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

Levett, Denny Z.H., Viganò, Agnese, Capitanio, Daniele, Vasso, Michele, De Palma, Sara, Moriggi, Manuela, Martin, Daniel S, Murray, Andrew J., Cerretelli, Paolo, Grocott, Mike P.W. and Gelfi, Cecilia (2014) Changes in muscle proteomics in the course of the Caudwell Research Expedition to Mt. Everest Proteomics, pp. 1-12. (doi:10.1002/pmic.201400306). (PMID:25370915).

Record type: Article

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.

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More information

Published date: 4 December 2014
Keywords: altitude hypoxia, biomedicine, ?-ketoglutarate
Organisations: Clinical & Experimental Sciences

Identifiers

Local EPrints ID: 372852
URI: http://eprints.soton.ac.uk/id/eprint/372852
ISSN: 1615-9853
PURE UUID: 11bfdc12-9087-4ed3-9626-d10efeeb6815

Catalogue record

Date deposited: 23 Dec 2014 14:29
Last modified: 17 Jul 2017 21:38

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Contributors

Author: Denny Z.H. Levett
Author: Agnese Viganò
Author: Daniele Capitanio
Author: Michele Vasso
Author: Sara De Palma
Author: Manuela Moriggi
Author: Daniel S Martin
Author: Andrew J. Murray
Author: Paolo Cerretelli
Author: Cecilia Gelfi

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