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Cited by 315Muscle Physiology and DisordersNutrition and Health in AgingMuscle metabolism and nutrition

Single Muscle Fiber Proteomics Reveals Fiber-Type-Specific Features of Human Muscle Aging

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Murgia, Marta, Toniolo, Luana, Nagaraj, Nagarjuna, Ciciliot, Stefano, Vindigni, Vincenzo, Schiaffino, Stefano, Reggiani, Carlo, Mann, Matthias·2017·Cell Reports
DOI 10.1016/j.celrep.2017.05.054
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Abstract

Skeletal muscle is a key tissue in human aging, which affects different muscle fiber types unequally. We developed a highly sensitive single muscle fiber proteomics workflow to study human aging and show that the senescence of slow and fast muscle fibers is characterized by diverging metabolic and protein quality control adaptations. Whereas mitochondrial content declines with aging in both fiber types, glycolysis and glycogen metabolism are upregulated in slow but downregulated in fast muscle fibers. Aging mitochondria decrease expression of the redox enzyme monoamine oxidase A. Slow fibers upregulate a subset of actin and myosin chaperones, whereas an opposite change happens in fast fibers. These changes in metabolism and sarcomere quality control may be related to the ability of slow, but not fast, muscle fibers to maintain their mass during aging. We conclude that single muscle fiber analysis by proteomics can elucidate pathophysiology in a sub-type-specific manner.

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  • Muscle loss in aging sarcopenia, cancer cachexia, chemotherapy-induced cachexia, and in a model of myasthenia gravis is characterized by the decline of both fusion and fission machinery.

    “Muscle loss in aging sarcopenia [185, 187, 215], cancer cachexia, chemotherapy-induced cachexia [157–159], and in a model of myasthenia gravis [216], is characterized by the decline of both fusion and fission machinery.”

    From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [215]

  • Muscle loss in aging sarcopenia, cancer cachexia, and myasthenia gravis is characterized by the decline of both fusion machinery and fission machinery.

    “However, muscle loss in aging sarcopenia, cancer cachexia, and myasthenia gravis are characterized by the decline of both fusion machinery and fission machinery [6,11,12,15,16,17,18].”

    From Inhibition of the Fission Machinery Mitigates OPA1 Impairment in Adult Skeletal Muscles (2019) · cites this paper as [12]

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Authors
Murgia, M., Toniolo, L., Nagaraj, N., Ciciliot, S., Vindigni, V., Schiaffino, S., Reggiani, C., & Mann, M.
Affiliations
  • University of Padua (IT)
  • Max Planck Institute of Biochemistry (DE)
  • Veneto Institute of Molecular Medicine (IT)
Corresponding author
  • Murgia, Marta
  • Mann, Matthias
ORCID
Venue
Cell Reports
Publisher
Elsevier BV
Published
2017-06
Volume
19
Issue
11
Pages
2396-2409
ISSN
2211-1247 (ISSN-L)
DOI
10.1016/j.celrep.2017.05.054
OpenAlex
W2625907748
Cited by
315
References
10
Citations by year
2026: 38 · 2025: 34 · 2024: 45 · 2023: 35 · 2022: 40 · 2021: 27 · 2020: 41 · 2019: 24 · 2018: 25 · 2017: 6
FWCI
10.73
Type
journal article
Language
en
Open access
Licence
Locations
  • Cell Reports (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion, other-oa)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Padua Research Archive (University of Padova) (submittedVersion, cc-by-nc-nd)
  • Padua Research Archive (University of Padova) (submittedVersion)
Funders
  • Max-Planck-Gesellschaft
  • Seventh Framework Programme (HEALTH-F4-2008-201648/PROSPECTS)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Health Sciences › Medicine › Physiology › Nutrition and Health in Aging
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Keywords
skeletal muscle aging, muscle fiber type, slow muscle fibers, fast-twitch muscle, mitochondrial content, glycolysis, glycogen metabolism, monoamine oxidase A, redox metabolism, protein quality control, myosin chaperone, sarcomere, muscle mass preservation
MeSH terms
Aging, Glycogen, Glycolysis, Humans, Muscle Fibers, Skeletal, Proteomics

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