Evidence map›Paper›PMID 21653810›Full record

ArticleThe Journal of experimental biology2011

Physiological adaptation of an Antarctic Na+/K+-ATPase to the cold.

Gaddiel Galarza-Muñoz, Sonia I Soto-Morales, Miguel Holmgren, Joshua J C Rosenthal

Open access · greenAbstract read
In one paragraph

Article in The Journal of experimental biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.1field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  6. Molecular determinants for cold adaptation in an Antarctic NaProceedings of the National Academy of Sciences of the United States of America · 2023
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  9. Review
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  11. TRPs et al.: a molecular toolkit for thermosensory adaptations.Pflugers Archiv : European journal of physiology · 2018
    Review
  12. Review
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  14. Review
  15. Protein cold adaptation strategy via a unique seven-amino acid domain in the icefish (Chionodraco hamatus) PEPT1 transporter.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
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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.

Gaddiel Galarza-MuñozInstitute of Neurobiology, University of Puerto Rico-Medical Sciences Campus, San Juan, Puerto Rico.
Sonia I Soto-Morales
Miguel Holmgren
Joshua J C Rosenthal
University of Puerto Rico, Medical Sciences Campus · PRNational Institutes of Health · US

Funding

VIRUS E34 TAILSPIKE: MODULE FOR PROTEIN:LPS INTERACTIONP20RR016470 · NCRR · UNIVERSITY OF PUERTO RICO RIO PIEDRAS · PI PENA DE ORTIZ, SANDRA · 2001 to 2011
$31.2M
SUPPLEMENT FOR RENOVATION OF ANIMAL FACILITIES AT INSTITUTE OF NEUROBIOLOGYG12RR003051 · NCRR · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI ESPINO, ANA M · 1986 to 2011
$28.1M
Structure and Function of Membrane ProteinsZIANS002993 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI HOLMGREN, MIGUEL · 2009 to 2025
$24.0M
X-RAY STUDY OF SYNTHETIC OXYGEN CARRIERS RELATED TO BIOLOGICAL SYSTEMSS06GM008102 · NIGMS · UNIVERSITY OF PUERTO RICO RIO PIEDRAS · PI ARCE, RAFAEL · 1989 to 2008
$23.8M
SPECIALIZED PROGRAMS IN CELLULAR/ MOLECULAR NEUROBIOLOGYU54NS039405 · NINDS · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI FRONTERA, WALTER R. · 1999 to 2011
$12.9M
TRANSLATIONAL PROTEOMICS CENTERG12MD007600 · NIMHD · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI FERNANDEZ-REPOLLET, EMMA · 2012 to 2016
$11.0M
Regulation of the Na/K Pump by RNA EditingR01NS064259 · NINDS · UNIVERSITY OF PUERTO RICO MED SCIENCES · PI ROSENTHAL, JOSHUA J.C. · 2010 to 2014
$1.5M
Intramural NIH HHS ZIA NS002993NCRR NIH HHS G12 RR003051NCRR NIH HHS G12 RR 03051NCRR NIH HHS P20 RR016470NCRR NIH HHS P20 RR16470NIGMS NIH HHS S06 GM008102NIGMS NIH HHS S06GM08102NIMHD NIH HHS G12 MD007600NINDS NIH HHS 1R01NS64259NINDS NIH HHS 2 U54 NS039405-06NINDS NIH HHS R01 NS064259NINDS NIH HHS U54 NS039405
6 · The paper itself

Abstract

Because enzymatic activity is strongly suppressed by the cold, polar poikilotherms face significant adaptive challenges. For example, at 0°C the catalytic activity of a typical enzyme from a temperate organism is reduced by more than 90%. Enzymes embedded in the plasma membrane, such as the Na(+)/K(+)-ATPase, may be even more susceptible to the cold because of thermal effects on the lipid bilayer. Accordingly, adaptive changes in response to the cold may include adjustments to the enzyme or the surrounding lipid environment, or synergistic changes to both. To assess the contribution of the enzyme itself, we cloned orthologous Na(+)/K(+)-ATPase α-subunits from an Antarctic (Pareledone sp.; -1.8°C) and a temperate octopus (Octopus bimaculatus; ∼18°C), and compared their turnover rates and temperature sensitivities in a heterologous expression system. The primary sequences of the two pumps were found to be highly similar (97% identity), with most differences being conservative changes involving hydrophobic residues. The physiology of the pumps was studied using an electrophysiological approach in intact Xenopus oocytes. The voltage dependence of the pumps was equivalent. However, at room temperature the maximum turnover rate of the Antarctic pump was found to be 25% higher than that of the temperate pump. In addition, the Antarctic pump exhibited a lower temperature sensitivity, leading to significantly higher relative activity at lower temperatures. Orthologous Na(+)/K(+) pumps were then isolated from two tropical and two Arctic octopus. The temperature sensitivities of these pumps closely matched those of the temperate and Antarctic pumps, respectively. Thus, reduced thermal sensitivity appears to be a common mechanism driving cold adaptation in the Na(+)/K(+)-ATPase.

Indexed as

AcclimatizationAdaptation, PhysiologicalAmino Acid SequenceAnimalsAntarctic RegionsBinding SitesCell MembraneElectrophysiologyIonsLipid BilayersMolecular ConformationMolecular Sequence DataProtein IsoformsProtein Structure, TertiarySodium-Potassium-Exchanging ATPaseTemperatureIonsLipid BilayersProtein IsoformsSodium-Potassium-Exchanging ATPase

Identifiers

PMID21653810
PMCPMC3110501
OpenAlexW2077795867

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.