메뉴 건너뛰기




Volumn 70, Issue 2, 1996, Pages 567-576

Differences in the multiple step process of inhibition of neurotransmitter release induced by tetanus toxin and botulinum neurotoxins type A and B at Aplysia synapses

Author keywords

SNAP 25; VAMP synaptobrevin

Indexed keywords

BOTULINUM TOXIN; TETANUS TOXIN;

EID: 0029655650     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/0306-4522(95)00336-3     Document Type: Article
Times cited : (17)

References (43)
  • 1
    • 0027416837 scopus 로고
    • Comparison of the intracellular effects of clostridial neurotoxins on exocytosis from streptolysin 0-permeabilized rat pheochromocytoma (PC 12) and bovine adrenal chromaffin cells
    • Ahnert-Hilger G. and Weller U. (1993) Comparison of the intracellular effects of clostridial neurotoxins on exocytosis from streptolysin 0-permeabilized rat pheochromocytoma (PC 12) and bovine adrenal chromaffin cells. Neuroscience 53, 547-552.
    • (1993) Neuroscience , vol.53 , pp. 547-552
    • Ahnert-Hilger, G.1    Weller, U.2
  • 2
    • 0028040137 scopus 로고
    • Pore formation by tetanus toxin, its chain and fragments in neuronal membranes and evaluation of the underlying motifs in the structure of the toxin molecule
    • Beise J., Hahnen J., Andersen-Beckh B. and Dreyer F. (1994) Pore formation by tetanus toxin, its chain and fragments in neuronal membranes and evaluation of the underlying motifs in the structure of the toxin molecule. Naunyn-Schmiedeberg's Arch. Pharmac. 349, 66-73.
    • (1994) Naunyn-Schmiedeberg's Arch. Pharmac. , vol.349 , pp. 66-73
    • Beise, J.1    Hahnen, J.2    Andersen-Beckh, B.3    Dreyer, F.4
  • 3
    • 0022556314 scopus 로고
    • 125I-labeled botulinum neurotoxins with nerve terminals. I. Ultrastructural autoradiographic localization and quantitation of distinct membrane acceptors for types a and B on motor nerves
    • 125I-labeled botulinum neurotoxins with nerve terminals. I. Ultrastructural autoradiographic localization and quantitation of distinct membrane acceptors for types A and B on motor nerves. J. Cell Biol. 103, 521-534.
    • (1986) J. Cell Biol. , vol.103 , pp. 521-534
    • Black, J.D.1    Dolly, J.O.2
  • 4
    • 0022556315 scopus 로고
    • 125I-labeled botulinum neurotoxins with nerve terminals. II. Autoradiographic evidence for its uptake into motor nerves by acceptor-mediated endocytosis
    • 125I-labeled botulinum neurotoxins with nerve terminals. II. Autoradiographic evidence for its uptake into motor nerves by acceptor-mediated endocytosis. J. Cell Biol. 103, 535-544.
    • (1986) J. Cell Biol. , vol.103 , pp. 535-544
    • Black, J.D.1    Dolly, J.O.2
  • 5
    • 0000700903 scopus 로고
    • Peptide toxins that alter neurotransmitter release
    • Selective Neurotoxicity (eds Herken H. and Hucho F.)
    • Dolly J. O. (1992) Peptide toxins that alter neurotransmitter release. In Selective Neurotoxicity (eds Herken H. and Hucho F.), Handbook of Experimental Pharmacology 102, 681-717.
    • (1992) Handbook of Experimental Pharmacology , vol.102 , pp. 681-717
    • Dolly, J.O.1
  • 7
    • 0022485787 scopus 로고
    • Ion-conducting channels produced by botulinum toxin in planar lipid membranes
    • Donovan J. J. and Middlebrook J. L. (1986) Ion-conducting channels produced by botulinum toxin in planar lipid membranes. Biochemistry 25, 2872-2876.
    • (1986) Biochemistry , vol.25 , pp. 2872-2876
    • Donovan, J.J.1    Middlebrook, J.L.2
  • 8
    • 0021052568 scopus 로고
    • Transmitter release in tetanus and botulinum a toxin-poisoned mammalian motor endplates and its dependence on nerve stimulation and temperature
    • Dreyer F. and Schmitt A. (1983) Transmitter release in tetanus and botulinum A toxin-poisoned mammalian motor endplates and its dependence on nerve stimulation and temperature. Pflügers Arch. 399, 228-234.
    • (1983) Pflügers Arch. , vol.399 , pp. 228-234
    • Dreyer, F.1    Schmitt, A.2
  • 9
    • 0028819440 scopus 로고
    • Synaptobrevin binding to synaptophysin: A potential mechanism for controlling the exocytotic fusion machine
    • Edelmann L., Hanson P. I., Chapman E. R. and Jahn R. (1995) Synaptobrevin binding to synaptophysin: a potential mechanism for controlling the exocytotic fusion machine. Eur. molec. Biol. Org. J. 14, 224-231.
    • (1995) Eur. Molec. Biol. Org. J. , vol.14 , pp. 224-231
    • Edelmann, L.1    Hanson, P.I.2    Chapman, E.R.3    Jahn, R.4
  • 10
    • 0028558884 scopus 로고
    • Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane proteins and various sized
    • Foran P., Shone C. C. and Dolly J. O. (1994) Differences in the protease activities of tetanus and botulinum B toxins revealed by the cleavage of vesicle-associated membrane proteins and various sized. Biochemistry 33, 15,365-15,374.
    • (1994) Biochemistry , vol.33
    • Foran, P.1    Shone, C.C.2    Dolly, J.O.3
  • 11
    • 0023180498 scopus 로고
    • Distinct sites of action of clostridial neurotoxins revealed by double-poisoning of mouse motor nerve terminals
    • Gansel M., Penner R. and Dreyer F. (1987) Distinct sites of action of clostridial neurotoxins revealed by double-poisoning of mouse motor nerve terminals. Pflügers Arch. 409, 533-539.
    • (1987) Pflügers Arch. , vol.409 , pp. 533-539
    • Gansel, M.1    Penner, R.2    Dreyer, F.3
  • 12
    • 0018838743 scopus 로고
    • Tetanus toxin blocks the neuromuscular transmission in vitro like botulinum a toxin
    • Habermann E., Dreyer F. and Bigalke H. (1980) Tetanus toxin blocks the neuromuscular transmission in vitro like botulinum A toxin. Naunyn-Schmiedeberg's Arch. Pharmac. 311, 33-40.
    • (1980) Naunyn-Schmiedeberg's Arch. Pharmac. , vol.311 , pp. 33-40
    • Habermann, E.1    Dreyer, F.2    Bigalke, H.3
  • 14
    • 85047694491 scopus 로고
    • Involvement of the constituent chains of botulinum neurotoxins, types A and B, in their blockade of neurotransmitter release
    • Maisey E. A., Wadsworth J. D. F., Poulain B., Shone C., Melling J., Gibbs P., Taue L. and Dolly J. O. (1988) Involvement of the constituent chains of botulinum neurotoxins, types A and B, in their blockade of neurotransmitter release. Eur. J. Biochem. 177, 683-691.
    • (1988) Eur. J. Biochem. , vol.177 , pp. 683-691
    • Maisey, E.A.1    Wadsworth, J.D.F.2    Poulain, B.3    Shone, C.4    Melling, J.5    Gibbs, P.6    Taue, L.7    Dolly, J.O.8
  • 15
    • 0028963427 scopus 로고
    • Synaptic core complex of synaptobrevin, syntaxin, and SNAP25 forms high affinity α-SNAP binding site
    • McMahon H. T. and Südhof T. C. (1995) Synaptic core complex of synaptobrevin, syntaxin, and SNAP25 forms high affinity α-SNAP binding site. J. biol. Chem. 270, 2213-2217.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2213-2217
    • McMahon, H.T.1    Südhof, T.C.2
  • 16
    • 0024599014 scopus 로고
    • Interaction of tetanus toxin with lipid vesicles. Effects of pH, surface charges, and transmembrane potential on the kinetics of channel formation
    • Menestrina G., Forti F. and Gambale G. (1989) Interaction of tetanus toxin with lipid vesicles. Effects of pH, surface charges, and transmembrane potential on the kinetics of channel formation. Biophys. J. 55, 393-405.
    • (1989) Biophys. J. , vol.55 , pp. 393-405
    • Menestrina, G.1    Forti, F.2    Gambale, G.3
  • 17
    • 0024356962 scopus 로고
    • Light chain of tetanus toxin intracellularly inhibits acetylcholine release at neuro-neuronal synapses, and its internalization is mediated by heavy chain
    • Mochida S., Poulain B., Weller U., Habermann E. and Taue L. (1989) Light chain of tetanus toxin intracellularly inhibits acetylcholine release at neuro-neuronal synapses, and its internalization is mediated by heavy chain. Fedn Eur. biochem. Socs Lett. 253, 47-51.
    • (1989) Fedn Eur. Biochem. Socs Lett. , vol.253 , pp. 47-51
    • Mochida, S.1    Poulain, B.2    Weller, U.3    Habermann, E.4    Taue, L.5
  • 18
    • 0028236333 scopus 로고
    • Bacterial protein toxins penetrate cells via a four-step mechanism
    • Montecucco C., Papini E. and Schiavo G. (1994) Bacterial protein toxins penetrate cells via a four-step mechanism. Fedn Eur. biochem. Socs Lett. 346, 92-98.
    • (1994) Fedn Eur. Biochem. Socs Lett. , vol.346 , pp. 92-98
    • Montecucco, C.1    Papini, E.2    Schiavo, G.3
  • 19
    • 0029613765 scopus 로고
    • Structure and function of tetanus and botulinum neurotoxins
    • in press
    • Montecucco C. and Schiavo G. (1995) Structure and function of tetanus and botulinum neurotoxins. Q. Rev. Biophys. (in press).
    • (1995) Q. Rev. Biophys.
    • Montecucco, C.1    Schiavo, G.2
  • 20
    • 0028268948 scopus 로고
    • Clostridial neurotoxins: New tools for dissecting exocytosis
    • Niemann H., Blasi J. and Jahn R. (1994) Clostridial neurotoxins: new tools for dissecting exocytosis. Trends Cell Biol. 4, 179-185.
    • (1994) Trends Cell Biol. , vol.4 , pp. 179-185
    • Niemann, H.1    Blasi, J.2    Jahn, R.3
  • 21
    • 0023196480 scopus 로고
    • A study of the mechanism of internalisation of tetanus toxin by primary mouse spinal cord cultures
    • Parton R. G., Ockleford C. D. and Critchley D. R. (1987) A study of the mechanism of internalisation of tetanus toxin by primary mouse spinal cord cultures. J. Neurochem. 49, 1057-1058.
    • (1987) J. Neurochem. , vol.49 , pp. 1057-1058
    • Parton, R.G.1    Ockleford, C.D.2    Critchley, D.R.3
  • 22
    • 0027946206 scopus 로고
    • Fusion complex formation protects synaptobrevin against proteolysis by tetanus toxin light chain
    • Pellegrini L., O'Connor V. and Betz H. (1994) Fusion complex formation protects synaptobrevin against proteolysis by tetanus toxin light chain. Fedn Eur. biochem. Socs Lett. 353, 319-323.
    • (1994) Fedn Eur. Biochem. Socs Lett. , vol.353 , pp. 319-323
    • Pellegrini, L.1    O'Connor, V.2    Betz, H.3
  • 23
    • 0022454866 scopus 로고
    • Intracellularly injected tetanus toxin inhibits exocytosis in bovine adrenal chromaffin cells
    • Penner R., Neher E. and Dreyer F. (1986) Intracellularly injected tetanus toxin inhibits exocytosis in bovine adrenal chromaffin cells. Nature 324, 76-78.
    • (1986) Nature , vol.324 , pp. 76-78
    • Penner, R.1    Neher, E.2    Dreyer, F.3
  • 24
    • 0026688903 scopus 로고
    • Differences in temperature dependence of botulinum and tetanus uptake in Aplysia
    • Poulain B., De Paiva A., Dolly J. O., Weller U. and Taue L. (1992) Differences in temperature dependence of botulinum and tetanus uptake in Aplysia. Neurosci. Lett. 139, 289-292.
    • (1992) Neurosci. Lett. , vol.139 , pp. 289-292
    • Poulain, B.1    De Paiva, A.2    Dolly, J.O.3    Weller, U.4    Taue, L.5
  • 25
    • 0025895748 scopus 로고
    • Heterologous combinations of heavy and light chains from botulinum neurotoxin a and tetanus toxin inhibit neuro-transmitter release in Aplysia
    • Poulain B., Mochida S., Weller U., Högy B., Habermann E., Wadsworth J. D. F., Dolly J. O., Shone C. C. and Taue L. (1991) Heterologous combinations of heavy and light chains from botulinum neurotoxin A and tetanus toxin inhibit neuro-transmitter release in Aplysia. J. biol. Chem. 266, 9580-9585.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9580-9585
    • Poulain, B.1    Mochida, S.2    Weller, U.3    Högy, B.4    Habermann, E.5    Wadsworth, J.D.F.6    Dolly, J.O.7    Shone, C.C.8    Taue, L.9
  • 26
    • 0023888382 scopus 로고
    • Neurotransmitter release is blocked intracellularly by Botulinum neurotoxin and this requires uptake of both its polypeptides by a process mediated by the larger chain
    • Poulain B., Taue L., Maisey E. A., Wadsworth J. D. F., Mohan M. and Dolly J. O. (1988) Neurotransmitter release is blocked intracellularly by Botulinum neurotoxin and this requires uptake of both its polypeptides by a process mediated by the larger chain. Proc. natn. Acad. Sci. U.S.A. 85, 4090-4093.
    • (1988) Proc. Natn. Acad. Sci. U.S.A. , vol.85 , pp. 4090-4093
    • Poulain, B.1    Taue, L.2    Maisey, E.A.3    Wadsworth, J.D.F.4    Mohan, M.5    Dolly, J.O.6
  • 28
    • 0028143698 scopus 로고
    • Mechanism of intracellular protein transport
    • Rothman J. E. (1994) Mechanism of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 30
    • 0019855166 scopus 로고
    • At least three sequential steps are involved in the tetanus toxin-induced block of neuromuscular transmission
    • Schmitt A., Dreyer F. and John C. (1981) At least three sequential steps are involved in the tetanus toxin-induced block of neuromuscular transmission. Naunyn-Schmiedeberg's Arch. Pharmac. 317, 326-330.
    • (1981) Naunyn-Schmiedeberg's Arch. Pharmac. , vol.317 , pp. 326-330
    • Schmitt, A.1    Dreyer, F.2    John, C.3
  • 31
    • 0018906584 scopus 로고
    • Kinetic studies on the interaction between botulinum toxin type a and the cholinergic neuromuscular junction
    • Simpson L. L. (1980) Kinetic studies on the interaction between botulinum toxin type A and the cholinergic neuromuscular junction. J. Pharmac. exp. Ther. 212, 16-21.
    • (1980) J. Pharmac. Exp. Ther. , vol.212 , pp. 16-21
    • Simpson, L.L.1
  • 32
    • 0019956937 scopus 로고
    • The interaction between aminoquinolines and presynaptically acting neurotoxins
    • Simpson L. L. (1982) The interaction between aminoquinolines and presynaptically acting neurotoxins. J. Pharmac. exp. Ther. 222, 43-48.
    • (1982) J. Pharmac. Exp. Ther. , vol.222 , pp. 43-48
    • Simpson, L.L.1
  • 33
    • 0020522175 scopus 로고
    • Ammonium chloride and methylamine hydrochloride antagonize clostridial neurotoxins
    • Simpson L. L. (1983) Ammonium chloride and methylamine hydrochloride antagonize clostridial neurotoxins. J. Pharmac. exp. Ther. 225, 546-552.
    • (1983) J. Pharmac. Exp. Ther. , vol.225 , pp. 546-552
    • Simpson, L.L.1
  • 34
    • 0022555430 scopus 로고
    • Molecular pharmacology of botulinum toxin and tetanus toxin
    • Simpson L. L. (1986) Molecular pharmacology of botulinum toxin and tetanus toxin. A. Rev. Pharmac. Toxic. 26, 427-453.
    • (1986) A. Rev. Pharmac. Toxic. , vol.26 , pp. 427-453
    • Simpson, L.L.1
  • 35
    • 0023899939 scopus 로고
    • Use of pharmacologic antagonists to deduce commonalities of biological activity among clostridial neurotoxins
    • Simpson L. L. (1988) Use of pharmacologic antagonists to deduce commonalities of biological activity among clostridial neurotoxins. J. Pharmac. exp. Ther. 245, 867-872.
    • (1988) J. Pharmac. Exp. Ther. , vol.245 , pp. 867-872
    • Simpson, L.L.1
  • 36
    • 0020663105 scopus 로고
    • Botulinum neurotoxin type E: Studies on mechanism of action and on structure-activity relationships
    • Simpson L. L. and DasGupta B. R. (1982) Botulinum neurotoxin type E: studies on mechanism of action and on structure-activity relationships. J. Pharmac. exp. Ther. 224, 135-140.
    • (1982) J. Pharmac. Exp. Ther. , vol.224 , pp. 135-140
    • Simpson, L.L.1    DasGupta, B.R.2
  • 37
    • 0016726129 scopus 로고
    • Comparison between the retrograde axonal transport of nerve growth factor and tetanus toxin in motor, sensory and adrenergic neurons
    • Stöckel K., Schwab M. and Thoenen H. (1975) Comparison between the retrograde axonal transport of nerve growth factor and tetanus toxin in motor, sensory and adrenergic neurons. Brain Res. 99, 1-16.
    • (1975) Brain Res. , vol.99 , pp. 1-16
    • Stöckel, K.1    Schwab, M.2    Thoenen, H.3
  • 38
    • 0028942065 scopus 로고
    • Vesicle-associated membrane protein-2 (synaptobrevin-2) forms a complex with synaptophysin
    • Washbourne P., Schiavo G. and Montecucco C. (1995) Vesicle-associated membrane protein-2 (synaptobrevin-2) forms a complex with synaptophysin. Biochem. J. 305, 721-724.
    • (1995) Biochem. J. , vol.305 , pp. 721-724
    • Washbourne, P.1    Schiavo, G.2    Montecucco, C.3
  • 39
    • 0025977925 scopus 로고
    • Cooperative action of the light chain of tetanus and the heavy chain of botulinum toxin type A on the transmitter release of mammalian motor endplates
    • Weller U., Aktories M.-E., Gansel M. and Dreyer F. (1991) Cooperative action of the light chain of tetanus and the heavy chain of botulinum toxin type A on the transmitter release of mammalian motor endplates. Neurosci. Lett. 122, 132-134.
    • (1991) Neurosci. Lett. , vol.122 , pp. 132-134
    • Weller, U.1    Aktories, M.-E.2    Gansel, M.3    Dreyer, F.4
  • 40
    • 0024395212 scopus 로고
    • Chains and fragments of tetanus toxin. Separation, reassociation and pharmacological properties
    • Weller U., Dauzenroth M.-E., Meyer zu Heringdorf D. and Habermann E. (1989) Chains and fragments of tetanus toxin. Separation, reassociation and pharmacological properties. Eur. J. Biochem. 182, 649-656.
    • (1989) Eur. J. Biochem. , vol.182 , pp. 649-656
    • Weller, U.1    Dauzenroth, M.-E.2    Meyer Zu Heringdorf, D.3    Habermann, E.4
  • 41
    • 0023028984 scopus 로고
    • Quantitative comparison between tetanus toxin, some fragments and toxoid for binding and axonal transport in the rat
    • Weller U., Taylor C. F. and Habermann E. (1986) Quantitative comparison between tetanus toxin, some fragments and toxoid for binding and axonal transport in the rat. Toxicon 24, 1055-1063.
    • (1986) Toxicon , vol.24 , pp. 1055-1063
    • Weller, U.1    Taylor, C.F.2    Habermann, E.3
  • 42
    • 0000354574 scopus 로고
    • Tetanus and botulinum neurotoxins
    • Selective Neurotoxicity eds Herken H. and Hucho F.
    • Wellhöner H. H. (1992) Tetanus and botulinum neurotoxins. In Selective Neurotoxicity (eds Herken H. and Hucho F.), Handbook of Experimental Pharmacology 102, 357-417.
    • (1992) Handbook of Experimental Pharmacology , vol.102 , pp. 357-417
    • Wellhöner, H.H.1
  • 43
    • 0027946632 scopus 로고
    • Bafilomycin Al inhibits the action of tetanus toxin in spinal cord neurons in cell culture
    • Williamson L. C. and Neale E. A. (1994) Bafilomycin Al inhibits the action of tetanus toxin in spinal cord neurons in cell culture. J. Neurochem. 63, 2342-2345.
    • (1994) J. Neurochem. , vol.63 , pp. 2342-2345
    • Williamson, L.C.1    Neale, E.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.