Skeletal muscle glucose uptake during exercise: A focus on reactive oxygen species and nitric oxide signaling

IUBMB Life ◽  
2009 ◽  
Vol 61 (5) ◽  
pp. 479-484 ◽  
Author(s):  
Troy L. Merry ◽  
Glenn K. McConell
Keyword(s):  
Nitric Oxide ◽  
Reactive Oxygen Species ◽  
Skeletal Muscle ◽  
Glucose Uptake ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Nitric Oxide Signaling ◽  
Skeletal Muscle Glucose Uptake

scholarly journals Stretch-stimulated glucose uptake in skeletal muscle is mediated by reactive oxygen species and p38 MAP-kinase

2009 ◽  
Vol 587 (13) ◽  
pp. 3363-3373 ◽  
Author(s):  
Melissa A. Chambers ◽  
Jennifer S. Moylan ◽  
Jeffrey D. Smith ◽  
Laurie J. Goodyear ◽  
Michael B. Reid
Keyword(s):  
Reactive Oxygen Species ◽  
Skeletal Muscle ◽  
Map Kinase ◽  
Glucose Uptake ◽  
Reactive Oxygen ◽  
P38 Map Kinase ◽  
Oxygen Species

scholarly journals TNF signals via neuronal-type nitric oxide synthase and reactive oxygen species to depress specific force of skeletal muscle

2013 ◽  
Vol 114 (11) ◽  
pp. 1629-1636 ◽  
Author(s):  
Shawn A. Stasko ◽  
Brian J. Hardin ◽  
Jeffrey D. Smith ◽  
Jennifer S. Moylan ◽  
Michael B. Reid
Keyword(s):  
Nitric Oxide ◽  
Reactive Oxygen Species ◽  
Skeletal Muscle ◽  
Contractile Function ◽  
Full Range ◽  
Reactive Oxygen ◽  
Specific Force ◽  
Oxygen Species ◽  
Cell Assays ◽  
Neuronal Type

TNF promotes skeletal muscle weakness, in part, by depressing specific force of muscle fibers. This is a rapid, receptor-mediated response, in which TNF stimulates cellular oxidant production, causing myofilament dysfunction. The oxidants appear to include nitric oxide (NO); otherwise, the redox mechanisms that underlie this response remain undefined. The current study tested the hypotheses that 1) TNF signals via neuronal-type NO synthase (nNOS) to depress specific force, and 2) muscle-derived reactive oxygen species (ROS) are essential co-mediators of this response. Mouse diaphragm fiber bundles were studied using live cell assays. TNF exposure increased general oxidant activity ( P < 0.05; 2′,7′-dichlorodihydrofluorescein diacetate assay) and NO activity ( P < 0.05; 4-amino-5-methylamino-2′,7′-difluorofluorescein diacetate assay) and depressed specific force across the full range of stimulus frequencies (1-300 Hz; P < 0.05). These responses were abolished by pretreatment with Nω-nitro-L-arginine methyl ester (L-NAME; a nonspecific inhibitor of NOS activity), confirming NO involvement. Genetic nNOS deficiency replicated L-NAME effects on TNF-treated muscle, diminishing NO activity (−80%; P < 0.05) and preventing the decrement in specific force ( P < 0.05). Comparable protection was achieved by selective depletion of muscle-derived ROS. Pretreatment with either SOD (degrades superoxide anion) or catalase (degrades hydrogen peroxide) depressed oxidant activity in TNF-treated muscle and abolished the decrement in specific force. These findings indicate that TNF signals via nNOS to depress contractile function, a response that requires ROS and NO as obligate co-mediators.

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