Evidence map›Paper›PMID 11956333›Full record

ArticleThe Journal of physiology2002

Rat nicotinic ACh receptor alpha7 and beta2 subunits co-assemble to form functional heteromeric nicotinic receptor channels.

Serguei S Khiroug, Patricia C Harkness, Patricia W Lamb, Sterling N Sudweeks, Leonard Khiroug, Neil S Millar, Jerrel L Yakel

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

74 citing papers in PubMed, 220 citations in OpenAlex.

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  8. Implications of Oligomeric Amyloid-Beta (oAβThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021
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14 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 2 countries.

Serguei S KhirougLaboratory of Signal Transduction, National Institute of Environmental Health Sciences, National Institutes of Health, PO Box 12233, Research Triangle Park, NC 27709, USA.
Patricia C Harkness
Patricia W Lamb
Sterling N Sudweeks
Leonard Khiroug
Neil S Millar
Jerrel L Yakel
National Institute of Environmental Health Sciences · USUniversity College London · GBNational Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rat hippocampal interneurons express diverse subtypes of functional nicotinic acetylcholine receptors (nAChRs), including alpha7-containing receptors that have properties unlike those expected for homomeric alpha7 nAChRs. We previously reported a strong correlation between expression of the alpha7 and of the beta2 subunits in individual neurons. To explore whether co-assembly of the alpha7 and beta2 subunits might occur, these subunits were co-expressed in Xenopus oocytes and the functional properties of heterologously expressed nAChRs were characterized by two-electrode voltage clamp. Co-expression of the beta2 subunit, both wild-type and mutant forms, with the alpha7 subunit significantly slowed the rate of nAChR desensitization and altered the pharmacological properties. Whereas ACh, carbachol and choline were full or near-full agonists for homomeric alpha7 receptor channels, both carbachol and choline were only partial agonists in oocytes expressing both alpha7 and beta2 subunits. In addition the EC(50) values for all three agonists significantly increased when the beta2 subunit was co-expressed with the alpha7 subunit. Co-expression with the beta2 subunit did not result in any significant change in the current-voltage curve. Biochemical evidence for the co-assembly of the alpha7 and beta2 subunits was obtained by co-immunoprecipitation of these subunits from transiently transfected human embryonic kidney (TSA201) cells. These data provide direct biophysical and molecular evidence that the nAChR alpha7 and beta2 subunits co-assemble to form a functional heteromeric nAChR with functional and pharmacological properties different from those of homomeric alpha7 channels. This co-assembly may help to explain nAChR channel diversity in rat hippocampal interneurons, and perhaps in other areas of the nervous system.

Indexed as

Acetylcholinealpha7 Nicotinic Acetylcholine ReceptorAnimalsCarbacholCholineDNA, ComplementaryElectric StimulationElectrophysiologyHumansKineticsMembrane PotentialsMuscarinic AgonistsOocytesPatch-Clamp TechniquesPrecipitin TestsRatsAcetylcholinealpha7 Nicotinic Acetylcholine ReceptorCarbacholCholineChrna7 protein, humanChrna7 protein, ratDNA, ComplementaryMuscarinic AgonistsReceptors, NicotinicRNA, Messenger

Identifiers

PMID11956333
PMCPMC2290261
OpenAlexW2079307058

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.