| Long-term swimming exercise does not modulate the Akt-dependent endothelial nitric oxide synthase phosphorylation in healthy mice. | |
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MedLine Citation:
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PMID: 21186380 Owner: NLM Status: In-Data-Review |
Abstract/OtherAbstract:
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Molecular mechanisms by which exercise exerts cardiovascular benefits are poorly understood. Exercise-induced increase of endothelial NO synthase (eNOS) phosphorylation through the protein kinase Akt has been shown to be a key mechanism underlying the beneficial effect of exercise in coronary artery disease patients. We examined whether this protective pathway might also be activated in long-term-exercised healthy mice. C57BL/6 wild-type mice swam for 24 weeks. A group of sedentary animals were used as controls. Aortic levels of total protein kinase Akt (protein kinase B), phosphorylated Akt at ser473 (p-Akt), total eNOS, phosphorylated eNOS at Ser1177 (p-eNOS), and PECAM-1 (platelet endothelial cell adhesion molecule-1) were assessed by Western blotting. Protein expressions of Akt, p-Akt, eNOS, p-eNOS, and PECAM-1 were not modulated by 24 weeks of exercise. The Akt-dependent eNOS phosphorylation did not seem to be a primary molecular adaptation in response to long-term exercise in healthy mice. |
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Authors:
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Maxime Pellegrin; Carole Miguet-Alfonsi; Alain Berthelot; Lucia Mazzolai; Pascal Laurant |
Publication Detail:
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Type: Journal Article |
Journal Detail:
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Title: Canadian journal of physiology and pharmacology Volume: 89 ISSN: 1205-7541 ISO Abbreviation: Can. J. Physiol. Pharmacol. Publication Date: 2011 Jan |
Date Detail:
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Created Date: 2010-12-27 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0372712 Medline TA: Can J Physiol Pharmacol Country: Canada |
Other Details:
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Languages: eng Pagination: 72-6 Citation Subset: IM |
Affiliation:
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Service of Vascular Medicine, Lausanne University Hospital, Centre Hospitalier Universitaire Vaudois, Av. Pierre Decker 5, 1011 Lausanne, Switzerland. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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