Evidence map›Paper›PMID 18682538›Full record

ArticleAmerican journal of physiology. Endocrinology and metabolism2008

Leucine stimulates protein synthesis in skeletal muscle of neonatal pigs by enhancing mTORC1 activation.

Agus Suryawan, Asumthia S Jeyapalan, Renan A Orellana, Fiona A Wilson, Hanh V Nguyen, Teresa A Davis

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Endocrinology and metabolism, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed, 1 pooled it
4.2field-weighted citation impact, top 5% 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

83 citing papers in PubMed, 1 synthesis or guideline pooled it, 169 citations in OpenAlex.

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  16. Metabolomic and lipidomic insights into the impact ofComputational and structural biotechnology journal · 2025
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23 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Agus SuryawanUnited States Department of Agriculture/Agriculture Research Service Children's Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, Texas 77030, USA.
Asumthia S Jeyapalan
Renan A Orellana
Fiona A Wilson
Hanh V Nguyen
Teresa A Davis
Baylor College of Medicine · US

Funding

Regulation of Neonatal Muscle Protein SynthesisR01AR044474 · NIAMS · BAYLOR COLLEGE OF MEDICINE · PI DAVIS, TERESA A · 1996 to 2012
$4.2M
NIAMS NIH HHS AR-44474NIAMS NIH HHS R01 AR044474
6 · The paper itself

Abstract

Skeletal muscle in the neonate grows at a rapid rate due in part to an enhanced sensitivity to the postprandial rise in amino acids, particularly leucine. To elucidate the molecular mechanism by which leucine stimulates protein synthesis in neonatal muscle, overnight-fasted 7-day-old piglets were treated with rapamycin [an inhibitor of mammalian target of rapamycin (mTOR) complex (mTORC)1] for 1 h and then infused with leucine for 1 h. Fractional rates of protein synthesis and activation of signaling components that lead to mRNA translation were determined in skeletal muscle. Rapamycin completely blocked leucine-induced muscle protein synthesis. Rapamycin markedly reduced raptor-mTOR association, an indicator of mTORC1 activation. Rapamycin blocked the leucine-induced phosphorylation of mTOR, S6 kinase 1 (S6K1), and eukaryotic initiation factor (eIF)4E-binding protein-1 (4E-BP1) and formation of the eIF4E.eIF4G complex and increased eIF4E.4E-BP1 complex abundance. Rapamycin had no effect on the association of mTOR with rictor, a crucial component for mTORC2 activation, or G protein beta-subunit-like protein (GbetaL), a component of mTORC1 and mTORC2. Neither leucine nor rapamycin affected the phosphorylation of AMP-activated protein kinase (AMPK), PKB, or tuberous sclerosis complex (TSC)2, signaling components that reside upstream of mTOR. Eukaryotic elongation factor (eEF)2 phosphorylation was not affected by leucine or rapamycin, although current dogma indicates that eEF2 phosphorylation is mTOR dependent. Together, these in vivo data suggest that leucine stimulates muscle protein synthesis in neonates by enhancing mTORC1 activation and its downstream effectors.

Indexed as

AMP-Activated Protein KinasesAnimalsAnimals, NewbornAntibiotics, AntineoplasticBlotting, WesternEukaryotic Initiation Factor-4EKineticsLeucineMultienzyme ComplexesMuscle ProteinsMuscle, SkeletalPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktSignal TransductionAMP-Activated Protein KinasesAntibiotics, AntineoplasticEukaryotic Initiation Factor-4ELeucineMultienzyme ComplexesMuscle ProteinsProtein KinasesProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktSirolimusTOR Serine-Threonine Kinases

Identifiers

PMID18682538
PMCPMC2575905
OpenAlexW2135302022

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.