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Botulinum neurotoxin (NT) is a potent inhibitor of neurotransmitter secretion, but its intracellular mechanism and site of action are unknown. In this study, the intracellular action of NT was investigated by rendering the secretory apparatus of PC12 cells accessible to macromolecules by a recently described "cell cracking" procedure. Soluble cytoplasmic(More)
The role of SNAP-25 (synaptosomal associated protein of 25 kDa) isotypes in the neurotransmitter release process was examined by varying their relative abundance during PC12 cell differentiation induced by nerve growth factor (NGF). Norepinephrine release by NGF-differentiated PC12 cells is more sensitive to type A botulinum toxin (BoNT/A) than by(More)
Permeabilized PC12 cells exhibit a Ca(2+)-stimulated norepinephrine secretory pathway which is sensitive to botulinum neurotoxin serotypes A, B and E [Lomneth R., Martin T.F.J. and DasGupta B. R. (1991) J. Neurochem. 57: 1413-1421]. Two novel amino terminal fragments of the 150 kDa neurotoxin serotype E (approximately 112 and 48 kDa), produced by digestion(More)
Response of the chick ciliary ganglion-iris muscle neuromuscular junction (NMJ) preparation to the botulinum neurotoxin (NT) was investigated. The 150 kDa serotypes A and E NTs inhibited muscle contraction in a dose dependent fashion. Neurotoxicity of type E NT increased 20-40 fold after mild digestion with trypsin. The 50 kDA light and 100 kDa heavy chains(More)
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