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Light chain of tetanus toxin intracellularly inhibits acetylcholine release at neuro‐neuronal synapses, and its internalization is mediated by heavy chain
Author(s) -
Mochida Sumiko,
Poulain Bernard,
Weller Ulrich,
Habermann Ernst,
Tauc Ladislav
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80926-3
Subject(s) - acetylcholine , internalization , chemistry , aplysia , toxin , intracellular , acetylcholine receptor , biophysics , biochemistry , receptor , pharmacology , biology , neuroscience
The ability of the two‐chain form of tetanus toxin (TeTx), its constituent light (LC) or heavy (HC) chains, and papain fragment to block evoked acetylcholine (ACh) release in the buccal ganglia of Aplysia californica was studied electrophysiologically. Extracellularly applied, TeTx or its B fragment (consisting of LC and β 2 , the amino‐terminal portion of HC) blocked ACh release, whereas LC, HC, or the β 2 fragment did not affect it. Toxicity was restored when LC was bath applied together with HC or the β 2 fragment. When injected into the presynaptic neuron, TeTx, the B fragment or LC, but not HC, induced inhibition of ACh release. These results indicate that the blockade of ACh release by TeTx is mimicked by intracellular action of LC, the internalization of which is mediated by the HC via its amino‐terminal moiety.