Evidence map›Paper›PMID 9801359›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1998

Na,K-ATPase subunit beta1 knock-in prevents lethality of beta2 deficiency in mice.

P Weber, U Bartsch, M Schachner, D Montag

Open access · greenAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
5.1field-weighted citation impact, top 5% 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

12 citing papers in PubMed, 31 citations in OpenAlex.

  1. Connecting the Dots: AMOG/βInternational journal of molecular sciences · 2025
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  2. Cells · 2025
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  11. Mouse Na+/K+-ATPase beta1-subunit has a K+-dependent cell adhesion activity for beta-GlcNAc-terminating glycans.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  12. Cellular and subcellular specification of Na,K-ATPase alpha and beta isoforms in the postnatal development of mouse retina.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999
    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

4 authors at 2 institutions in 2 countries.

P WeberDepartment of Neurobiology, Swiss Federal Institute of Technology, CH-8093 Zürich, Switzerland.
U Bartsch
M Schachner
D Montag
École Polytechnique Fédérale de Lausanne · CHLeibniz Institute for Neurobiology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The beta2 subunit of the Na,K-ATPase displays functional properties of both an integral constituent of an ion pump and an adhesion and neurite outgrowth-promoting molecule in vitro. To investigate whether the beta1 subunit of the Na,K-ATPase can functionally substitute for the beta2 isoform in vivo, we have generated beta2/beta1 knock-in mice by homologous recombination in embryonic stem cells. In beta2/beta1 knock-in mice, expression of beta2 was abolished, whereas beta1 mRNA expression from the mutated gene amounted to approximately 15% of the normal expression of beta2 in the adult mouse brain and prevented the juvenile lethality observed for beta2 null mutant mice. In contrast to beta2 null mutant mice, the overall morphological structure of all analyzed brain regions was normal. By immunohistochemical analysis, beta1 expression was detected in photoreceptor cells in the retina of knock-in mice at an age when expression of beta1 and beta2, respectively, is downregulated and persisting in the wild-type mice. Morphological analysis by light and electron microscopy revealed a progressive degeneration of photoreceptor cells. Apoptotic death of photoreceptor cells determined quantitatively by terminal deoxynucleotidyl transferase-mediated dUTP nick end labeling analysis increased in beta2/beta1 knock-in mice with age. These observations suggest that the beta1 subunit of the Na,K-ATPase can substitute sufficiently, at least in certain cell types, for the role of the beta2 subunit as a component of a functional Na,K-ATPase, but they do not allow us to determine the possible role of the beta2 subunit as an adhesion molecule in vivo.

Indexed as

Amino Acid SequenceAnimalsApoptosisCell Adhesion MoleculesHomeostasisImmunohistochemistryIn Situ Nick-End LabelingMiceMice, Mutant StrainsMicroscopy, ElectronMolecular Sequence DataMutagenesisNeurogliaPhenotypePhotoreceptor Cells, VertebrateRetinitis PigmentosaCell Adhesion MoleculesSodium-Potassium-Exchanging ATPase

Identifiers

PMID9801359
PMCPMC6792892
OpenAlexW2122485157

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.