Evidence map›Paper›PMID 25617592›Full record

ArticleFree radical biology & medicine2015

The lipid peroxidation product 4-hydroxy-trans-2-nonenal causes protein synthesis in cardiac myocytes via activated mTORC1-p70S6K-RPS6 signaling.

Timothy D Calamaras, Charlie Lee, Fan Lan, Yasuo Ido, Deborah A Siwik, Wilson S Colucci

Abstract read
In one paragraph

Article in Free radical biology & medicine, 2015. 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
3.8field-weighted citation impact, top 6% 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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  14. Mixed lineage kinase-3 prevents cardiac dysfunction and structural remodeling with pressure overload.American journal of physiology. Heart and circulatory physiology · 2019
    Article
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  16. Review
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  19. 4-hydroxynonenal-mediated signaling and aging.Free radical biology & medicine · 2017
    Review
  20. Review
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 3 institutions in 2 countries.

Timothy D CalamarasMyocardial Biology Unit, Cardiovascular Medicine, and Diabetes and Metabolism Research Unit, Section of Endocrinology, Department of Medicine, Boston University School of Medicine, Boston, MA 02118, USA.
Charlie LeeBrigham and Women׳s Hospital, Boston, MA 02115, USA.
Fan LanDepartment of Endocrinology, Second Affiliated Hospital Chongqing Medical University, Chongqing, China.
Yasuo IdoDiabetes and Metabolism Research Unit, Section of Endocrinology, Department of Medicine, Boston University School of Medicine, Boston, MA 02118, USA.
Deborah A SiwikMyocardial Biology Unit, Cardiovascular Medicine, and Diabetes and Metabolism Research Unit, Section of Endocrinology, Department of Medicine, Boston University School of Medicine, Boston, MA 02118, USA.
Wilson S ColucciMyocardial Biology Unit, Cardiovascular Medicine, and Diabetes and Metabolism Research Unit, Section of Endocrinology, Department of Medicine, Boston University School of Medicine, Boston, MA 02118, USA. Electronic address: Wilson.colucci@bmc.org.
Boston University · USBrigham and Women's Hospital · USChongqing Medical University · CN

Funding

Oxidative Stress in Myocardial Remodeling and FailureR01HL064750 · NHLBI · BOSTON MEDICAL CENTER · PI COLUCCI, WILSON S. · 2001 to 2018
$5.0M
Training Program in Cardiovascular Biology: Pre-DoctoralT32HL007969 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI RAVID, KATYA · 2003 to 2019
$3.2M
NO &02-IN POSTMYOCARDIAL INFARCTION REMODELING &FAR01HL061639 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COLUCCI, WILSON S. · 1998 to 2007
$2.8M
NHLBI PROTEOMICS INITIATIVE-N01HV28178N01HV028178 · HV · BOSTON UNIVERSITY MEDICAL CAMPUS · PI COSTELLO, CATHERINE E. · 2002 to 2006
–
STRUCTURAL CHARACTERIZATION OF THE APOPROTEIN E RECEPTORR01HL028178 · NHLBI · J. DAVID GLADSTONE INSTITUTES · PI INNERARITY, THOMAS L. · 1986 to 1988
–
NHLBI NIH HHS HL-007969NHLBI NIH HHS HL-061639NHLBI NIH HHS N01 HV028178NHLBI NIH HHS N01-HV-28178NHLBI NIH HHS R01 HL061639NHLBI NIH HHS R01 HL064750NHLBI NIH HHS T32 HL007969
6 · The paper itself

Abstract

Reactive oxygen species (ROS) are elevated in the heart in response to hemodynamic and metabolic stress and promote hypertrophic signaling. ROS also mediate the formation of lipid peroxidation-derived aldehydes that may promote myocardial hypertrophy. One lipid peroxidation by-product, 4-hydroxy-trans-2-nonenal (HNE), is a reactive aldehyde that covalently modifies proteins thereby altering their function. HNE adducts directly inhibit the activity of LKB1, a serine/threonine kinase involved in regulating cellular growth in part through its interaction with the AMP-activated protein kinase (AMPK), but whether this drives myocardial growth is unclear. We tested the hypothesis that HNE promotes myocardial protein synthesis and if this effect is associated with impaired LKB1-AMPK signaling. In adult rat ventricular cardiomyocytes, exposure to HNE (10 μM for 1h) caused HNE-LKB1 adduct formation and inhibited LKB1 activity. HNE inhibited the downstream kinase AMPK, increased hypertrophic mTOR-p70S6K-RPS6 signaling, and stimulated protein synthesis by 27.1 ± 3.5%. HNE also stimulated Erk1/2 signaling, which contributed to RPS6 activation but was not required for HNE-stimulated protein synthesis. HNE-stimulated RPS6 phosphorylation was completely blocked using the mTOR inhibitor rapamycin. To evaluate if LKB1 inhibition by itself could promote the hypertrophic signaling changes observed with HNE, LKB1 was depleted in adult rat ventricular myocytes using siRNA. LKB1 knockdown did not replicate the effect of HNE on hypertrophic signaling or affect HNE-stimulated RPS6 phosphorylation. Thus, in adult cardiac myocytes HNE stimulates protein synthesis by activation of mTORC1-p70S6K-RPS6 signaling most likely mediated by direct inhibition of AMPK. Because HNE in the myocardium is commonly increased by stimuli that cause pathologic hypertrophy, these findings suggest that therapies that prevent activation of mTORC1-p70S6K-RPS6 signaling may be of therapeutic value.

Indexed as

AldehydesAMP-Activated Protein KinasesAnimalsCells, CulturedEnzyme ActivationExtracellular Signal-Regulated MAP KinasesHypertrophy, Left VentricularLipid PeroxidationMaleMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesMyocardiumMyocytes, CardiacPhosphorylationProtein BiosynthesisProtein Serine-Threonine Kinases2-nonenal4-hydroxy-2-nonenalAldehydesAMP-Activated Protein KinasesExtracellular Signal-Regulated MAP KinasesMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesProtein Serine-Threonine KinasesReactive Oxygen SpeciesRibosomal Protein S6Ribosomal Protein S6 Kinases, 70-kDaribosomal protein S6, mouseRNA, Small InterferingSirolimusStk11 protein, mouseTOR Serine-Threonine Kinases4-HNECardiac myocytesErk1/2Free radicalsmTORC1Protein synthesis

Identifiers

PMID25617592
PMCPMC4387097
OpenAlexW1971152541

What OpenQuestion holds

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Registered trials

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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.