Evidence map›Paper›PMID 23500391›Full record

ArticleJournal of molecular and cellular cardiology2013

Impaired translocation and activation of mitochondrial Akt1 mitigated mitochondrial oxidative phosphorylation Complex V activity in diabetic myocardium.

Jia-Ying Yang, Wu Deng, Yumay Chen, Weiwei Fan, Kenneth M Baldwin, Richard S Jope, Douglas C Wallace, Ping H Wang

Abstract read
In one paragraph

Article in Journal of molecular and cellular cardiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

23 citing papers in PubMed, 42 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Jia-Ying YangCenter for Diabetes Research and Treatment, University of California, Irvine, CA 92697, USA.
Wu Deng
Yumay Chen
Weiwei Fan
Kenneth M Baldwin
Richard S Jope
Douglas C Wallace
Ping H Wang
University of California, Irvine · USUniversity of Miami · US

Funding

MITOCHONDRIAL INBORN ERRORS OF METABOLISMR01NS021328 · NINDS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WALLACE, DOUGLAS C · 1985 to 2017
$6.5M
LITHIUM EFFECTS ON CHOLINERGIC ACTIVITYR01MH038752 · NIMH · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI JOPE, RICHARD S. · 1985 to 2015
$4.4M
Mitochondrial Diabetes & Manganic Porphyrin TreatmentR01DK073691 · NIDDK · UNIVERSITY OF CALIFORNIA-IRVINE · PI WALLACE, DOUGLAS C · 2006 to 2010
$1.5M
Insulin's Control of Myocardial Mitochondria Bioenergetics and BiogenesisR01HL096987 · NHLBI · UNIVERSITY OF CALIFORNIA-IRVINE · PI WANG, PING H · 2010 to 2013
$1.5M
NHLBI NIH HHS R01 HL096987NHLBI NIH HHS R01HL096987NIDDK NIH HHS DK73691NIDDK NIH HHS R01 DK073691NIMH NIH HHS R01 MH038752NIMH NIH HHS R01MH038752NINDS NIH HHS R01 NS021328
6 · The paper itself

Abstract

Insulin can translocate Akt to mitochondria in cardiac muscle. The goals of this study were to define sub-mitochondrial localization of the translocated Akt, to dissect the effects of insulin on Akt isoform translocation, and to determine the direct effect of mitochondrial Akt activation on Complex V activity in normal and diabetic myocardium. The translocated Akt sequentially localized to the mitochondrial intermembrane space, inner membrane, and matrix. To confirm Akt translocation, in vitro import assay showed rapid entry of Akt into mitochondria. Akt isoforms were differentially regulated by insulin stimulation, only Akt1 translocated into mitochondria. In the insulin-resistant Type 2 diabetes model, Akt1 translocation was blunted. Mitochondrial activation of Akt1 increased Complex V activity by 24% in normal myocardium in vivo and restored Complex V activity in diabetic myocardium. Basal mitochondrial Complex V activity was lower by 22% in the Akt1(-/-) myocardium. Insulin-stimulated Complex V activity was not impaired in the Akt1(-/-) myocardium, due to compensatory translocation of Akt2 to mitochondria. Akt1 is the primary isoform that relayed insulin signaling to mitochondria and modulated mitochondrial Complex V activity. Activation of mitochondrial Akt1 enhanced ATP production and increased phosphocreatine in cardiac muscle cells. Dysregulation of this signal pathway might impair mitochondrial bioenergetics in diabetic myocardium.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAnimalsCalciumCarrier ProteinsDiabetes Mellitus, Type 2InsulinIn Vitro TechniquesMass SpectrometryMembrane ProteinsMiceMitochondriaMitochondrial Proton-Translocating ATPasesMyocardiumOxidative PhosphorylationPhosphocreatineAdenosine TriphosphatasesAdenosine TriphosphateCalciumCarrier ProteinsInsulinMembrane ProteinsMitochondrial Proton-Translocating ATPasesoligomycin sensitivity-conferring proteinPhosphocreatineProto-Oncogene Proteins c-akt

Identifiers

PMID23500391
PMCPMC3872535
OpenAlexW2027107711

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.