{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,16]],"date-time":"2026-05-16T01:04:34Z","timestamp":1778893474454,"version":"3.51.4"},"reference-count":51,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2018,2,14]],"date-time":"2018-02-14T00:00:00Z","timestamp":1518566400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100005884","name":"Centro Nacional de Investigaciones Cardiovasculares","doi-asserted-by":"publisher","award":["SEV\u20102015\u20100505"],"award-info":[{"award-number":["SEV\u20102015\u20100505"]}],"id":[{"id":"10.13039\/501100005884","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004587","name":"Instituto de Salud Carlos III","doi-asserted-by":"publisher","award":["PI15\/00558"],"award-info":[{"award-number":["PI15\/00558"]}],"id":[{"id":"10.13039\/501100004587","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004587","name":"Instituto de Salud Carlos III","doi-asserted-by":"publisher","award":["PI15\/01756"],"award-info":[{"award-number":["PI15\/01756"]}],"id":[{"id":"10.13039\/501100004587","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Journal of Physiology"],"published-print":{"date-parts":[[2018,3,15]]},"abstract":"<jats:sec><jats:title>Key points<\/jats:title><jats:p><jats:list list-type=\"bullet\"><jats:list-item><jats:p>Although they are unable to utilize muscle glycogen, McArdle mice adapt favourably to an individualized moderate\u2010intensity endurance exercise training regime. Yet, they fail to reach the performance capacity of healthy mice with normal glycogen availability.<\/jats:p><\/jats:list-item><jats:list-item><jats:p>There is a remarkable difference in the protein networks involved in muscle tissue adaptations to endurance exercise training in mice with and without glycogen availability.<\/jats:p><\/jats:list-item><jats:list-item><jats:p>Indeed, endurance exercise training promoted the expression of only three proteins common to both McArdle and wild\u2010type mice: LIMCH1, PARP1 and TIGD4.<\/jats:p><\/jats:list-item><jats:list-item><jats:p>In turn, trained McArdle mice presented strong expression of mitogen\u2010activated protein kinase 12 (MAPK12).<\/jats:p><\/jats:list-item><\/jats:list><\/jats:p><\/jats:sec><jats:sec><jats:title>Abstract<\/jats:title><jats:p>McArdle's disease is an inborn disorder of skeletal muscle glycogen metabolism that results in blockade of glycogen breakdown due to mutations in the myophosphorylase gene. We recently developed a mouse model carrying the homozygous p.R50X common human mutation (McArdle mouse), facilitating the study of how glycogen availability affects muscle molecular adaptations to endurance exercise training. Using quantitative differential analysis by liquid chromatography with tandem mass spectrometry, we analysed the quadriceps muscle proteome of 16\u2010week\u2010old McArdle (<jats:italic>n<\/jats:italic>\u00a0=\u00a05) and wild\u2010type (WT) (<jats:italic>n<\/jats:italic>\u00a0=\u00a04) mice previously subjected to 8\u00a0weeks\u2019 moderate\u2010intensity treadmill training or to an equivalent control (no training) period. Protein networks enriched within the differentially expressed proteins with training in WT and McArdle mice were assessed by hypergeometric enrichment analysis. Whereas endurance exercise training improved the estimated maximal aerobic capacity of both WT and McArdle mice as compared with controls, it was \u223c50% lower than normal in McArdle mice before and after training. We found a remarkable difference in the protein networks involved in muscle tissue adaptations induced by endurance exercise training with and without glycogen availability, and training induced the expression of only three proteins common to McArdle and WT mice: LIM and calponin homology domains\u2010containing protein 1 (LIMCH1), poly (ADP\u2010ribose) polymerase 1 (PARP1 \u2013 although the training effect was more marked in McArdle mice), and tigger transposable element derived 4 (TIGD4). Trained McArdle mice presented strong expression of mitogen\u2010activated protein kinase 12 (MAPK12). Through an in\u2010depth proteomic analysis, we provide mechanistic insight into how glycogen availability affects muscle protein signalling adaptations to endurance exercise training.<\/jats:p><\/jats:sec>","DOI":"10.1113\/jp275292","type":"journal-article","created":{"date-parts":[[2018,1,10]],"date-time":"2018-01-10T04:34:07Z","timestamp":1515558847000},"page":"1035-1061","source":"Crossref","is-referenced-by-count":30,"title":["Muscle molecular adaptations to endurance exercise training are conditioned by glycogen availability: a proteomics\u2010based analysis in the McArdle mouse model"],"prefix":"10.1113","volume":"596","author":[{"given":"Carmen","family":"Fiuza\u2010Luces","sequence":"first","affiliation":[{"name":"Mitochondrial and Neuromuscular Diseases Laboratory and \u2018MITOLAB\u2010CM\u2019 Research Institute of Hospital \u201812 de Octubre\u2019 (\u2018i+12\u2019) Madrid 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