Evidence map›Paper›PMID 31114002›Full record

ArticleScientific reports2019

Role of Bcl2-associated Athanogene 3 in Turnover of Gap Junction Protein, Connexin 43, in Neonatal Cardiomyocytes.

Farzaneh Ghasemi Tahrir, Manish Gupta, Valerie Myers, Jennifer Gordon, Joseph Y Cheung, Arthur M Feldman, Kamel Khalili

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

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. MicroRNA regulation of BAG3.Experimental biology and medicine (Maywood, N.J.) · 2022
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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

7 authors at 1 institution in 1 country.

Farzaneh Ghasemi TahrirDepartment of Neuroscience, Center for Neurovirology, Lewis Katz School of Medicine at Temple University, Philadelphia, Pennsylvania, USA.
Manish GuptaDepartment of Neuroscience, Center for Neurovirology, Lewis Katz School of Medicine at Temple University, Philadelphia, Pennsylvania, USA.
Valerie MyersDepartment of Medicine, Lewis Katz School of Medicine at Temple University, Philadelphia, Pennsylvania, USA.
Jennifer GordonDepartment of Neuroscience, Center for Neurovirology, Lewis Katz School of Medicine at Temple University, Philadelphia, Pennsylvania, USA.
Joseph Y CheungDepartment of Medicine, Lewis Katz School of Medicine at Temple University, Philadelphia, Pennsylvania, USA.
Arthur M FeldmanDepartment of Medicine, Lewis Katz School of Medicine at Temple University, Philadelphia, Pennsylvania, USA.
Kamel KhaliliDepartment of Neuroscience, Center for Neurovirology, Lewis Katz School of Medicine at Temple University, Philadelphia, Pennsylvania, USA. kamel.khalili@temple.edu.
Temple University · US

Funding

Viral Gene Editing and Bioinformatics Core for Institution # 269291P30MH092177 · NIMH · TEMPLE UNIV OF THE COMMONWEALTH · PI SHOHREH AMINI · 2011 to 2026
$24.9M
Involvement of BAG3 in HIV-1 induced cardiomyopathyR01HL123093 · NHLBI · TEMPLE UNIV OF THE COMMONWEALTH · PI CHEUNG, JOSEPH Y, FELDMAN, ARTHUR M · 2014 to 2018
$3.7M
NHLBI NIH HHS R01 HL123093NIMH NIH HHS P30 MH092177
6 · The paper itself

Abstract

Any pathological stress that impairs expression, turnover and phosphorylation of connexin 43 (Cx43), one of the major proteins of gap junctions, can adversely impact myocardial cell behavior, thus leading to the development of cardiac arrhythmias and heart failure. Our results in primary neonatal rat ventricular cardiomyocytes (NRVCs) show that impairment of the autophagy-lysosome pathway dysregulates degradation of Cx43, either by inhibiting lysosomal activity or suppressing the level of Bcl2-associated athanogene 3 (BAG3), a stress-induced pleiotropic protein that is involved in protein quality control (PQC) via the autophagy pathway. Inhibition of lysosomal activity leads to the accumulation of Cx43 aggregates and suppression of BAG3 significantly diminished turnover of Cx43. In addition, knock-down of BAG3 reduced the levels of Cx43 by dysregulating Cx43 protein stability. Under stress conditions, expression of BAG3 affected the state of Cx43 phosphorylation and its degradation. Furthermore, we found that BAG3 co-localized with the cytoskeleton protein, α-Tubulin, and depolymerization of α-Tubulin led to the intracellular accumulation of Cx43. These observations ascribe a novel function for BAG3 that involves control of Cx43 turnover under normal and stress conditions and potentially for optimizing communication of cardiac muscle cells through gap junctions.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsApoptosis Regulatory ProteinsCells, CulturedConnexin 43LysosomesMyocytes, CardiacPhosphorylationProtein MultimerizationProtein StabilityProteolysisRatsRats, Sprague-DawleyTubulinAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsBAG3 protein, ratConnexin 43Gja1 protein, ratTubulin

Identifiers

PMID31114002
PMCPMC6529437
OpenAlexW2946691232

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.