Evidence map›Paper›PMID 22696220›Full record

ArticleThe Journal of biological chemistry2012

Subunit isoform selectivity in assembly of Na,K-ATPase α-β heterodimers.

Elmira Tokhtaeva, Rebecca J Clifford, Jack H Kaplan, George Sachs, Olga Vagin

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
–field-weighted citation impact
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

36 citing papers in PubMed.

  1. Role of an Angiotensin II Type-1 Receptor (ATBiological trace element research · 2026
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  17. NaJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2017
    Article
  18. Review
  19. A SINE Insertion inG3 (Bethesda, Md.) · 2017
    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

5 authors.

Elmira TokhtaevaDepartment of Physiology, School of Medicine, UCLA and Veterans Affairs Greater Los Angeles Health Care System, Los Angeles, California 90073, USA.
Rebecca J Clifford
Jack H Kaplan
George Sachs
Olga Vagin

Funding

The Roles of Sodium Pump Beta Subunits in Mammalian CellsR01GM039500 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KAPLAN, JACK H · 1988 to 2010
$3.3M
THE GASTRIC ACID PUMP AS A TARGET FOR ULCER TREATMENTR01DK058333 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SACHS, GEORGE · 2000 to 2009
$2.6M
Role of Na, K-ATPase beta isoforms in pump sorting and epithelial integrityR01DK077149 · NIDDK · BRENTWOOD BIOMEDICAL RESEARCH INSTITUTE · PI VAGIN, OLGA · 2007 to 2010
$811k
The Gastric Acid Pump as a Target for Ulcer TreatmentR56DK058333 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SACHS, GEORGE · 2010 to 2010
$229k
NIDDK NIH HHS DK058333NIDDK NIH HHS DK077149NIDDK NIH HHS R01 DK058333NIDDK NIH HHS R01 DK077149NIDDK NIH HHS R56 DK058333NIGMS NIH HHS GM39500NIGMS NIH HHS R01 GM039500
6 · The paper itself

Abstract

To catalyze ion transport, the Na,K-ATPase must contain one α and one β subunit. When expressed by transfection in various expression systems, each of the four α subunit isoforms can assemble with each of the three β subunit isoforms and form an active enzyme, suggesting the absence of selective α-β isoform assembly. However, it is unknown whether in vivo conditions the α-β assembly is random or isoform-specific. The α(2)-β(2) complex was selectively immunoprecipitated by both anti-α(2) and anti-β(2) antibodies from extracts of mouse brain, which contains cells co-expressing multiple Na,K-ATPase isoforms. Neither α(1)-β(2) nor α(2)-β(1) complexes were detected in the immunoprecipitates. Furthermore, in MDCK cells co-expressing α(1), β(1), and β(2) isoforms, a greater fraction of the β(2) subunits was unassembled with α(1) as compared with that of the β(1) subunits, indicating preferential association of the α(1) isoform with the β(1) isoform. In addition, the α(1)-β(2) complex was less resistant to various detergents than the α(1)-β(1) complex isolated from MDCK cells or the α(2)-β(2) complex isolated from mouse brain. Therefore, the diversity of the α-β Na,K-ATPase heterodimers in vivo is determined not only by cell-specific co-expression of particular isoforms, but also by selective association of the α and β subunit isoforms.

Indexed as

Protein MultimerizationAnimalsBacterial ProteinsBinding, CompetitiveBrainCell MembraneCells, CulturedDogsEnzyme StabilityHumansImmunoprecipitationIsoenzymesKidneyLuminescent ProteinsMiceModels, MolecularBacterial ProteinsIsoenzymesLuminescent ProteinsRecombinant Fusion ProteinsSodium-Potassium-Exchanging ATPaseyellow fluorescent protein, Bacteria

Identifiers

PMID22696220
PMCPMC3406695

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Registered trials

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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.