Evidence map›Paper›PMID 19841000›Full record

ArticleThe Journal of physiology2009

Redox modulation of global phosphatase activity and protein phosphorylation in intact skeletal muscle.

Valerie P Wright, Peter J Reiser, Thomas L Clanton

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.7field-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

48 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
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  13. Cardiac ischemia-reperfusion injury induces ROS-dependent loss of PKA regulatory subunit RIα.American journal of physiology. Heart and circulatory physiology · 2019
    Article
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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

3 authors at 3 institutions in 1 country.

Valerie P WrightUniversity of Florida, Department of Applied Physiology & Kinesiology, Room 100 FLG, PO Box 118205, Gainesville, FL 32611, USA.
Peter J Reiser
Thomas L Clanton
Florida College · USLung Institute · USThe Ohio State University · US

Funding

REDOX MECHANISMS OF RESPIRATORY MUSCLE STRESS ADAPTATIONR01HL053333 · NHLBI · UNIVERSITY OF FLORIDA · PI CLANTON, THOMAS LINDSAY · 1995 to 2009
$2.9M
NHLBI NIH HHS R01 HL053333
6 · The paper itself

Abstract

Skeletal muscles produce transient reactive oxygen species (ROS) in response to intense stimulation, disuse atrophy, heat stress, hypoxia, osmotic stress, stretch and cell receptor activation. The physiological significance is not well understood. Protein phosphatases (PPases) are known to be highly sensitive to oxidants and could contribute to many different signalling responses in muscle. We tested whether broad categories of PPases are inhibited by levels of acute oxidant exposure that do not result in loss of contractile function or gross oxidative stress. We also tested if this exposure results in elevated levels of global protein phosphorylation. Rat diaphragm muscles were treated with either 2,3-dimethoxy-1-naphthoquinone (DMNQ; 1, 10, 100 microm; a mitochondrial O(2)(.-)/H2O2 generator) or exogenous H2O2 (5, 50, 500 microm) for 30 min. Supernatants were assayed for serine/threonine PPase (Ser/Thr-PPase) or protein tyrosine PPase (PTP) activities. With the exception of 500 microm H2O2, no other oxidant exposures significantly elevated protein carbonyl formation, nor did they alter the magnitude of twitch force. DMNQ significantly decreased all categories of PPase activity at 10 and 100 microm and reduced PTP at 1 microm. Similar reductions in Ser/Thr-PPase activity were seen in response to 50 and 500 microm H2O2 and PTP at 500 microm H2O2. ROS treatments resulted a dose-dependent increase in the phosphorylation states of many proteins. The data are consistent with the concept that PPases, within intact skeletal muscles, are highly sensitive to acute changes in ROS activity and that localized ROS play a critical role in lowering the barriers for effective phosphorylation events to occur in muscle cells, thus increasing the probability for cell signalling responses to proceed.

Indexed as

AnimalsDose-Response Relationship, DrugHydrogen PeroxideIn Vitro TechniquesKineticsMaleMuscle ContractionMuscle ProteinsMuscle, SkeletalNaphthoquinonesOxidantsOxidation-ReductionOxidative StressPhosphoprotein PhosphatasesPhosphorylationProtein Carbonylation2,3-dimethoxy-1,4-naphthoquinoneHydrogen PeroxideMuscle ProteinsNaphthoquinonesOxidantsPhosphoprotein PhosphatasesProtein Tyrosine PhosphatasesReactive Oxygen Species

Identifiers

PMID19841000
PMCPMC2805384
OpenAlexW1546273936

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.