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Volumn 645, Issue 1, 2010, Pages 213-221

Characterisation of neurotoxic polypeptides from Cyanea capillata medusae (Scyphozoa)

Author keywords

Jellyfish; Mass spectrometry; Toxin; Venom; Voltage gated sodium channel

Indexed keywords

CELL ASSAYS; CHARACTERISATION; CRUDE VENOMS; EXCITABLE CELLS; ION CHANNEL; IONISATION; MALDI TOF MS; MASS SPECTRA; MATRIX ASSISTED LASER DESORPTION; MEDUSAE; NEUROBLASTOMAS; NEUROTOXIC PEPTIDES; PURIFICATION PROCESS; RECEPTOR SITES; REVERSED-PHASE CHROMATOGRAPHY; SODIUM CHANNEL; TIME OF FLIGHT MASS SPECTROMETRY; VOLTAGE GATED ION CHANNELS;

EID: 77952010465     PISSN: 00188158     EISSN: 15735117     Source Type: Journal    
DOI: 10.1007/s10750-010-0215-x     Document Type: Article
Times cited : (15)

References (30)
  • 1
    • 33646772912 scopus 로고    scopus 로고
    • Marine toxins targeting ion channels
    • Arias, H. R., 2006. Marine toxins targeting ion channels. Marine Drugs 4: 37-69.
    • (2006) Marine Drugs , vol.4 , pp. 37-69
    • Arias, H.R.1
  • 2
    • 0346657903 scopus 로고    scopus 로고
    • Voltage-gated sodium channel toxins - poisons, probes, and future promise
    • Blumenthal, K. M. & A. L. Seibert, 2003. Voltage-gated sodium channel toxins - poisons, probes, and future promise. Cell Biochemistry and Biophysics 38: 215-237.
    • (2003) Cell Biochemistry and Biophysics , vol.38 , pp. 215-237
    • Blumenthal, K.M.1    Seibert, A.L.2
  • 3
    • 0029026638 scopus 로고
    • Structure and function of voltage-gated ion channels
    • Catterall, W. A., 1995. Structure and function of voltage-gated ion channels. Annual Review of Biochemistry 64: 493-531.
    • (1995) Annual Review of Biochemistry , vol.64 , pp. 493-531
    • Catterall, W.A.1
  • 4
    • 0033731909 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotoxin action on voltage-gated sodium channels
    • Cestèle, S. & W. A. Catterall, 2000. Molecular mechanisms of neurotoxin action on voltage-gated sodium channels. Biochimie 82: 883-892.
    • (2000) Biochimie , vol.82 , pp. 883-892
    • Cestèle, S.1    Catterall, W.A.2
  • 5
    • 0028970541 scopus 로고
    • A μ-conotoxin-insensitive Na + channel mutant: Possible localization of a binding site at the outer vestibule
    • Dudley, S. C., H. Todt, G. Lipkind & H. A. Fozzard, 1995. A μ-conotoxin-insensitive Na + channel mutant: possible localization of a binding site at the outer vestibule. Biophysical Journal 69: 1657-1665.
    • (1995) Biophysical Journal , vol.69 , pp. 1657-1665
    • Dudley, S.C.1    Todt, H.2    Lipkind, G.3    Fozzard, H.A.4
  • 6
    • 0030058733 scopus 로고    scopus 로고
    • Interactions between a pore-blocking peptide and the voltage sensor of the sodium channel: An electrostatic approach to channel geometry
    • French, R. J., E. Prusak-Sochaczewski, G. W. Zamponi, S. Becker, A. S. Kularatna & R. Horn, 1996. Interactions between a pore-blocking peptide and the voltage sensor of the sodium channel: an electrostatic approach to channel geometry. Neuron 16: 407-413.
    • (1996) Neuron , vol.16 , pp. 407-413
    • French, R.J.1    Prusak-Sochaczewski, E.2    Zamponi, G.W.3    Becker, S.4    Kularatna, A.S.5    Horn, R.6
  • 7
    • 0026549496 scopus 로고
    • A tissue-culture assay for direct detection of sodium-channel blocking toxins in bacterial culture supernates
    • Gallacher, S. & T. H. Birkbeck, 1992. A tissue-culture assay for direct detection of sodium-channel blocking toxins in bacterial culture supernates. FEMS Microbiology Letters 92: 101-108.
    • (1992) FEMS Microbiology Letters , vol.92 , pp. 101-108
    • Gallacher, S.1    Birkbeck, T.H.2
  • 8
    • 0031032755 scopus 로고    scopus 로고
    • Evidence for production of paralytic shellfish toxins by bacteria associated with Alexandrium spp. (Dinophyta) in culture
    • Gallacher, S., K. J. Flynn, J. M. Franco, E. E. Brueggemann & H. B. Hines, 1997. Evidence for production of paralytic shellfish toxins by bacteria associated with Alexandrium spp. (Dinophyta) in culture. Applied and Environmental Microbiology 63: 239-245.
    • (1997) Applied and Environmental Microbiology , vol.63 , pp. 239-245
    • Gallacher, S.1    Flynn, K.J.2    Franco, J.M.3    Brueggemann, E.E.4    Hines, H.B.5
  • 9
    • 34249814004 scopus 로고    scopus 로고
    • Comparative study on the cell toxicity and enzymatic activity of two northern scyphozoan species Cyanea capillata (L.) and Cyanea lamarckii (Péron & Léslieur)
    • Helmholz, H., C. Ruhnau, C. Schuett & A. Prange, 2007. Comparative study on the cell toxicity and enzymatic activity of two northern scyphozoan species Cyanea capillata (L.) and Cyanea lamarckii (Péron & Léslieur). Toxicon 50: 53-64.
    • (2007) Toxicon , vol.50 , pp. 53-64
    • Helmholz, H.1    Ruhnau, C.2    Schuett, C.3    Prange, A.4
  • 10
    • 33144485759 scopus 로고    scopus 로고
    • Peptide toxins in sea anemones: Structural and functional aspects
    • Honma, T. & K. Shiomi, 2006. Peptide toxins in sea anemones: structural and functional aspects. Marine Biotechnology 8: 1-10.
    • (2006) Marine Biotechnology , vol.8 , pp. 1-10
    • Honma, T.1    Shiomi, K.2
  • 11
    • 0036141825 scopus 로고    scopus 로고
    • Electrostatic and steric contributions to block of the skeletal muscle sodium channel by μ-conotoxin
    • Hui, K. Y., G. Lipkind, H. A. Fozzard & R. J. French, 2002. Electrostatic and steric contributions to block of the skeletal muscle sodium channel by μ-conotoxin. Journal of General Physiology 119: 45-54.
    • (2002) Journal of General Physiology , vol.119 , pp. 45-54
    • Hui, K.Y.1    Lipkind, G.2    Fozzard, H.A.3    French, R.J.4
  • 12
    • 0033865588 scopus 로고    scopus 로고
    • Conotoxins - new vistas for peptide therapeutics
    • Jones, R. M. & G. Bulaj, 2000. Conotoxins - new vistas for peptide therapeutics. Current Pharmaceutical Design 6: 1249-1285.
    • (2000) Current Pharmaceutical Design , vol.6 , pp. 1249-1285
    • Jones, R.M.1    Bulaj, G.2
  • 14
    • 0001208115 scopus 로고
    • Isolation, characterization, and comparison of hemolytic peptides in nematocyst venoms of 2 species of jellyfish (Chrysaoraquinquecirrha and Cyanea capillata)
    • Long, K. O. & J. W. Burnett, 1989. Isolation, characterization, and comparison of hemolytic peptides in nematocyst venoms of 2 species of jellyfish (Chrysaoraquinquecirrha and Cyanea capillata). Comparative Biochemistry and Physiology Part B: Biochemistry & Molecular Biology 94: 641-646.
    • (1989) Comparative Biochemistry and Physiology Part B: Biochemistry & Molecular Biology , vol.94 , pp. 641-646
    • Long, K.O.1    Burnett, J.W.2
  • 15
    • 0027521670 scopus 로고
    • Tetrazolium-based cell bioassay for neurotoxins active on voltage-sensitive sodium-channels - semiautomated assay for saxitoxins, brevetoxins, and ciguatoxins
    • Manger, R. L., L. S. Leja, S. Y. Lee, J. M. Hungerford & M. M. Wekell, 1993. Tetrazolium-based cell bioassay for neurotoxins active on voltage-sensitive sodium-channels - semiautomated assay for saxitoxins, brevetoxins, and ciguatoxins. Analytical Biochemistry 214: 190-194.
    • (1993) Analytical Biochemistry , vol.214 , pp. 190-194
    • Manger, R.L.1    Leja, L.S.2    Lee, S.Y.3    Hungerford, J.M.4    Wekell, M.M.5
  • 16
    • 33646785425 scopus 로고    scopus 로고
    • Cnidarian toxins acting on voltage-gated ion channels
    • Messerli, S. M. & R. M. Greenberg, 2006. Cnidarian toxins acting on voltage-gated ion channels. Marine Drugs 4: 70-81.
    • (2006) Marine Drugs , vol.4 , pp. 70-81
    • Messerli, S.M.1    Greenberg, R.M.2
  • 17
    • 33847416219 scopus 로고    scopus 로고
    • Insect-selective spider toxins targeting voltage-gated sodium-channels
    • Nicholson, G. M., 2007. Insect-selective spider toxins targeting voltage-gated sodium-channels. Toxicon 49: 490-512.
    • (2007) Toxicon , vol.49 , pp. 490-512
    • Nicholson, G.M.1
  • 18
    • 0025915724 scopus 로고
    • Structure and structure-function-relationships of sea anemone proteins that interact with the sodium-channel
    • Norton, R. S., 1991. Structure and structure-function-relationships of sea anemone proteins that interact with the sodium-channel. Toxicon 29: 1051-1084.
    • (1991) Toxicon , vol.29 , pp. 1051-1084
    • Norton, R.S.1
  • 19
    • 0001716782 scopus 로고    scopus 로고
    • Nematocyst analysis of Cyanea capillata and Cyanealamarckii (Scyphozoa, Cnidaria)
    • Östman, C. & J. Hydman, 1997. Nematocyst analysis of Cyanea capillata and Cyanealamarckii (Scyphozoa, Cnidaria). Scientia Marina 61: 313-344.
    • (1997) Scientia Marina , vol.61 , pp. 313-344
    • Östman, C.1    Hydman, J.2
  • 20
    • 0001370196 scopus 로고
    • The functions of nematocysts in prey capture by epipelagic siphonophores (Coelenterata, Hydrozoa)
    • Purcell, J. E., 1984. The functions of nematocysts in prey capture by epipelagic siphonophores (Coelenterata, Hydrozoa). Biological Bulletin 166: 310-327.
    • (1984) Biological Bulletin , vol.166 , pp. 310-327
    • Purcell, J.E.1
  • 21
    • 0002332222 scopus 로고
    • The correlation between nematocyst types to diets in pelagic Hydrozoa
    • D. A. Hessinger and H. M. Lenhoff (Eds.), San Diego: Academic Press
    • Purcell, J. E. & C. E. Mills, 1988. The correlation between nematocyst types to diets in pelagic Hydrozoa. In Hessinger, D. A. & H. M. Lenhoff (eds), The Biology of Nematocysts. Academic Press, San Diego: 463-485.
    • (1988) The Biology of Nematocysts , pp. 463-485
    • Purcell, J.E.1    Mills, C.E.2
  • 23
    • 33644635402 scopus 로고    scopus 로고
    • Partial purification and characterization of a novel neurotoxin and three cytolysins from box jellyfish (Carybdeamarsupialis) nematocyst venom
    • Sanchez-Rodriguez, J., E. Torrens & L. Segura-Puertas, 2006. Partial purification and characterization of a novel neurotoxin and three cytolysins from box jellyfish (Carybdeamarsupialis) nematocyst venom. Archives of Toxicology 80: 163-168.
    • (2006) Archives of Toxicology , vol.80 , pp. 163-168
    • Sanchez-rodriguez, J.1    Torrens, E.2    Segura-Puertas, L.3
  • 25
    • 0347989461 scopus 로고    scopus 로고
    • Conus venoms: A rich source of novel ion channel-targeted peptides
    • Terlau, H. & B. M. Olivera, 2004. Conus venoms: a rich source of novel ion channel-targeted peptides. Physiological Reviews 84: 41-68.
    • (2004) Physiological Reviews , vol.84 , pp. 41-68
    • Terlau, H.1    Olivera, B.M.2
  • 26
    • 0017354003 scopus 로고
    • The cardiac actions of a toxin-containing material from the jellyfish, Cyanea capillata
    • Walker, A. J. A., 1977. The cardiac actions of a toxin-containing material from the jellyfish, Cyanea capillata. Toxicon 15: 15-27.
    • (1977) Toxicon , vol.15 , pp. 15-27
    • Walker, A.J.A.1
  • 27
    • 77952011385 scopus 로고    scopus 로고
    • Separation and analysis of different types of nematocysts from Cyanea capillata (L.) medusae
    • doi: 10. 1007/s10750-010-0227-6
    • Wiebring, A., H. Helmholz, S. Lassen, A. Prange & G. Jarms, 2010. Separation and analysis of different types of nematocysts from Cyanea capillata (L.) medusae. Hydrobiologia. doi: 10. 1007/s10750-010-0227-6.
    • (2010) Hydrobiologia
    • Wiebring, A.1    Helmholz, H.2    Lassen, S.3    Prange, A.4    Jarms, G.5
  • 29
    • 0037264170 scopus 로고    scopus 로고
    • Overview of the voltage-gated sodium channel family
    • Yu, F. H. & W. A. Catterall, 2003. Overview of the voltage-gated sodium channel family. Genome Biology 4(207): 1-7.
    • (2003) Genome Biology , vol.4 , Issue.207 , pp. 1-7
    • Yu, F.H.1    Catterall, W.A.2
  • 30
    • 0042666840 scopus 로고    scopus 로고
    • Hydralysin, a novel animal group-selective paralytic and cytolytic protein from a noncnidocystic origin in hydra
    • Zhang, M. L., Y. Fishman, D. Sher & E. Zlotkin, 2003. Hydralysin, a novel animal group-selective paralytic and cytolytic protein from a noncnidocystic origin in hydra. Biochemistry 42: 8939-8944.
    • (2003) Biochemistry , vol.42 , pp. 8939-8944
    • Zhang, M.L.1    Fishman, Y.2    Sher, D.3    Zlotkin, E.4


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