Document Detail


Local hindlimb antioxidant infusion does not affect muscle glucose uptake during in situ contractions in rat.
MedLine Citation:
PMID:  20203065     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
There is evidence that reactive oxygen species (ROS) contribute to the regulation of skeletal muscle glucose uptake during highly fatiguing ex vivo contraction conditions via AMP-activated protein kinase (AMPK). In this study we investigated the role of ROS in the regulation of glucose uptake and AMPK signaling during low-moderate intensity in situ hindlimb muscle contractions in rats, which is a more physiological protocol and preparation. Male hooded Wistar rats were anesthetized, and then N-acetylcysteine (NAC) was infused into the epigastric artery (125 mg.kg(-1).h(-1)) of one hindlimb (contracted leg) for 15 min before this leg was electrically stimulated (0.1-ms impulse at 2 Hz and 35 V) to contract at a low-moderate intensity for 15 min. The contralateral leg did not receive stimulation or local NAC infusion (rest leg). NAC infusion increased (P<0.05) plasma cysteine and cystine (by approximately 360- and 1.4-fold, respectively) and muscle cysteine (by 1.5-fold, P=0.001). Although contraction did not significantly alter muscle tyrosine nitration, reduced (GSH) or oxidized glutathione (GSSG) content, S-glutathionylation of protein bands at approximately 250 and 150 kDa was increased (P<0.05) approximately 1.7-fold by contraction, and this increase was prevented by NAC. Contraction increased (P<0.05) skeletal muscle glucose uptake 20-fold, AMPK phosphorylation 6-fold, ACCbeta phosphorylation 10-fold, and p38 MAPK phosphorylation 60-fold, and the muscle fatigued by approximately 30% during contraction and NAC infusion had no significant effect on any of these responses. This was despite NAC preventing increases in S-glutathionylation with contraction. In conclusion, unlike during highly fatiguing ex vivo contractions, local NAC infusion during in situ low-moderate intensity hindlimb contractions in rats, a more physiological preparation, does not attenuate increases in skeletal muscle glucose uptake or AMPK signaling.
Authors:
T L Merry; R M Dywer; E A Bradley; S Rattigan; G K McConell
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Publication Detail:
Type:  Journal Article     Date:  2010-03-04
Journal Detail:
Title:  Journal of applied physiology (Bethesda, Md. : 1985)     Volume:  108     ISSN:  1522-1601     ISO Abbreviation:  J. Appl. Physiol.     Publication Date:  2010 May 
Date Detail:
Created Date:  2010-05-05     Completed Date:  2010-08-12     Revised Date:  2013-09-26    
Medline Journal Info:
Nlm Unique ID:  8502536     Medline TA:  J Appl Physiol (1985)     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1275-83     Citation Subset:  IM    
Affiliation:
Department of Physiology, The University of Melbourne, Parkville, Victoria 3010, Australia. t.merry@pgrad.unimelb.edu.au
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MeSH Terms
Descriptor/Qualifier:
AMP-Activated Protein Kinases / metabolism
Acetylcysteine / administration & dosage*,  metabolism
Animals
Antioxidants / administration & dosage*,  metabolism
Biological Transport
Blood Pressure
Cysteine / blood
Cystine / blood
Electric Stimulation
Glucose / metabolism*
Glutathione / metabolism
Heart Rate
Hindlimb
Infusions, Intra-Arterial
Male
Muscle Contraction*
Muscle Fatigue
Muscle Strength
Muscle, Skeletal / blood supply,  drug effects*,  innervation,  metabolism
Phosphorylation
Rats
Rats, Wistar
Reactive Oxygen Species / metabolism
Regional Blood Flow
Time Factors
Tyrosine / metabolism
Vascular Resistance
p38 Mitogen-Activated Protein Kinases / metabolism
Chemical
Reg. No./Substance:
0/Antioxidants; 0/Reactive Oxygen Species; 50-99-7/Glucose; 52-90-4/Cysteine; 55520-40-6/Tyrosine; 56-89-3/Cystine; 616-91-1/Acetylcysteine; 70-18-8/Glutathione; EC 2.7.11.1/AMP-Activated Protein Kinases; EC 2.7.11.24/p38 Mitogen-Activated Protein Kinases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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