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Long-term swimming exercise does not modulate the Akt-dependent endothelial nitric oxide synthase phosphorylation in healthy mice.
MedLine Citation:
PMID:  21186380     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
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.
Authors:
Maxime Pellegrin; Carole Miguet-Alfonsi; Alain Berthelot; Lucia Mazzolai; Pascal Laurant
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Canadian journal of physiology and pharmacology     Volume:  89     ISSN:  1205-7541     ISO Abbreviation:  Can. J. Physiol. Pharmacol.     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2010-12-27     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372712     Medline TA:  Can J Physiol Pharmacol     Country:  Canada    
Other Details:
Languages:  eng     Pagination:  72-6     Citation Subset:  IM    
Affiliation:
Service of Vascular Medicine, Lausanne University Hospital, Centre Hospitalier Universitaire Vaudois, Av. Pierre Decker 5, 1011 Lausanne, Switzerland.
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