Evidence map›Paper›PMID 15339253›Full record

ArticleThe Biochemical journal2004

Cytochrome c oxidase subunit IV as a marker of protein kinase Cepsilon function in neonatal cardiac myocytes: implications for cytochrome c oxidase activity.

Mourad Ogbi, Catherine S Chew, Jan Pohl, Olga Stuchlik, Safia Ogbi, John A Johnson

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

33 citing papers in PubMed, 60 citations in OpenAlex.

  1. Review
  2. CytochromeCells · 2021
    Review
  3. Review
  4. PKC and PKN in heart disease.Journal of molecular and cellular cardiology · 2019
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
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  13. Cardiac mitochondrial matrix and respiratory complex protein phosphorylation.American journal of physiology. Heart and circulatory physiology · 2012
    Review
  14. Review
  15. Article
  16. Article
  17. Review
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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

6 authors at 2 institutions in 1 country.

Mourad OgbiDepartment of Pharmacology and Toxicology, School of Medicine, Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, GA 30912-2300, USA.
Catherine S Chew
Jan Pohl
Olga Stuchlik
Safia Ogbi
John A Johnson
Augusta University · USEmory University · US

Funding

PHS HHS 02878PHS HHS 12878PHS HHS 13948
6 · The paper itself

Abstract

We have previously demonstrated that low concentrations of phorbol esters stimulate the selective translocation of protein kinase C (PKC) alpha and epsilon from the cell soluble to the particulate fraction in NCMs (neonatal rat cardiac myocytes). We therefore determined if the in vitro phosphorylation of substrates in these fractions could be used as assays of PKCalpha or epsilon activation. Intact cell phorbol ester treatment caused a decline in the in vitro (32)P-incorporation into several proteins in the cell-soluble fraction. These declines occurred in the presence or absence of in vitro Ca(2+) and probably reflected the exit of PKC isoenzymes from the soluble fraction. In contrast, an approx. 18 kDa protein incorporated (32)P in particulate fractions isolated from 4beta-PMA-treated cells in a Ca(2+)-independent manner. Proteomic and immunoprecipitation analyses indicated that the protein is subunit IV of the cytochrome c oxidase complex (COIV). In vitro phosphorylation of COIV was attenuated by PKC pseudosubstrate peptides. Introduction of an PKCepsilon-selective translocation inhibitor [Johnson, Gray, Chen and Mochly-Rosen (1996) J. Biol. Chem. 271, 24962-24966] into NCMs before 4beta-PMA treatments also attenuated the in vitro phosphorylation of COIV. In mitochondrial extracts from 4beta-PMA-treated NCMs, the PKCepsilon isoenzyme coimmunoprecipitated with COIV, and cytochrome c oxidase activity was enhanced 2-fold. The in vitro phosphorylation of COIV reflects a novel approach for monitoring PKCepsilon function in NCMs. Furthermore, PKCepsilon probably interacts with COIV in NCM mitochondria to enhance electron-transport chain complex IV activity.

Indexed as

AnimalsAnimals, NewbornCalciumElectron Transport Complex IVImmunoprecipitationIn Vitro TechniquesIsoenzymesMitochondria, HeartMyocytes, CardiacPhosphorylationProtein BindingProtein Kinase CProtein Kinase C-epsilonRatsRats, Sprague-DawleyTetradecanoylphorbol AcetateCalciumElectron Transport Complex IVIsoenzymesPrkce protein, ratProtein Kinase CProtein Kinase C-epsilonTetradecanoylphorbol Acetate

Identifiers

PMID15339253
PMCPMC1133968
OpenAlexW1991237970

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.