Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus.

Journal article

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 ...

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Authors: Bon, C; Greenfield, S

• Publication status: Published
• Journal: European journal of neuroscience
• Volume: 17
• Issue: 9
• Pages: 1991-1995
• Publication date: 2003-05-01
• DOI: 10.1046/j.1460-9568.2003.02648.x
• EISSN: 1460-9568
• ISSN: 0953-816X
• Language: English
• Keywords: Hippocampus; Acetylcholinesterase; Membrane Potentials; Peptide Fragments; Guinea Pigs; Action Potentials; Male; Electrophysiology; Animals; N-Methylaspartate