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Cited by 108Muscle Physiology and DisordersUbiquitin and proteasome pathwaysMuscle metabolism and nutrition

Out of Control: The Role of the Ubiquitin Proteasome System in Skeletal Muscle during Inflammation

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Haberecht-Müller, Stefanie, Krüger, Elke, Fielitz, Jens·2021·Biomolecules
DOI 10.3390/biom11091327PMC PMC8468834
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Abstract

The majority of critically ill intensive care unit (ICU) patients with severe sepsis develop ICU-acquired weakness (ICUAW) characterized by loss of muscle mass, reduction in myofiber size and decreased muscle strength leading to persisting physical impairment. This phenotype results from a dysregulated protein homeostasis with increased protein degradation and decreased protein synthesis, eventually causing a decrease in muscle structural proteins. The ubiquitin proteasome system (UPS) is the predominant protein-degrading system in muscle that is activated during diverse muscle atrophy conditions, e.g., inflammation. The specificity of UPS-mediated protein degradation is assured by E3 ubiquitin ligases, such as atrogin-1 and MuRF1, which target structural and contractile proteins, proteins involved in energy metabolism and transcription factors for UPS-dependent degradation. Although the regulation of activity and function of E3 ubiquitin ligases in inflammation-induced muscle atrophy is well perceived, the contribution of the proteasome to muscle atrophy during inflammation is still elusive. During inflammation, a shift from standard- to immunoproteasome was described; however, to which extent this contributes to muscle wasting and whether this changes targeting of specific muscular proteins is not well described. This review summarizes the function of the main proinflammatory cytokines and acute phase response proteins and their signaling pathways in inflammation-induced muscle atrophy with a focus on UPS-mediated protein degradation in muscle during sepsis. The regulation and target-specificity of the main E3 ubiquitin ligases in muscle atrophy and their mode of action on myofibrillar proteins will be reported. The function of the standard- and immunoproteasome in inflammation-induced muscle atrophy will be described and the effects of proteasome-inhibitors as treatment strategies will be discussed.

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  • IL-1β and SAA1 are crucial for muscle atrophy in sepsis and both increased mRNA and protein expression of IL-6 as well as MuRF1/Trim63 and Atrogin-1/Fbxo32.

    “Recently, we showed that IL‐1β and SAA1 are crucial for muscle atrophy in sepsis and that both increased the mRNA and protein expression of IL‐6 as well as MuRF1/Trim63 and Atrogin‐1/Fbxo32. 11 , 12 , 26”

    From Sepsis induces interleukin 6, gp130/JAK2/STAT3, and muscle wasting (2022) · cites this paper as [26]

    Sections 4.3 and 4.4 link IL-1β and SAA1 to muscle atrophy in sepsis and describe pathways involving MuRF1 and atrogin-1. Section 4.2 says IL-1β stimulates IL-6 production, while section 4.4 reports SAA1-induced IL6 expression in non-muscle cells. The review does not establish the more specific claim that both factors increased mRNA and protein expression of IL-6, MuRF1 and atrogin-1. (LLM, conf=0.85)

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200 of 377 shown

Cited by

Sorted by citations

  • Sepsis induces interleukin 6, gp130/JAK2/STAT3, and muscle wasting

    Zanders, L., Kny, M., Hahn, A., Schmidt, S., Wundersitz, S., Todiras, M., Lahmann, I., Bandyopadhyay, A., Wollersheim, T., Kaderali, L., et al. (2022) · Journal of Cachexia, Sarcopenia and Muscle · doi:10.1002/jcsm.12867 · Cited by 225 · see citing works

    “Recently, we showed that IL-1β and SAA1 are crucial for muscle atrophy in sepsis and that both increased the mRNA and protein expression of IL-6 as well as MuRF1/Trim63 and Atrogin-1/Fbxo32.(11,12,26) Together with our novel data, we 720 L.”
    BackgroundSelf-citation

Authors
Haberecht-Müller, S., Krüger, E., & Fielitz, J.
Affiliations
Universitätsmedizin Greifswald (DE)
Corresponding author
  • Krüger, Elke
  • Fielitz, Jens
ORCID
Venue
Biomolecules
Publisher
MDPI AG
Published
2021-09-08
Volume
11
Issue
9
Pages
1327
ISSN
2218-273X (ISSN-L)
DOI
10.3390/biom11091327
PMC
PMC8468834
OpenAlex
W3198276966
Cited by
108
References
36
Citations by year
2026: 35 · 2025: 21 · 2024: 20 · 2023: 18 · 2022: 13 · 2021: 1
FWCI
1.39
Type
journal article
Language
en
Open access
Licence
Locations
  • Biomolecules (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, other-oa)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • MDC Repository (Max-Delbrueck-Center for Molecular Medicine) (acceptedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Deutsche Forschungsgemeinschaft (SFBTR186 TP A13; FI 965/5-2, FI 965/9-1)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Keywords
ubiquitin-proteasome system, skeletal muscle atrophy, inflammation, sepsis, ICU-acquired weakness, E3 ubiquitin ligase, atrogin-1, MuRF1, immunoproteasome, inflammatory cytokines, acute phase proteins, proteasome inhibitors, protein degradation, muscle atrophy
MeSH terms
Animals, Humans, Inflammation, Cytokines, Muscle, Skeletal, Ubiquitin, Proteasome Endopeptidase Complex, Proteolysis

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