Cited by 56Muscle Physiology and DisordersNutrition and Health in AgingMuscle metabolism and nutrition

Role of Protein Carbonylation in Skeletal Muscle Mass Loss Associated with Chronic Conditions

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Barreiro, Esther·2016·Proteomes

Abstract

Muscle dysfunction, characterized by a reductive remodeling of muscle fibers, is a common systemic manifestation in highly prevalent conditions such as chronic heart failure (CHF), chronic obstructive pulmonary disease (COPD), cancer cachexia, and critically ill patients. Skeletal muscle dysfunction and impaired muscle mass may predict morbidity and mortality in patients with chronic diseases, regardless of the underlying condition. High levels of oxidants may alter function and structure of key cellular molecules such as proteins, DNA, and lipids, leading to cellular injury and death. Protein oxidation including protein carbonylation was demonstrated to modify enzyme activity and DNA binding of transcription factors, while also rendering proteins more prone to proteolytic degradation. Given the relevance of protein oxidation in the pathophysiology of many chronic conditions and their comorbidities, the current review focuses on the analysis of different studies in which the biological and clinical significance of the modifications induced by reactive carbonyls on proteins have been explored so far in skeletal muscles of patients and animal models of chronic conditions such as COPD, disuse muscle atrophy, cancer cachexia, sepsis, and physiological aging. Future research will elucidate the specific impact and sites of reactive carbonyls on muscle protein content and function in human conditions.

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  • In muscle, ROS mainly originate from mitochondrial respiration and membrane NADPH oxidase; in lung, ROS are produced by alveolar macrophages and activated neutrophils.

    “In the muscle, ROS mainly originate from mitochondrial respiration and membrane (NAPDH oxidase). In the lung, by contrast, ROS are produced by alveolar macrophages and activated neutrophils [117].”

    From Main Pathogenic Mechanisms and Recent Advances in COPD Peripheral Skeletal Muscle Wasting (2023) · cites this paper as [117]

    Section 3 says skeletal-muscle ROS are mainly produced by the mitochondrial respiratory chain and also identifies NADPH oxidase as a source. Section 8.2 identifies mitochondria and membrane NADPH oxidase as the main sources specifically in respiratory and limb muscles of patients with severe COPD. Our copy does not support the separate claim that lung ROS are produced by alveolar macrophages and activated neutrophils (searched for alveolar macrophages). (LLM, conf=0.86)

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Authors
Barreiro, E.
Affiliations
Universitat Pompeu Fabra (ES)
Corresponding author
Barreiro, Esther
Venue
Proteomes
Publisher
MDPI AG
Published
2016-05-06
Volume
4
Issue
2
Pages
18
ISSN
2227-7382 (ISSN-L)
OpenAlex
W2345518686
Cited by
56
References
166
Citations by year
2026: 4 · 2025: 4 · 2024: 7 · 2023: 8 · 2022: 4 · 2021: 10 · 2020: 7 · 2019: 4 · 2018: 6 · 2017: 2
FWCI
0.36
Type
journal article
Language
en
Open access
Locations
  • Proteomes (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Repositori digital de la UPF (Universitat Pompeu Fabra) (publishedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • RECERCAT (Consorci de Serveis Universitaris de Catalunya) (submittedVersion, cc-by)
Funders
  • Fundació Catalana de Pneumologia
  • Sociedad Española de Neumología y Cirugía Torácica (SEPAR 2010)
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
protein carbonylation, skeletal muscle atrophy, muscle mass loss, chronic heart failure, chronic obstructive pulmonary disease, cancer cachexia, sepsis, disuse atrophy, aging, oxidative stress, muscle dysfunction, protein oxidation, proteolysis

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