| Endothelial nitric oxide synthase is central to skeletal muscle metabolic regulation and enzymatic signaling during exercise in vivo. | |
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MedLine Citation:
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PMID: 20200137 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Endothelial nitric oxide synthase (eNOS) is associated with a number of physiological functions involved in the regulation of metabolism; however, the functional role of eNOS is poorly understood. We tested the hypothesis that eNOS is critical to muscle cell signaling and fuel usage during exercise in vivo, using 16-wk-old catheterized (carotid artery and jugular vein) C57BL/6J mice with wild-type (WT), partial (+/-), or no expression (-/-) of eNOS. Quantitative reductions in eNOS expression ( approximately 40%) elicited many of the phenotypic effects observed in enos(-/-) mice under fasted, sedentary conditions, with expression of oxidative phosphorylation complexes I to V and ATP levels being decreased, and total NOS activity and Ca(2+)/CaM kinase II Thr(286) phosphorylation being increased in skeletal muscle. Despite these alterations, exercise tolerance was markedly impaired in enos(-/-) mice during an acute 30-min bout of exercise. An eNOS-dependent effect was observed with regard to AMP-activated protein kinase signaling and muscle perfusion. Muscle glucose and long-chain fatty acid uptake, and hepatic and skeletal muscle glycogenolysis during the exercise bout was markedly accelerated in enos(-/-) mice compared with enos(+/-) and WT mice. Correspondingly, enos(-/-) mice exhibited hypoglycemia during exercise. Thus, the ablation of eNOS alters a number of physiological processes that result in impaired exercise capacity in vivo. The finding that a partial reduction in eNOS expression is sufficient to induce many of the changes associated with ablation of eNOS has implications for chronic metabolic diseases, such as obesity and insulin resistance, which are associated with reduced eNOS expression. |
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Authors:
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Robert S Lee-Young; Julio E Ayala; Charles F Hunley; Freyja D James; Deanna P Bracy; Li Kang; David H Wasserman |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2010-03-03 |
Journal Detail:
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Title: American journal of physiology. Regulatory, integrative and comparative physiology Volume: 298 ISSN: 1522-1490 ISO Abbreviation: Am. J. Physiol. Regul. Integr. Comp. Physiol. Publication Date: 2010 May |
Date Detail:
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Created Date: 2010-08-17 Completed Date: 2010-09-08 Revised Date: 2011-07-28 |
Medline Journal Info:
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Nlm Unique ID: 100901230 Medline TA: Am J Physiol Regul Integr Comp Physiol Country: United States |
Other Details:
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Languages: eng Pagination: R1399-408 Citation Subset: IM |
Affiliation:
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Department of Molecular Physiology and Biophysics, Vanderbilt University, School of Medicine, 2200 Pierce Ave., Nashville, TN 37232, U.S.A. robert.s.lee-young@vanderbilt.edu |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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AMP-Activated Protein Kinases
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metabolism Animals Body Composition / physiology Body Weight / physiology Calorimetry, Indirect Energy Metabolism / physiology* Female Gluconeogenesis / physiology Glycogen / metabolism Hypoglycemia / metabolism, physiopathology Insulin / blood Male Mice Mice, Inbred C57BL Mice, Mutant Strains Mitochondria / physiology Muscle, Skeletal / blood supply, enzymology* Nitric Oxide Synthase Type III / genetics, metabolism* Oxidative Phosphorylation Photoperiod Physical Conditioning, Animal / physiology Physical Exertion / physiology* Pregnancy Regional Blood Flow / physiology Signal Transduction / physiology* |
| Grant Support | |
ID/Acronym/Agency:
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R01 DK-54902/DK/NIDDK NIH HHS; U24 DK-59637/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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11061-68-0/Insulin; 9005-79-2/Glycogen; EC 1.14.13.39/Nitric Oxide Synthase Type III; EC 1.14.13.39/Nos3 protein, mouse; EC 2.7.11.1/AMP-Activated Protein Kinases; EC 2.7.11.1/AMPK alpha1 subunit, mouse |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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