메뉴 건너뛰기




Volumn 289, Issue 3, 1999, Pages 1509-1516

Characterization of a vertebrate neuromuscular junction that demonstrates selective resistance to Botulinum toxin

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LATROTOXIN; BETA BUNGAROTOXIN; BOTULINUM TOXIN A; BOTULINUM TOXIN B; CELL SURFACE RECEPTOR;

EID: 0032995728     PISSN: 00223565     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (19)

References (39)
  • 1
    • 0017669630 scopus 로고
    • Isolation and characterization of presynaptically acting neurotoxins from the venom of Bungarus snakes
    • Abe T, Alem S and Miledi R (1977) Isolation and characterization of presynaptically acting neurotoxins from the venom of Bungarus snakes. Eur J Biochem 80:1-12.
    • (1977) Eur J Biochem , vol.80 , pp. 1-12
    • Abe, T.1    Alem, S.2    Miledi, R.3
  • 2
    • 0029074299 scopus 로고
    • Molecular aspects of tetanus and botulinum neurotoxin poisoning
    • Ahnert-Hilger G and Bigalke H (1995) Molecular aspects of tetanus and botulinum neurotoxin poisoning Prog Neurobiol 46:83-96.
    • (1995) Prog Neurobiol , vol.46 , pp. 83-96
    • Ahnert-Hilger, G.1    Bigalke, H.2
  • 3
    • 0025943451 scopus 로고
    • Lectins from Triticum vulgaris and Limax flavus are universal antagonists of botulinum neurotoxin and tetanus toxin
    • Bakry N, Kamata Y and Simpson LL (1991a) Lectins from Triticum vulgaris and Limax flavus are universal antagonists of botulinum neurotoxin and tetanus toxin. J Pharmacol Exp Ther 258:830-836.
    • (1991) J Pharmacol Exp Ther , vol.258 , pp. 830-836
    • Bakry, N.1    Kamata, Y.2    Simpson, L.L.3
  • 4
    • 0025936145 scopus 로고
    • Tetanus toxin and neuronal membranes: The relationship between binding and toxicity
    • Bakry N, Kamata Y, Sorensen R and Simpson LL (1991b) Tetanus toxin and neuronal membranes: The relationship between binding and toxicity. J Pharmacol Exp Ther 258:613-619.
    • (1991) J Pharmacol Exp Ther , vol.258 , pp. 613-619
    • Bakry, N.1    Kamata, Y.2    Sorensen, R.3    Simpson, L.L.4
  • 5
    • 0030914435 scopus 로고    scopus 로고
    • Expression of botulinum toxin binding sites in Xenopus oocytes
    • Bakry NM, Kamata Y and Simpson LL (1997) Expression of botulinum toxin binding sites in Xenopus oocytes. Infect Immun 65:2225-2232.
    • (1997) Infect Immun , vol.65 , pp. 2225-2232
    • Bakry, N.M.1    Kamata, Y.2    Simpson, L.L.3
  • 6
    • 0026584039 scopus 로고
    • Optical analysis of synaptic vesicle recycling at the frog neuromuscular junction
    • Betz WJ and Bewick GS (1992) Optical analysis of synaptic vesicle recycling at the frog neuromuscular junction Science (Wash DC) 255:200-203.
    • (1992) Science (Wash DC) , vol.255 , pp. 200-203
    • Betz, W.J.1    Bewick, G.S.2
  • 7
    • 0027464699 scopus 로고
    • Optical and electrophysiological monitoring of transmitter release and synaptic vesicle recycling at the frog neuromuscular junction
    • Betz WJ and Bewick GS (1993) Optical and electrophysiological monitoring of transmitter release and synaptic vesicle recycling at the frog neuromuscular junction. J Physiol (Lond) 460:287-309.
    • (1993) J Physiol (Lond) , vol.460 , pp. 287-309
    • Betz, W.J.1    Bewick, G.S.2
  • 8
    • 0026536634 scopus 로고
    • Activity-dependent fluorescent staining and destaining of living vertebrate motor nerve terminals
    • Betz WJ, Mao F and Bewick GS (1992) Activity-dependent fluorescent staining and destaining of living vertebrate motor nerve terminals. J Neurosci 12:363-375.
    • (1992) J Neurosci , vol.12 , pp. 363-375
    • Betz, W.J.1    Mao, F.2    Bewick, G.S.3
  • 9
    • 0002301979 scopus 로고
    • The action of botulinum toxin on the neuromuscular junction
    • Burgen ASV, Dickens F and Zatman LJ (1949) The action of botulinum toxin on the neuromuscular junction. J Physiol (Lond) 109:10-24.
    • (1949) J Physiol (Lond) , vol.109 , pp. 10-24
    • Burgen, A.S.V.1    Dickens, F.2    Zatman, L.J.3
  • 10
    • 0021892584 scopus 로고
    • Influence of divalent cations on the phospholipase-independent action of á-bungarotoxin at frog neuromuscular junctions
    • Caratsch CG, Miledi R and Strong PN (1985) Influence of divalent cations on the phospholipase-independent action of á-bungarotoxin at frog neuromuscular junctions. J Physiol (Lond) 363:169-179.
    • (1985) J Physiol (Lond) , vol.363 , pp. 169-179
    • Caratsch, C.G.1    Miledi, R.2    Strong, P.N.3
  • 11
    • 0030897432 scopus 로고    scopus 로고
    • In vitro characterization of botulinum toxin types A, C and D action on human tissues: Combined electrophysiologic, pharmacologic and molecular biologic approaches
    • Coffield JA, Bakry N, Zhang R-D, Carlson J, Gomella LG and Simpson LL (1997) In vitro characterization of botulinum toxin types A, C and D action on human tissues: Combined electrophysiologic, pharmacologic and molecular biologic approaches. J Pharmacol Exp Ther 280:1489-1498.
    • (1997) J Pharmacol Exp Ther , vol.280 , pp. 1489-1498
    • Coffield, J.A.1    Bakry, N.2    Zhang, R.-D.3    Carlson, J.4    Gomella, L.G.5    Simpson, L.L.6
  • 12
    • 0028807364 scopus 로고
    • Monitoring of black widow spider venom (BWSV) induced exo- and endocytosis in living frog motor nerve terminals with FM1-43
    • Henkel AW and Betz WJ (1995) Monitoring of Black Widow spider venom (BWSV) induced exo- and endocytosis in living frog motor nerve terminals with FM1-43 Neuropharmacology 34:1397-1406.
    • (1995) Neuropharmacology , vol.34 , pp. 1397-1406
    • Henkel, A.W.1    Betz, W.J.2
  • 13
    • 0029885396 scopus 로고    scopus 로고
    • Synaptic vesicle movements monitored by fluorescence recovery after photobleaching in nerve terminals stained with FM1-43
    • Henkel AW, Simpson LL, Ridge RMAP and Betz WJ (1996) Synaptic vesicle movements monitored by fluorescence recovery after photobleaching in nerve terminals stained with FM1-43 J Neurosci 16:3960-3967.
    • (1996) J Neurosci , vol.16 , pp. 3960-3967
    • Henkel, A.W.1    Simpson, L.L.2    Rmap, R.3    Betz, W.J.4
  • 14
    • 0027516462 scopus 로고
    • Purification and characterization of the ganglioside-binding fragment of Clostridium botulinum type E neurotoxin
    • Kamata Y, Kimura Y, Hiroi T, Sakaguchi G and Kozaki S (1993) Purification and characterization of the ganglioside-binding fragment of Clostridium botulinum type E neurotoxin. Biochim Biophys Acta 1156:213-218.
    • (1993) Biochim Biophys Acta , vol.1156 , pp. 213-218
    • Kamata, Y.1    Kimura, Y.2    Hiroi, T.3    Sakaguchi, G.4    Kozaki, S.5
  • 15
    • 0018867612 scopus 로고
    • Interaction between Clostridium botulinum neurotoxin and gangliosides
    • Kitamura M, Iwamori M and Nagal Y (1980) Interaction between Clostridium botulinum neurotoxin and gangliosides. Biochim Biophys Acta 628:328-335.
    • (1980) Biochim Biophys Acta , vol.628 , pp. 328-335
    • Kitamura, M.1    Iwamori, M.2    Nagal, Y.3
  • 16
    • 0029031896 scopus 로고
    • Synaptic vesicle dynamics in living cultured hippocampal neurons vizualized with CY-3 conjugated antibodies directed against the lumenal domain of synaptotagmin
    • Kraszewski K, Mundigl O, Daniell L, Verderio C, Matteoli M and De Camilli P (1995) Synaptic vesicle dynamics in living cultured hippocampal neurons vizualized with CY-3 conjugated antibodies directed against the lumenal domain of synaptotagmin. J Neurosci 15:4328-4342.
    • (1995) J Neurosci , vol.15 , pp. 4328-4342
    • Kraszewski, K.1    Mundigl, O.2    Daniell, L.3    Verderio, C.4    Matteoli, M.5    De Camilli, P.6
  • 18
    • 0016296642 scopus 로고
    • Absence of action potentials in frog slow muscle fibres paralysed by botulinum toxin
    • Miledi R and Spitzer NC (1974) Absence of action potentials in frog slow muscle fibres paralysed by botulinum toxin. J Physiol (Lond) 241:183-199.
    • (1974) J Physiol (Lond) , vol.241 , pp. 183-199
    • Miledi, R.1    Spitzer, N.C.2
  • 19
    • 46149134882 scopus 로고
    • How do tetanus and botulinum toxins bind to neuronal membranes?
    • Montecucco C (1986) How do tetanus and botulinum toxins bind to neuronal membranes? Trends Biochem Sci 11:314-317.
    • (1986) Trends Biochem Sci , vol.11 , pp. 314-317
    • Montecucco, C.1
  • 20
    • 0028310404 scopus 로고
    • Mechanism of action of tetanus and botulinum neurotoxins
    • Montecucco C and Schiavo G (1994) Mechanism of action of tetanus and botulinum neurotoxins. Mol Microbiol 13:1-8.
    • (1994) Mol Microbiol , vol.13 , pp. 1-8
    • Montecucco, C.1    Schiavo, G.2
  • 21
    • 0028941983 scopus 로고
    • A radioimmunoassay to monitor synaptic activity in hippocampal neurons in vitro
    • Mundigl O, Verderio C, Kraszewski K, DeCamilli P and Matteoli M (1995) A radioimmunoassay to monitor synaptic activity in hippocampal neurons in vitro. Eur J Cell Biol 66:246-256. mc>Nishiki T, Kamata Y, Nemoto Y, Omori A, Ito T, Takahashi M and Kozaki S (1994) Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes. J Biol Chem 269: 10498-10503.
    • (1995) Eur J Cell Biol , vol.66 , pp. 246-256
    • Mundigl, O.1    Verderio, C.2    Kraszewski, K.3    DeCamilli, P.4    Matteoli, M.5
  • 22
    • 0028341442 scopus 로고
    • Identification of protein receptor for clostridium botulinum type B neurotoxin in rat brain synaptosomes
    • Mundigl O, Verderio C, Kraszewski K, DeCamilli P and Matteoli M (1995) A radioimmunoassay to monitor synaptic activity in hippocampal neurons in vitro. Eur J Cell Biol 66:246-256. mc>Nishiki T, Kamata Y, Nemoto Y, Omori A, Ito T, Takahashi M and Kozaki S (1994) Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes. J Biol Chem 269: 10498-10503.
    • (1994) J Biol Chem , vol.269 , pp. 10498-10503
    • Nishiki, T.1    Kamata, Y.2    Nemoto, Y.3    Omori, A.4    Ito, T.5    Takahashi, M.6    Kozaki, S.7
  • 23
    • 0027486425 scopus 로고
    • Solubilization and characterization of the acceptor for Clostridium botulinum type B neurotoxin from rat brain synaptic membranes
    • Nishiki T, Ogasawara J, Kamata Y and Kozaki S (1993) Solubilization and characterization of the acceptor for Clostridium botulinum type B neurotoxin from rat brain synaptic membranes. Biochim Biophys Acta 1158:333-338.
    • (1993) Biochim Biophys Acta , vol.1158 , pp. 333-338
    • Nishiki, T.1    Ogasawara, J.2    Kamata, Y.3    Kozaki, S.4
  • 24
    • 0030064241 scopus 로고    scopus 로고
    • The high affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/ GD1a
    • Nishiki T, Tokuyama Y, Kamata Y, Nemoto Y, Yoshida A, Sato K, Sekiguchi M, Takahashi M and Kozaki S (1996) The high affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/ GD1a. FEBS Lett 378:253-257.
    • (1996) FEBS Lett , vol.378 , pp. 253-257
    • Nishiki, T.1    Tokuyama, Y.2    Kamata, Y.3    Nemoto, Y.4    Yoshida, A.5    Sato, K.6    Sekiguchi, M.7    Takahashi, M.8    Kozaki, S.9
  • 26
    • 0024829325 scopus 로고
    • Multiple domains of botulinum neurotoxin contribute to its inhibition of transmitter release in Aplysia neurons
    • Poulain B, Wadsworth JDF, Shone CC, Mochida S, Lande S, Melling J, Dolly JO and Taue L (1989) Multiple domains of botulinum neurotoxin contribute to its inhibition of transmitter release in Aplysia neurons. J Biol Chem 264:21928-21933.
    • (1989) J Biol Chem , vol.264 , pp. 21928-21933
    • Poulain, B.1    Wadsworth, J.D.F.2    Shone, C.C.3    Mochida, S.4    Lande, S.5    Melling, J.6    Dolly, J.O.7    Taue, L.8
  • 27
    • 0017672831 scopus 로고
    • Action of brown widow spider venom and botulinum toxin on the frog neuromuscular junction examined with the freeze-fracture technique
    • Pumplin DW and Reese TS (1977) Action of brown widow spider venom and botulinum toxin on the frog neuromuscular junction examined with the freeze-fracture technique. J Physiol (Lond) 273:443-457.
    • (1977) J Physiol (Lond) , vol.273 , pp. 443-457
    • Pumplin, D.W.1    Reese, T.S.2
  • 28
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H and Von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166:368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 29
    • 0028355349 scopus 로고
    • Tetanus and botulinum neurotoxins are zinc proteases specific for components of the neuroeocytosis apparatus
    • Schiavo G, Rossetto O, Benfenati F, Poulain B and Montecucco C (1994) Tetanus and botulinum neurotoxins are zinc proteases specific for components of the neuroeocytosis apparatus. Ann NY Acad Sci 710:65-75.
    • (1994) Ann NY Acad Sci , vol.710 , pp. 65-75
    • Schiavo, G.1    Rossetto, O.2    Benfenati, F.3    Poulain, B.4    Montecucco, C.5
  • 30
  • 31
    • 0019619833 scopus 로고
    • The origin, structure, and pharmacological activity of botulinum toxin
    • Simpson LL (1981) The origin, structure, and pharmacological activity of botulinum toxin. Pharmacol Rev 33:155-188.
    • (1981) Pharmacol Rev , vol.33 , pp. 155-188
    • Simpson, L.L.1
  • 32
    • 0015084187 scopus 로고
    • Ganglioside inactivation of botulinum toxin
    • Simpson LL and Rapport MM (1971) Ganglioside inactivation of botulinum toxin. J Neurochem 18:1341-1343.
    • (1971) J Neurochem , vol.18 , pp. 1341-1343
    • Simpson, L.L.1    Rapport, M.M.2
  • 33
    • 0018906584 scopus 로고
    • Kinetic studies on the interaction between botulinum toxin type A and the cholinergic neuromuscular junction
    • Simpson LL (1980) Kinetic studies on the interaction between botulinum toxin type A and the cholinergic neuromuscular junction. J Pharmacol Exp Ther 212:16-21.
    • (1980) J Pharmacol Exp Ther , vol.212 , pp. 16-21
    • Simpson, L.L.1
  • 34
    • 0019956937 scopus 로고
    • The interaction between aminoquinolines and presynaptically acting neurotoxins
    • Simpson LL (1982) The interaction between aminoquinolines and presynaptically acting neurotoxins. J Pharmacol Exp Ther 222:43-48.
    • (1982) J Pharmacol Exp Ther , vol.222 , pp. 43-48
    • Simpson, L.L.1
  • 35
    • 0020522175 scopus 로고
    • Ammonium chloride and methylamine hydrochloride antagonize clostridial neurotoxins
    • Simpson LL (1983) Ammonium chloride and methylamine hydrochloride antagonize clostridial neurotoxins. J Pharmacol Exp Ther 225:546-552.
    • (1983) J Pharmacol Exp Ther , vol.225 , pp. 546-552
    • Simpson, L.L.1
  • 37
    • 0028293577 scopus 로고
    • Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins
    • Simpson LL, Coffield JA and Bakry N (1994) Inhibition of vacuolar adenosine triphosphatase antagonizes the effects of clostridial neurotoxins but not phospholipase A2 neurotoxins. J Pharmacol Exp Ther 269:256-262.
    • (1994) J Pharmacol Exp Ther , vol.269 , pp. 256-262
    • Simpson, L.L.1    Coffield, J.A.2    Bakry, N.3
  • 38
    • 0020663105 scopus 로고
    • Botulinum neurotoxin type E: Studies on mechanism of action and on structure-activity relationships
    • Simpson LL and DasGupta BR (1983) Botulinum neurotoxin type E: Studies on mechanism of action and on structure-activity relationships. J Pharmacol Exp Ther 224:135-140.
    • (1983) J Pharmacol Exp Ther , vol.224 , pp. 135-140
    • Simpson, L.L.1    DasGupta, B.R.2
  • 39
    • 0024272567 scopus 로고
    • Isolation and characterization of the botulinum neurotoxins
    • Simpson LL, Schmidt JJ and Middlebrook JL (1988) Isolation and characterization of the botulinum neurotoxins. Methods Enzymol 165:76-85.
    • (1988) Methods Enzymol , vol.165 , pp. 76-85
    • Simpson, L.L.1    Schmidt, J.J.2    Middlebrook, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.