Evidence map›Paper›PMID 16055943›Full record

ArticleJournal of molecular neuroscience : MN2005

Inhibition of neuronal nicotinic acetylcholine receptor channels expressed in Xenopus oocytes by beta-amyloid1-42 peptide.

Patricia W Lamb, Mark A Melton, Jerrel L Yakel

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of molecular neuroscience : MN, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.4field-weighted citation impact, top 21% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Amyloid Beta Peptide (AβJournal of clinical medicine · 2020
    Article
  8. Review
  9. Tetrapeptide Ac-HAEE-NHInternational journal of molecular sciences · 2020
    Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Review
  17. Review
  18. A novel nicotinic mechanism underlies β-amyloid-induced neuronal hyperexcitation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Patricia W LambLaboratory of Neurobiology, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, Research Triangle Park, NC 27709 <f.
Mark A Melton
Jerrel L Yakel
National Institute of Environmental Health Sciences · USNational Institutes of Health · US

Funding

Modulation Of Neuronal Channels and Receptors in the BrainZIAES090089 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI YAKEL, JERREL L · 2009 to 2025
$42.2M
MODULATION OF NEURONAL LIGAND-GATED CHANNELS BY CALCIUM DEPENDENT MECHANISMSZ01ES090089 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI YAKEL, JERREL L · 1997 to 2008
$3.6M
6 · The paper itself

Abstract

Neuronal nicotinic acetylcholine receptors (nAChRs) are involved in a variety of physiological processes, including cognition and development. Dysfunctions in nAChRs have been linked to Alzheimer's disease (AD), a human neurological disorder that is the leading cause of dementia. AD is characterized by an increasing loss of cognitive function, nAChRs, cholinergic neurons, and choline acetyltransferase activity. A major hallmark of AD is the presence of extracellular neuritic plaques composed of the beta-amyloid (Abeta1-42) peptide; however, the link between Abeta1-42 and the loss of cognitive function has not been established. Many groups have shown direct interactions between Abeta1-42 and nAChR function, however, with differing results. For example, in rat hippocampal CA1 interneurons in slices, we found that Abeta1-42 inhibits nAChR channels directly, and non-alpha7 receptors were more sensitive to block than alpha7 receptors. However, some groups have found that alpha7 subtypes were potently blocked by Abeta1-42, whereas other groups reported that Abeta1-42 can activate nAChRs (i.e., both alpha7 and non-alpha7 subtypes). To further investigate the link between nAChR function and Abeta1-42, we expressed various subtypes of nAChRs in Xenopus oocytes (e.g., alpha4beta2, alpha2beta2, alpha4alpha5beta2, and alpha7) and found that Abeta1-42 blocked these various non-alpha7 nAChRs, without any effect on alpha7 nAChRs. Furthermore, none of these channels was activated by Abeta1-42. The relative block by Abeta1-42 was dependent on the subunit makeup and apparent stoichiometry of these receptors. These data further support our previous findings that Abeta1-42 directly and preferentially inhibits non-alpha7 nAChRs.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAnimalsHumansNeuronsOocytesPatch-Clamp TechniquesPeptide FragmentsProtein IsoformsProtein SubunitsRatsReceptors, NicotinicXenopus laevisAmyloid beta-Peptidesamyloid beta-protein (1-42)Peptide FragmentsProtein IsoformsProtein SubunitsReceptors, Nicotinic

Identifiers

PMID16055943
OpenAlexW2059300571

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.