Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus.
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...
| Main Authors: | , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
2003
|
| _version_ | 1797063966253383680 |
|---|---|
| author | Bon, C Greenfield, S |
| author_facet | Bon, C Greenfield, S |
| author_sort | Bon, C |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T21:07:32Z |
| format | Journal article |
| id | oxford-uuid:3cfc62a2-340f-4e1d-b9ec-e7ac912ddba4 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:07:32Z |
| publishDate | 2003 |
| record_format | dspace |
| spelling | oxford-uuid:3cfc62a2-340f-4e1d-b9ec-e7ac912ddba42022-03-26T14:16:49ZBioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:3cfc62a2-340f-4e1d-b9ec-e7ac912ddba4EnglishSymplectic Elements at Oxford2003Bon, CGreenfield, SAcetylcholinesterase 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. |
| spellingShingle | Bon, C Greenfield, S Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus. |
| title | Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus. |
| title_full | Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus. |
| title_fullStr | Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus. |
| title_full_unstemmed | Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus. |
| title_short | Bioactivity of a peptide derived from acetylcholinesterase: electrophysiological characterization in guinea-pig hippocampus. |
| title_sort | bioactivity of a peptide derived from acetylcholinesterase electrophysiological characterization in guinea pig hippocampus |
| work_keys_str_mv | AT bonc bioactivityofapeptidederivedfromacetylcholinesteraseelectrophysiologicalcharacterizationinguineapighippocampus AT greenfields bioactivityofapeptidederivedfromacetylcholinesteraseelectrophysiologicalcharacterizationinguineapighippocampus |