β-amyloid peptides inhibit acetylcholine release from cholinergic presynaptic nerve endings isolated from an electric ray
(2001) In Neuroscience Letters 302(2-3). p.97-100- Abstract
We investigated the effects of β-amyloid (Aβ) peptides on cholinergic synaptosomes isolated from the electric organ of the Japanese marine ray Narke japonica. Fresh and pre-incubated solutions of Aβ(1-42) inhibited acetylcholine (ACh) release from the synaptosomes evoked by high [K+] depolarization when incubated with synaptosomes for 10 min before the depolarizing stimulus. A freshly prepared solution of Aβ(1-40) did not inhibit the evoked ACh release, but prolonged pre-incubation of Aβ(1-40) solution caused the inhibition. Aβ(1-15) neither in fresh nor pre-incubated solution inhibited. These results have demonstrated that Aβ peptides can acutely inhibit the depolarization-evoked release of ACh by acting directly on... (More)
We investigated the effects of β-amyloid (Aβ) peptides on cholinergic synaptosomes isolated from the electric organ of the Japanese marine ray Narke japonica. Fresh and pre-incubated solutions of Aβ(1-42) inhibited acetylcholine (ACh) release from the synaptosomes evoked by high [K+] depolarization when incubated with synaptosomes for 10 min before the depolarizing stimulus. A freshly prepared solution of Aβ(1-40) did not inhibit the evoked ACh release, but prolonged pre-incubation of Aβ(1-40) solution caused the inhibition. Aβ(1-15) neither in fresh nor pre-incubated solution inhibited. These results have demonstrated that Aβ peptides can acutely inhibit the depolarization-evoked release of ACh by acting directly on cholinergic presynaptic nerve endings. The electrophoresis analysis showed a strong correlation between Aβ aggregation and its inhibition for ACh release.
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- author
- Satoh, Yasushi ; Hirakura, Yutaka ; Shibayama, Sotaro LU ; Hirashima, Naohide ; Suzuki, Toshiharu and Kirino, Yutaka
- publishing date
- 2001-04-20
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- β-Amyloid, aggregation, cholinergic neurons, electric organ, high [K] depolarization, nerve terminals, synaptosomes
- in
- Neuroscience Letters
- volume
- 302
- issue
- 2-3
- pages
- 4 pages
- publisher
- Elsevier
- external identifiers
-
- scopus:0035917827
- pmid:11290396
- ISSN
- 0304-3940
- DOI
- 10.1016/S0304-3940(01)01665-2
- language
- English
- LU publication?
- no
- id
- 8b2b02ad-4b10-44b2-84e3-8f9678f49c7b
- date added to LUP
- 2017-04-19 16:41:02
- date last changed
- 2024-02-29 13:12:18
@article{8b2b02ad-4b10-44b2-84e3-8f9678f49c7b,
abstract = {{<p>We investigated the effects of β-amyloid (Aβ) peptides on cholinergic synaptosomes isolated from the electric organ of the Japanese marine ray Narke japonica. Fresh and pre-incubated solutions of Aβ(1-42) inhibited acetylcholine (ACh) release from the synaptosomes evoked by high [K<sup>+</sup>] depolarization when incubated with synaptosomes for 10 min before the depolarizing stimulus. A freshly prepared solution of Aβ(1-40) did not inhibit the evoked ACh release, but prolonged pre-incubation of Aβ(1-40) solution caused the inhibition. Aβ(1-15) neither in fresh nor pre-incubated solution inhibited. These results have demonstrated that Aβ peptides can acutely inhibit the depolarization-evoked release of ACh by acting directly on cholinergic presynaptic nerve endings. The electrophoresis analysis showed a strong correlation between Aβ aggregation and its inhibition for ACh release.</p>}},
author = {{Satoh, Yasushi and Hirakura, Yutaka and Shibayama, Sotaro and Hirashima, Naohide and Suzuki, Toshiharu and Kirino, Yutaka}},
issn = {{0304-3940}},
keywords = {{β-Amyloid; aggregation; cholinergic neurons; electric organ; high [K] depolarization; nerve terminals; synaptosomes}},
language = {{eng}},
month = {{04}},
number = {{2-3}},
pages = {{97--100}},
publisher = {{Elsevier}},
series = {{Neuroscience Letters}},
title = {{β-amyloid peptides inhibit acetylcholine release from cholinergic presynaptic nerve endings isolated from an electric ray}},
url = {{http://dx.doi.org/10.1016/S0304-3940(01)01665-2}},
doi = {{10.1016/S0304-3940(01)01665-2}},
volume = {{302}},
year = {{2001}},
}