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Two groups of subjects, participating in a medical research expedition (A,\n                    <jats:italic>n<\/jats:italic>\n                    = 5, 19d at 5300 m altitude; B,\n                    <jats:italic>n<\/jats:italic>\n                    = 6, 66d up to 8848 m) underwent a \u2248 30% drop of muscular creatine kinase and of glycolytic enzymes abundance. Protein abundance of most enzymes of the tricarboxylic acid cycle and oxidative phosphorylation was reduced both in A and, particularly, in B. Restriction of \u03b1\u2010ketoglutarate toward succinyl\u2010CoA resulted in increased prolyl hydroxylase 2 and glutamine synthetase. Both A and B were characterized by a reduction of elongation factor 2alpha, controlling protein translation, and by an increase of heat shock cognate 71 kDa protein involved in chaperone\u2010mediated autophagy. Increased protein levels of catalase and biliverdin reductase occurred in A alongside a decrement of voltage\u2010dependent anion channels 1 and 2 and of myosin\u2010binding protein C, suggesting damage to the sarcomeric structures. This study suggests that during acclimatization to hypobaric hypoxia the muscle behaves as a producer of substrates activating a metabolic reprogramming able to support anaplerotically the tricarboxylic acid cycle, to control protein translation, to prevent energy expenditure and to activate chaperone\u2010mediated autophagy.\n                  <\/jats:p>","DOI":"10.1002\/pmic.201400306","type":"journal-article","created":{"date-parts":[[2014,11,5]],"date-time":"2014-11-05T04:53:08Z","timestamp":1415163188000},"page":"160-171","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":40,"title":["Changes in muscle proteomics in the course of the Caudwell Research Expedition to Mt. 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