Evidence map›Paper›PMID 15047701›Full record

ArticleThe Journal of biological chemistry2004

Novel isoforms of the sodium channels Nav1.8 and Nav1.5 are produced by a conserved mechanism in mouse and rat.

Niall C H Kerr, Fiona E Holmes, David Wynick

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed, 54 citations in OpenAlex.

  1. Contribution of tetrodotoxin-resistant persistent NaThe journal of headache and pain · 2022
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  7. Review
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  9. Specialized functions of Nav1.5 and Nav1.9 channels in electrogenesis of myenteric neurons in intact mouse ganglia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  10. Article
  11. Early development of electrical excitability in the mouse enteric nervous system.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
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  12. Article
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  19. A novel Na+ channel splice form contributes to the regulation of an androgen-dependent social signal.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008
    Article
  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.

Niall C H KerrLaboratories for Integrated Neuroscience and Endocrinology (LINE), Dorothy Hodgkin Building, Whitson Street, Bristol BS1 3NY, United Kingdom.
Fiona E Holmes
David Wynick

Funding

Medical Research Council G0300028Medical Research Council G0300028(65120)
6 · The paper itself

Abstract

The voltage-gated sodium channel Na(v)1.8 is only expressed in subsets of neurons in dorsal root ganglia (DRG) and trigeminal and nodose ganglia. We have isolated mouse partial length Na(v)1.8 cDNA clones spanning the exon 17 sequence, which have 17 nucleotide substitutions and 12 predicted amino acid differences from the published sequence. The absence of a mutually exclusive alternative exon 17 was confirmed by sequencing 4.1 kilobases of genomic DNA spanning exons 16-18 of Scn10a. A novel cDNA isoform was identified, designated Na(v)1.8c, which results from alternative 3'-splice site selection at a CAG/CAG motif to exclude the codon for glutamine 1031 within the interdomain cytoplasmic loop IDII/III. The ratio of Na(v)1.8c (CAG-skipped) to Na(v)1.8 (CAG-inclusive) mRNA in mouse is approximately 2:1 in adult DRG, trigeminal ganglion, and neonatal DRG. A Na(v)1.8c isoform also occurs in rat DRG, but is less common. Of the two other tetrodotoxin-resistant channels, no analogous alternative splicing of mouse Na(v)1.9 was detected, whereas rare alternative splicing of Na(v)1.5 at a CAG/CAG motif resulted in the introduction of a CAG trinucleotide. This isoform, designated Na(v)1.5c, is conserved in rat and encodes an additional glutamine residue that disrupts a putative CK2 phosphorylation site. In summary, novel isoforms of Na(v)1.8 and Na(v)1.5 are each generated by alternative splicing at CAG/CAG motifs, which result in the absence or presence of predicted glutamine residues within the interdomain cytoplasmic loop IDII/III. Mutations of sodium channels within this cytoplasmic loop have previously been demonstrated to alter electrophysiological properties and cause cardiac arrhythmias and epilepsy.

Indexed as

Alternative SplicingAmino Acid MotifsAmino Acid SequenceAnimalsBase SequenceCodonConserved SequenceCytoplasmDNA, ComplementaryExonsGlutamineHumansMaleMiceMolecular Sequence DataMuscle ProteinsCodonDNA, ComplementaryGlutamineMuscle ProteinsNAV1.5 Voltage-Gated Sodium ChannelNAV1.8 Voltage-Gated Sodium ChannelNerve Tissue ProteinsProtein IsoformsRNASCN10A protein, humanScn10a protein, mouseScn10a protein, ratSCN5A protein, humanScn5a protein, mouseScn5a protein, ratSodium Channels

Identifiers

PMID15047701
PMCPMC2726572
OpenAlexW1996767161

What OpenQuestion holds

Textmetadata
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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.