Evidence map›Paper›PMID 24361238›Full record

ArticleJournal of molecular and cellular cardiology2014

p38α regulates SERCA2a function.

Leena Kaikkonen, Johanna Magga, Veli-Pekka Ronkainen, Elina Koivisto, Ábel Perjes, J Kurt Chuprun, Leif Erik Vinge, Teemu Kilpiö, Jani Aro, Johanna Ulvila and 6 more

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of molecular and cellular cardiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
  2. Article
  3. Circulation. Arrhythmia and electrophysiology · 2024
    Article
  4. Article
  5. p38 MAPK Pathway in the Heart: New Insights in Health and Disease.International journal of molecular sciences · 2020
    Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. 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

16 authors at 6 institutions in 5 countries.

Leena KaikkonenDept. of Pharmacology and Toxicology, Institute of Biomedicine, University of Oulu, P.O. BOX 5000, FI-90014 Oulu, Finland.
Johanna MaggaDept. of Pharmacology and Toxicology, Institute of Biomedicine, University of Oulu, P.O. BOX 5000, FI-90014 Oulu, Finland.
Veli-Pekka RonkainenBiocenter Oulu, University of Oulu, P.O. BOX 5000, FI-90014 Oulu, Finland.
Elina KoivistoDept. of Pharmacology and Toxicology, Institute of Biomedicine, University of Oulu, P.O. BOX 5000, FI-90014 Oulu, Finland.
Ábel PerjesDept. of Pharmacology and Toxicology, Institute of Biomedicine, University of Oulu, P.O. BOX 5000, FI-90014 Oulu, Finland.
J Kurt ChuprunTemple University School of Medicine, MERB 9th floor, 3500 N Broad St., Philadelphia, PA 19140, USA.
Leif Erik VingeResearch Institute of Internal Medicine, Sognsvannsveien 20, 0027 Oslo, Norway; Department of Cardiology, Oslo University Hospital Rikshospitalet, Sognsvannsveien 20, 0027 Oslo, Norway; Center for Heart Failure Research, University of Oslo, Norway.
Teemu KilpiöDept. of Pharmacology and Toxicology, Institute of Biomedicine, University of Oulu, P.O. BOX 5000, FI-90014 Oulu, Finland.
Jani AroDept. of Pharmacology and Toxicology, Institute of Biomedicine, University of Oulu, P.O. BOX 5000, FI-90014 Oulu, Finland.
Johanna UlvilaDept. of Pharmacology and Toxicology, Institute of Biomedicine, University of Oulu, P.O. BOX 5000, FI-90014 Oulu, Finland.
Tarja AlakoskiDept. of Pharmacology and Toxicology, Institute of Biomedicine, University of Oulu, P.O. BOX 5000, FI-90014 Oulu, Finland.
James A BibbDepartment of Psychiatry, University of Texas, Southwestern Medical Center, 5323 Harry Hines Boulevard, Dallas, TX 75390-9070, USA.
Istvan SzokodiHeart Institute, Medical School, University of Pécs, 13 Ifjúság St., 7624 Pécs Hungary.
Walter J KochTemple University School of Medicine, MERB 9th floor, 3500 N Broad St., Philadelphia, PA 19140, USA.
Heikki RuskoahoDept. of Pharmacology and Toxicology, Institute of Biomedicine, University of Oulu, P.O. BOX 5000, FI-90014 Oulu, Finland; Dept. of Pharmacology and Toxicology, Faculty of Pharmacy; University of Helsinki, Viikinkaari 9, FI-00014 Helsinki, Finland.
Risto KerkeläDept. of Pharmacology and Toxicology, Institute of Biomedicine, University of Oulu, P.O. BOX 5000, FI-90014 Oulu, Finland; Medical Research Center Oulu, Oulu University Hospital and University of Oulu, Finland. Electronic address: Risto.Kerkela@oulu.fi.
University of Oulu · FITemple University · USOulu University Hospital · FIThe University of Texas Southwestern Medical Center · USUniversity of Oslo · NOUniversity of Pecs · HU

Funding

The Role of Cdk5 in StrokeR01NS073855 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI BIBB, JAMES A · 2012 to 2017
$1.7M
The Regulation of Dopamine Neurotransmission by CDK5R01MH079710 · NIMH · UT SOUTHWESTERN MEDICAL CENTER · PI BIBB, JAMES A · 2008 to 2011
$1.7M
NMDA RECEPTOR REGULATION IN ADDICTIONR01DA033485 · NIDA · UT SOUTHWESTERN MEDICAL CENTER · PI BIBB, JAMES A · 2012 to 2016
$1.6M
NIDA NIH HHS R01 DA033485NIMH NIH HHS R01 MH079710NINDS NIH HHS R01 NS073855
6 · The paper itself

Abstract

cAMP-dependent protein kinase (PKA) regulates the L-type calcium channel, the ryanodine receptor, and phospholamban (PLB) thereby increasing inotropy. Cardiac contractility is also regulated by p38 MAPK, which is a negative regulator of cardiac contractile function. The aim of this study was to identify the mechanism mediating the positive inotropic effect of p38 inhibition. Isolated adult and neonatal cardiomyocytes and perfused rat hearts were utilized to investigate the molecular mechanisms regulated by p38. PLB phosphorylation was enhanced in cardiomyocytes by chemical p38 inhibition, by overexpression of dominant negative p38α and by p38α RNAi, but not with dominant negative p38β. Treatment of cardiomyocytes with dominant negative p38α significantly decreased Ca(2+)-transient decay time indicating enhanced sarco/endoplasmic reticulum Ca(2+)-ATPase function and increased cardiomyocyte contractility. Analysis of signaling mechanisms involved showed that inhibition of p38 decreased the activity of protein phosphatase 2A, which renders protein phosphatase inhibitor-1 phosphorylated and thereby inhibits PP1. In conclusion, inhibition of p38α enhances PLB phosphorylation and diastolic Ca(2+) uptake. Our findings provide evidence for novel mechanism regulating cardiac contractility upon p38 inhibition.

Indexed as

AnimalsCalciumCalcium-Binding ProteinsEnzyme ActivationMuscle ContractionMyocytes, Cardiacp38 Mitogen-Activated Protein KinasesPhospholambanPhosphorylationRatsRNA InterferenceSarcoplasmic Reticulum Calcium-Transporting ATPasesCalciumCalcium-Binding Proteinsp38 Mitogen-Activated Protein KinasesPhospholambanSarcoplasmic Reticulum Calcium-Transporting ATPasesadult mouse ventricular myocyteadult rat ventricular myocyteAMVMARVMCardiac contractilitydndominant negativeendothelin-1ET-1G protein coupled receptor kinaseGRKI-1inhibitor-1MAPKmitogen-activated protein kinaseneonatal rat ventricular myocyteNRVMOAokadaic acidp38phospholambanPhospholambanPLBPP1PP2Aprotein phosphatase-1protein phosphatase-2Asarco/endoplasmic reticulum Ca(2+) ATPaseSERCA2a

Identifiers

PMID24361238
PMCPMC4296568
OpenAlexW2018012883

What OpenQuestion holds

Textmetadata
LicenceTDM
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.