Evidence map›Paper›PMID 20810907›Full record

ArticleAmerican journal of physiology. Cell physiology2010

A role for AMPK in increased insulin action after serum starvation.

James Kain Ching, Pooja Rajguru, Nandhini Marupudi, Sankha Banerjee, Jonathan S Fisher

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

31 citing papers in PubMed, 47 citations in OpenAlex.

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  10. Intermittent Starvation Extends the Functional Lifetime of Primary Human Hepatocyte Cultures.Toxicological sciences : an official journal of the Society of Toxicology · 2020
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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

5 authors at 1 institution in 1 country.

James Kain ChingDepartment of Biology, Saint Louis University, St. Louis, Missouri 63103, USA.
Pooja Rajguru
Nandhini Marupudi
Sankha Banerjee
Jonathan S Fisher
Saint Louis University · US

Funding

ARK5 AMP-activated protein kinase and glucose transportK01DK066330 · NIDDK · SAINT LOUIS UNIVERSITY · PI FISHER, JONATHAN S · 2004 to 2007
$373k
The role of ATM in glucose transport and insulin signaling in skeletal muscleR15DK080437 · NIDDK · SAINT LOUIS UNIVERSITY · PI FISHER, JONATHAN S. · 2008 to 2010
$359k
NIDDK NIH HHS K01 DK066330NIDDK NIH HHS R15 DK080437NIDDK NIH HHS R15 DK080437-01S2
6 · The paper itself

Abstract

Serum starvation is a common cell culture procedure for increasing cellular response to insulin, though the mechanism for the serum starvation effect is not understood. We hypothesized that factors known to potentiate insulin action [e.g., AMP-activated protein kinase (AMPK) and p38] or to be involved in insulin signaling leading to glucose transport [e.g., Akt, PKCζ, AS160, and ataxia telangiectasia mutated (ATM)] would be phosphorylated during serum starvation and would be responsible for increased insulin action after serum starvation. L6 myotubes were incubated in serum-containing or serum-free medium for 3 h. Levels of phosphorylated AMPK, Akt, and ATM were greater in serum-starved cells than in control cells. Serum starvation did not affect p38, PKCζ, or AS160 phosphorylation or insulin-stimulated Akt or AS160 phosphorylation. Insulin had no effect on glucose transport in control cells but caused an increase in glucose uptake for serum-starved cells that was preventable by compound C (an AMPK inhibitor), by expression of dominant negative AMPK (AMPK-DN), and by KU55933 (an ATM inhibitor). ATM protein levels increased during serum starvation, and this increase in ATM was prevented by compound C and AMPK-DN. Thus, it appears that AMPK is required for the serum starvation-related increase in insulin-stimulated glucose transport, with ATM as a possible downstream effector.

Indexed as

Cell Culture TechniquesAMP-Activated Protein KinasesAnimalsAtaxia Telangiectasia Mutated ProteinsBiological TransportCell Cycle ProteinsCell LineDNA-Binding ProteinsGlucoseInsulinIsoenzymesMiceMice, KnockoutMuscle Fibers, SkeletalProtein Serine-Threonine KinasesPyrazolesAMP-Activated Protein KinasesAtaxia Telangiectasia Mutated ProteinsAtm protein, mouseCell Cycle ProteinsDNA-Binding ProteinsdorsomorphinGlucoseInsulinIsoenzymesProtein Serine-Threonine KinasesPyrazolesPyrimidinesTumor Suppressor Proteins

Identifiers

PMID20810907
PMCPMC2980310
OpenAlexW2098233925

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.