Evidence map›Paper›PMID 15030312›Full record

ArticleThe Biochemical journal2004

Mechanical stimuli regulate rapamycin-sensitive signalling by a phosphoinositide 3-kinase-, protein kinase B- and growth factor-independent mechanism.

Troy A Hornberger, Rudy Stuppard, Kevin E Conley, Mark J Fedele, Marta L Fiorotto, Eva R Chin, Karyn A Esser

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 102 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
102citing 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

102 citing papers in PubMed, 1 synthesis or guideline pooled it, 251 citations in OpenAlex.

  1. Pooled it
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  12. Strength Training in Swimming.International journal of environmental research and public health · 2022
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42 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

7 authors at 4 institutions in 1 country.

Troy A HornbergerSchool of Kinesiology, University of Illinois at Chicago, 901 W. Roosevelt, Chicago, IL 60608, USA.
Rudy Stuppard
Kevin E Conley
Mark J Fedele
Marta L Fiorotto
Eva R Chin
Karyn A Esser
Roosevelt University · USUniversity of Washington · USChildren's Nutrition Research Center at Baylor College of Medicine · USPfizer (United States) · US

Funding

SKELETAL MUSCLE HYPERTROPHY AND INTRACELLULAR SIGNALINGR01AR045617 · NIAMS · UNIVERSITY OF KENTUCKY · PI ESSER, KARYN A · 1999 to 2011
$2.9M
SKELETAL MUSCLE ENERGY METABOLISMR01AR036281 · NIAMS · UNIVERSITY OF WASHINGTON · PI KUSHMERICK, MARTIN J · 1986 to 2004
$2.5M
RESPIRATION AND GLYCOLYSIS--INTEGRATION IN ACTIVE MUSCLER01AR045184 · NIAMS · UNIVERSITY OF WASHINGTON · PI CONLEY, KEVIN E · 1998 to 2002
$872k
NIAMS NIH HHS AR36281NIAMS NIH HHS AR45184NIAMS NIH HHS AR45617PHS HHS T32 07692
6 · The paper itself

Abstract

In response to growth factors, mTOR (mammalian target of rapamycin) has been identified as a central component of the signalling pathways that control the translational machinery and cell growth. Signalling through mTOR has also been shown to be necessary for the mechanical load-induced growth of cardiac and skeletal muscles. Although the mechanisms involved for mechanically induced activation of mTOR are not known, it has been suggested that activation of PI3K (phosphoinositide 3-kinase) and protein kinase B (Akt), via the release of locally acting growth factors, underlies this process. In the present study, we show that mechanically stimulating (passive stretch) the skeletal muscle ex vivo results in the activation of mTOR-dependent signalling events. The activation of mTOR-dependent signalling events was necessary for an increase in translational efficiency, demonstrating the physiological significance of this pathway. Using pharmacological inhibitors, we show that activation of mTOR-dependent signalling occurs through a PI3K-independent pathway. Consistent with these results, mechanically induced signalling through mTOR was not disrupted in muscles from Akt1-/- mice. In addition, ex vivo co-incubation experiments, along with in vitro conditioned-media experiments, demonstrate that a mechanically induced release of locally acting autocrine/paracrine growth factors was not sufficient for the activation of the mTOR pathway. Taken together, our results demonstrate that mechanical stimuli can activate the mTOR pathway independent of PI3K/Akt1 and locally acting growth factors. Thus mechanical stimuli and growth factors provide distinct inputs through which mTOR co-ordinates an increase in the translational efficiency.

Indexed as

Physical StimulationAnimalsCell LineGrowth SubstancesMaleMiceMice, Inbred C57BLMice, TransgenicMuscle Fibers, SkeletalMuscle, SkeletalPeptide BiosynthesisPhosphatidylinositol 3-KinasesProtein BiosynthesisProtein KinasesProtein Serine-Threonine KinasesProto-Oncogene ProteinsGrowth SubstancesmTOR protein, mousePhosphatidylinositol 3-KinasesProtein KinasesProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSirolimusTOR Serine-Threonine Kinases

Identifiers

PMID15030312
PMCPMC1224227
OpenAlexW1972880994

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.