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Transcriptome analysis of aging muscle progenitors (human myoblasts)

ABSTRACT: Although sarcopenia is evident from the fifth decade, mechanisms leading to this phenomenon start earlier, emphasizing the importance of defining biomarkers related to the onset of muscle weakness. To this aim, a transcriptome analysis will be performed on muscle cell cultures (myoblasts) obtained from adult donors of different ages. Any biomarkers identified by this analysis will be confirmed by western blot and immunostatining. We will then assess the role of those biomarkers in muscle aging. Human myoblasts were extracted from the quadriceps of young (15-20 years old) and elderly (>70 years old) healthy subjects . The muscle cell population has been sorted using CD56 MACS beads. The myogenicity and the life span analysis of each muscle cell extract have been determined.

ORGANISM(S): Homo sapiens

PROVIDER: GSE52699 | GEO | 2015/06/01

SECONDARY ACCESSION(S): PRJNA229850

REPOSITORIES: GEO

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Project description:Background Muscle ageing contributes to both loss of functional autonomy and increased morbidity. Muscle atrophy accelerates after 50 years of age, but the mechanisms involved are complex and likely result from the alteration of a variety of interrelated functions. In order to better understand the molecular mechanisms underlying muscle chronological ageing in human, we have undertaken a top-down differential proteomic approach to identify novel biomarkers after the fifth decade of age. Results Muscle samples were compared between adult (56 years) and old (78 years) post-menopausal women. In addition to total muscle extracts, low-ionic strength extracts were investigated to remove high abundance myofibrillar proteins and improve the detection of low abundance proteins. Two-dimensional gel electrophoreses with overlapping IPGs were used to improve the separation of muscle proteins. Overall, 1919 protein spots were matched between all individuals, 95 were differentially expressed and identified by mass spectrometry, and they corresponded to 67 different proteins. Our results suggested important modifications in cytosolic, mitochondrial and lipid energy metabolism, which may relate to dysfunctions in old muscle force generation. A fraction of the differentially expressed proteins were linked to the sarcomere and cytoskeleton (myosin light-chains, troponin T, ankyrin repeat domain-containing protein-2, vinculin, four and a half LIM domain protein-3), which may account for alterations in contractile properties. In line with muscle contraction, we also identified proteins related to calcium signal transduction (calsequestrin-1, sarcalumenin, myozenin-1, annexins). Muscle ageing was further characterized by the differential regulation of several proteins implicated in cytoprotection (catalase, peroxiredoxins), ion homeostasis (carbonic anhydrases, selenium-binding protein 1) and detoxification (aldo-keto reductases, aldehyde dehydrogenases). Notably, many of the differentially expressed proteins were central for proteostasis, including heat shock proteins and proteins involved in proteolysis (valosin-containing protein, proteasome subunit beta type-4, mitochondrial elongation factor-Tu). Conclusions This study describes the most extensive proteomic analysis of muscle ageing in humans, and identified 34 new potential biomarkers. None of them were previously recognized as differentially expressed in old muscles, and each may represent a novel starting point to elucidate the mechanisms of muscle chronological ageing in humans.

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Transcriptome analysis of aging muscle progenitors (human myoblasts)

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