http://www.cnr.it/ontology/cnr/individuo/prodotto/ID290471

Changes in muscle proteomics in the course of the Caudwell Research Expedition to Mt. Everest. (Articolo in rivista)

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Changes in muscle proteomics in the course of the Caudwell Research Expedition to Mt. Everest. (Articolo in rivista) (literal)

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Denny Z.H. Levett1,2*, Agnese Viganò 3*, Daniele Capitanio3,4, Michele Vasso5, Sara De Palma5, Manuela Moriggi3,4, Daniel S. Martin1, Andrew J. Murray6, Paolo Cerretelli5, Mike P. W. Grocott2,7,8* and Cecilia Gelfi3,4,5* (2015)
Changes in muscle proteomics in the course of the Caudwell Research Expedition to Mt. Everest.
in Proteomics (Weinh., Internet)
(literal)

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Denny Z.H. Levett1,2*, Agnese Viganò 3*, Daniele Capitanio3,4, Michele Vasso5, Sara De Palma5, Manuela Moriggi3,4, Daniel S. Martin1, Andrew J. Murray6, Paolo Cerretelli5, Mike P. W. Grocott2,7,8* and Cecilia Gelfi3,4,5* (literal)

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Centre for Altitude, Space, and Extreme Environment Medicine, University College London (UCL), Institute of Child Health, University College London, London, UK 2 Anaesthesia and Critical Care Research Unit, University Hospital Southampton, NHS Foundation Trust, Southampton, UK 3 Department of Biomedical Sciences for Health, University of Milan, Segrate, Milan, Italy 4 IRCCS Policlinico San Donato, San Donato Milanese, Milano, Italy 5 CNR-Institute of Bioimaging and Molecular Physiology, Cefalu-Segrate, Italy ` 6 Department of Physiology, Development, and Neuroscience, University of Cambridge, Cambridge, UK 7 Integrative Physiology and Critical Illness Group, Division of Clinical and Experimental Science, Faculty of Medicine, University of Southampton, Southampton, UK 8 Southampton NIHR Respiratory Biomedical Research Unit, Southampton, UK (literal)

Titolo

Changes in muscle proteomics in the course of the Caudwell Research Expedition to Mt. Everest. (literal)

Abstract

This study employed differential proteomic and immunoassay techniques to elucidate the biochemical mechanisms utilized by human muscle (vastus lateralis) in response to high altitude hypoxia exposure. Two groups of subjects, participating in a medical research expedition (A, n = 5, 19d at 5300 m altitude; B, n = 6, 66d up to 8848 m) underwent a ? 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 ?-ketoglutarate toward succinyl-CoA 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-mediated autophagy. Increased protein levels of catalase and biliverdin reductase occurred in A alongside a decrement of voltage-dependent anion channels 1 and 2 and of myosin-binding 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-mediated autophagy. (literal)

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