, W177-W181.
    • (2006) Nucleic Acids Res , vol.34
    • Ceroni, A.1    Passerini, A.2    Vullo, A.3    Frasconi, P.4
  • 62
    • 0026485457 scopus 로고
    • 2+ channel determined by construction of multimeric cDNAs
    • 2+ channel determined by construction of multimeric cDNAs. Neuron 9, 861-871.
    • (1992) Neuron , vol.9 , pp. 861-871
    • Liman, E.R.1    Tytgat, J.2    Hess, P.3


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