Evidence map›Paper›PMID 21289289›Full record

ArticleAmerican journal of physiology. Cell physiology2011

Full-length cardiac Na+/Ca2+ exchanger 1 protein is not phosphorylated by protein kinase A.

Pimthanya Wanichawan, William E Louch, Kristin H Hortemo, Bjørg Austbø, Per Kristian Lunde, John D Scott, Ole M Sejersted, Cathrine R Carlson

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2011. 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
2.1field-weighted citation impact, top 11% 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. Article
  2. Compartmentalized cAMP signalling and control of cardiac rhythm.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Palmitoylation of the Na/Ca exchanger cytoplasmic loop controls its inactivation and internalization during stress signaling.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. The Na+/Ca²+ exchanger in cardiac ischemia/reperfusion injury.Medical science monitor : international medical journal of experimental and clinical research · 2012
    Review
  12. Kinome profiling.Scientifica · 2012
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Pimthanya WanichawanInstitute for Experimental Medical Research, Oslo Univ. Hospital, Ullevaal, Oslo, Norway. pimthanya.wanichawan@medisin.uio.no
William E Louch
Kristin H Hortemo
Bjørg Austbø
Per Kristian Lunde
John D Scott
Ole M Sejersted
Cathrine R Carlson
Institutt for Eksperimentell Medisinsk Forskning · NOUniversity of Oslo · NOOslo University Hospital · NOUniversity of Washington · US

Funding

Anchored Kinase Signaling Mechanisms in Cardiac HypertrophyR01HL088366 · NHLBI · UNIVERSITY OF WASHINGTON · PI SCOTT, JOHN D · 2008 to 2012
$2.0M
NHLBI NIH HHS HL-088366NHLBI NIH HHS R01 HL088366
6 · The paper itself

Abstract

The cardiac Na(+)/Ca(2+) exchanger 1 (NCX1) is an important regulator of intracellular Ca(2+) homeostasis and cardiac function. Several studies have indicated that NCX1 is phosphorylated by the cAMP-dependent protein kinase A (PKA) in vitro, which increases its activity. However, this finding is controversial and no phosphorylation site has so far been identified. Using bioinformatic analysis and peptide arrays, we screened NCX1 for putative PKA phosphorylation sites. Although several NCX1 synthetic peptides were phosphorylated by PKA in vitro, only one PKA site (threonine 731) was identified after mutational analysis. To further examine whether NCX1 protein could be PKA phosphorylated, wild-type and alanine-substituted NCX1-green fluorescent protein (GFP)-fusion proteins expressed in human embryonic kidney (HEK)293 cells were generated. No phosphorylation of full-length or calpain- or caspase-3 digested NCX1-GFP was observed with purified PKA-C and [γ-(32)P]ATP. Immunoblotting experiments with anti-PKA substrate and phosphothreonine-specific antibodies were further performed to investigate phosphorylation of endogenous NCX1. Phospho-NCX1 levels were also not increased after forskolin or isoproterenol treatment in vivo, in isolated neonatal cardiomyocytes, or in total heart homogenate. These data indicate that the novel in vitro PKA phosphorylation site is inaccessible in full-length as well as in calpain- or caspase-3 digested NCX1 protein, suggesting that NCX1 is not a direct target for PKA phosphorylation.

Indexed as

Adrenergic beta-AgonistsAmino Acid SequenceAnimalsCells, CulturedColforsinComputational BiologyCyclic AMP-Dependent Protein KinasesHeartHEK293 CellsHumansIsoproterenolMiceMolecular Sequence DataMyocardiumPhosphorylationRatsAdrenergic beta-AgonistsColforsinCyclic AMP-Dependent Protein KinasesIsoproterenolSodium-Calcium Exchangersodium-calcium exchanger 1

Identifiers

PMID21289289
PMCPMC3093950
OpenAlexW2136670789

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.