{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,17]],"date-time":"2023-10-17T06:10:47Z","timestamp":1697523047135},"reference-count":40,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2012,9,6]],"date-time":"2012-09-06T00:00:00Z","timestamp":1346889600000},"content-version":"vor","delay-in-days":1650,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Obesity"],"published-print":{"date-parts":[[2008,3]]},"abstract":"<jats:p><jats:bold>Objective:<\/jats:bold> Mitochondrial activity is altered in skeletal muscle of obese, insulin\u2010resistant or type 2 diabetic patients. We hypothesized that this situation was associated with profound adaptations in resting muscle energetics. For that purpose, we used <jats:italic>in vivo<\/jats:italic> <jats:sup>31<\/jats:sup>P\u2010nuclear magnetic resonance (<jats:sup>31<\/jats:sup>P\u2010NMR) in male sedentary Wistar rats fed with obesogenic diets known to induce alterations in muscle mitochondrial activity.<\/jats:p><jats:p><jats:bold>Methods and Procedures:<\/jats:bold> Two experimental diets (high sucrose and high fat) were provided for 6 weeks at two levels of energy (standard, N and high, H) and compared to control diet. The rates of the adenosine triphosphate (ATP) exchange between phosphocreatine (PCr) and <jats:bold>\u03b3<\/jats:bold>\u2010ATP (<jats:italic>k<\/jats:italic><jats:sub>a<\/jats:sub>) and <jats:bold>\u03b2<\/jats:bold>\u2010adenosine diphosphate (<jats:bold>\u03b2<\/jats:bold>\u2010ADP) to <jats:bold>\u03b2<\/jats:bold>\u2010ATP (<jats:italic>k<\/jats:italic><jats:sub>b<\/jats:sub>) were evaluated using <jats:sup>31<\/jats:sup>P\u2010NMR in resting <jats:italic>gastrocnemius<\/jats:italic> muscle. Muscle contents in phosphorylated compounds as well as creatine, were assessed using <jats:sup>31<\/jats:sup>P\u2010NMR and biochemical assays, respectively.<\/jats:p><jats:p><jats:bold>Results:<\/jats:bold> ATP content increased by 6.7\u20138.5% in standard\u2010energy high\u2010sucrose (NSU), high\u2010energy high\u2010fat (HF) and high\u2010energy high\u2010sucrose (HSU) groups compared to control (<jats:italic>P<\/jats:italic> &lt; 0.05), whereas PCr content decreased by 4.2\u20136.4% (<jats:italic>P<\/jats:italic> &lt; 0.01). Consequently, PCr to ATP ratio decreased in NSU, HF, and HSU groups, compared to control (<jats:italic>P<\/jats:italic> &lt; 0.01). Furthermore in high\u2010energy groups (HF and HSU) compared to control, creatine contents were decreased by 14\u201319% (<jats:italic>P<\/jats:italic> &lt; 0.001), whereas <jats:italic>k<\/jats:italic><jats:sub>a<\/jats:sub> and <jats:italic>k<\/jats:italic><jats:sub>b<\/jats:sub> fluxes were increased by 89\u2013133% (<jats:italic>P<\/jats:italic> &lt; 0.001) and 243\u2013277% (<jats:italic>P<\/jats:italic> &lt; 0.01), respectively.<\/jats:p><jats:p><jats:bold>Discussion:<\/jats:bold> Our <jats:italic>in vivo<\/jats:italic> data showed adaptations of resting skeletal muscle energetics in response to high\u2010energy diets. Increased activity of enzymes catalyzing ATP production may reflect a compensatory mechanism to face impaired mitochondrial ATP synthesis in order to preserve intracellular energy homeostasis.<\/jats:p>","DOI":"10.1038\/oby.2007.91","type":"journal-article","created":{"date-parts":[[2008,1,31]],"date-time":"2008-01-31T15:36:21Z","timestamp":1201793781000},"page":"572-577","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Impaired Resting Muscle Energetics Studied by <sup>31<\/sup>P\u2010NMR in Diet\u2010induced Obese Rats"],"prefix":"10.1002","volume":"16","author":[{"given":"Emilie","family":"Chanseaume","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guy","family":"Bielicki","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anne\u2010Laure","family":"Tardy","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jean\u2010Pierre","family":"Renou","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Damien","family":"Freyssenet","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yves","family":"Boirie","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"B\u00e9atrice","family":"Morio","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2012,9,6]]},"reference":[{"key":"e_1_2_7_2_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.ijo.0802804"},{"key":"e_1_2_7_3_2","doi-asserted-by":"publisher","DOI":"10.2337\/diacare.27.5.1047"},{"key":"e_1_2_7_4_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJMsr043743"},{"key":"e_1_2_7_5_2","doi-asserted-by":"publisher","DOI":"10.2337\/diabetes.54.1.8"},{"key":"e_1_2_7_6_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1104343"},{"key":"e_1_2_7_7_2","doi-asserted-by":"publisher","DOI":"10.1056\/NEJMoa031314"},{"key":"e_1_2_7_8_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pmed.0020233"},{"key":"e_1_2_7_9_2","doi-asserted-by":"publisher","DOI":"10.1161\/01.CIR.0000072789.89096.10"},{"key":"e_1_2_7_10_2","first-page":"133","article-title":"Interaction of creatine kinase and adenylate kinase systems in muscle cells","author":"Savabi F.","year":"1994","journal-title":"Mol Cell Biochem"},{"key":"e_1_2_7_11_2","first-page":"133","article-title":"Metabolic compartmentation and substrate channelling in muscle cells. 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