title: Oxidative proteome alterations during skeletal muscle ageing.
abstract: Sarcopenia corresponds to the degenerative loss of skeletal muscle mass, quality, and strength associated with ageing and leads to a progressive impairment of mobility and quality of life. However, the cellular and molecular mechanisms involved in this process are not completely understood. A hallmark of cellular and tissular ageing is the accumulation of oxidatively modified (carbonylated) proteins, leading to a decreased quality of the cellular proteome that could directly impact on normal cellular functions. Although increased oxidative stress has been reported during skeletal muscle ageing, the oxidized protein targets, also referred as to the 'oxi-proteome' or 'carbonylome', have not been characterized yet. To better understand the mechanisms by which these damaged proteins build up and potentially affect muscle function, proteins targeted by these modifications have been identified in human rectus abdominis muscle obtained from young and old healthy donors using a bi-dimensional gel electrophoresis-based proteomic approach coupled with immunodetection of carbonylated proteins. Among evidenced protein spots, 17 were found as increased carbonylated in biopsies from old donors comparing to young counterparts. These proteins are involved in key cellular functions such as cellular morphology and transport, muscle contraction and energy metabolism. Importantly, impairment of these pathways has been described in skeletal muscle during ageing. Functional decline of these proteins due to irreversible oxidation may therefore impact directly on the above-mentioned pathways, hence contributing to the generation of the sarcopenic phenotype.
authors.affiliation: Sorbonne Universités, UPMC Univ Paris 06, UMR 8256, Biological Adaptation and Ageing-IBPS, Paris F-75005, France; CNRS UMR-8256, Paris F-75005, France; Inserm U1164, Paris F-75005, France.
authors.forename: Sofia
authors.initials: S
authors.lastname: Lourenço Dos Santos
authors.affiliation: Sorbonne Universités, UPMC Univ Paris 06, UMR 8256, Biological Adaptation and Ageing-IBPS, Paris F-75005, France; CNRS UMR-8256, Paris F-75005, France; Inserm U1164, Paris F-75005, France.
authors.forename: Martin A
authors.initials: MA
authors.lastname: Baraibar
authors.affiliation: Department of Women's and Children's Health, Uppsala University, Uppsala SE-751 82, Sweden.
authors.forename: Staffan
authors.initials: S
authors.lastname: Lundberg
authors.affiliation: Department of Women's and Children's Health, Uppsala University, Uppsala SE-751 82, Sweden.
authors.forename: Orvar
authors.initials: O
authors.lastname: Eeg-Olofsson
authors.affiliation: Department of Physiology and Pharmacology, Karolinska Institutet, Stockholm SE-171 77, Sweden; Department of Clinical Neuroscience, Clinical Neurophysiology, Karolinska Institutet, Stockholm SE-171 77, Sweden.
authors.forename: Lars
authors.initials: L
authors.lastname: Larsson
authors.affiliation: Sorbonne Universités, UPMC Univ Paris 06, UMR 8256, Biological Adaptation and Ageing-IBPS, Paris F-75005, France; CNRS UMR-8256, Paris F-75005, France; Inserm U1164, Paris F-75005, France. Electronic address: bertrand.friguet@upmc.fr.
authors.forename: Bertrand
authors.initials: B
authors.lastname: Friguet
mesh_terms: D000368:Aged; D000375:Aging; D002648:Child; D002675:Child, Preschool; D015180:Electrophoresis, Gel, Two-Dimensional; D006801:Humans; D007223:Infant; D007231:Infant, Newborn; D008875:Middle Aged; D018482:Muscle, Skeletal / Q000378:metabolism* / Q000473:pathology; D018384:Oxidative Stress; D050050:Protein Carbonylation; D020543:Proteome / Q000032:analysis*; D053719:Tandem Mass Spectrometry
chemical_list: D020543:Proteome
keywords: Ageing; Human rectus abdominis skeletal muscle; Oxidative stress; Protein carbonylation; Proteomics