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Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea‐pig hippocampus
Author(s) -
Bon Christelle L. M.,
Greenfield Susan A.
Publication year - 2003
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1046/j.1460-9568.2003.02648.x
Subject(s) - acetylcholinesterase , peptide , acetylcholine , depolarization , chemistry , glycine , guinea pig , biochemistry , pharmacology , biophysics , neuroscience , biology , amino acid , endocrinology , enzyme
Acetylcholinesterase is well known to have noncholinergic functions. Only recently, however, has the salient part been identified of the molecule responsible for these nonclassical actions, a peptide of 14 amino acids towards the C‐terminus of acetylcholinesterase. The aim of this study was to test the bioactivity of this ‘acetylcholinesterase‐peptide’ using intracellular recordings in guinea‐pig hippocampal slices. In the presence of tetrodotoxin, acetylcholinesterase‐peptide alone affected neither the membrane potential nor the input resistance of CA1 neurons; however, a modulatory action was observed, as a concentration‐dependent decrease of N ‐methyl‐ d ‐aspartic acid‐induced depolarization. When calcium potentials were elicited by a depolarizing current pulse, application of acetylcholinesterase‐peptide increased or reduced the degree of calcium spike firing in, respectively, the presence or absence of the N ‐methyl‐ d ‐aspartic acid antagonist d (–)‐2‐amino‐5‐phosphonopentanoic acid. In contrast, a peptide derived from the equivalent region of butyrylcholinesterase, which also hydrolyses acetylcholine, had no effect. In conclusion, acetylcholinesterase‐peptide has a selective bioactivity in the hippocampus; it could thus offer new ways of targeting mechanisms of calcium‐induced neurotoxicity.