Cited by 40Muscle Physiology and DisordersMeat and Animal Product QualityMuscle metabolism and nutrition

Cinnamaldehyde regulates H2O2‐induced skeletal muscle atrophy by ameliorating the proteolytic and antioxidant defense systems

Kaur, Nirmaljeet, Gupta, Prachi, Saini, Vikram, Sherawat, Sandeep, Gupta, Sanjeev, Dua, Anita, Kumar, Vinod, Injeti, Elisha +1 more·2019·Journal of Cellular Physiology

Abstract

Abstract Skeletal muscle atrophy/wasting is associated with impaired protein metabolism in diverse physiological and pathophysiological conditions. Elevated levels of reactive oxygen species (ROS), disturbed redox status, and weakened antioxidant defense system are the major contributing factors toward atrophy. Regulation of protein metabolism by controlling ROS levels and its associated catabolic pathways may help in treating atrophy and related clinical conditions. Although cinnamaldehyde (CNA) enjoys the established status of antioxidant and its role in ROS management is reported, impact of CNA on skeletal muscle atrophy and related pathways is still unexplored. In the current study, the impact of CNA on C2C12 myotubes and the possible protection of cultured cells from H 2O 2‐induced atrophy is examined. Myotubes were treated with H 2O 2 in the presence and absence of CNA and the changes in the antioxidative, proteolytic systems, and mitochondrial functions were scored. Morphological analysis showed significant protective effects of CNA on length, diameter, and nuclei fusion index of myotubes. The evaluation of biochemical markers of atrophy; creatine kinase, lactate dehydrogenase, succinate dehydrogenase along with the study of muscle‐specific structural protein (i.e., myosin heavy chain‐fast [MHCf] type) showed significant protection of proteins by CNA. CNA pretreatment not only checked the activation of proteolytic systems (ubiquitin‐proteasome E3‐ligases [MuRF1/Atrogin1]), autophagy [Beclin1/LC3B], cathepsin L, calpain, caspase), but also prevented any alteration in the activities of antioxidative defense enzymes (catalase, glutathione‐ S‐transferase, glutathione‐peroxidase, superoxide dismutase, glutathione reductase). The results suggest that CNA protects myotubes from H 2O 2‐induced atrophy by inhibiting/resisting the amendments in proteolytic systems and maintains cellular redox‐balance.

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Crossref · 10.1002/jcp.27348

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  • Cinnamaldehyde protects H2O2-induced C2C12 myotubes atrophy by inhibiting the expression of MuRF1 and MAFbx and maintaining the balance of cellular redox.

    “Cinnamaldehyde protects H2O2-induced C2C12 myotubes atrophy by inhibiting the expression of MuRF1 and MAFbx and maintaining the balance of cellular redox [155].”

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Authors
Kaur, N., Gupta, P., Saini, V., Sherawat, S., Gupta, S., Dua, A., Kumar, V., Injeti, E., & Mittal, A.
Affiliations
  • Kurukshetra University (IN)
  • All India Institute of Medical Sciences (IN)
  • Maharishi Markandeshwar University, Mullana (IN)
  • Cedarville University (US)
Corresponding author
Mittal, Ashwani
Venue
Journal of Cellular Physiology
Publisher
Wiley
Published
2018-10-14
Volume
234
Issue
5
Pages
6194-6208
ISSN
  • 0021-9541 (ISSN-L)
  • 1097-4652
OpenAlex
W2896259626
Cited by
40
References
62
Citations by year
2026: 2 · 2025: 9 · 2024: 6 · 2023: 5 · 2022: 2 · 2021: 3 · 2020: 9 · 2019: 4
FWCI
1.42
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Cellular Physiology (publishedVersion)
  • PubMed (publishedVersion)
Funders
Indian Council of Medical Research (IRIS Cell No. 2012‐2656)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
  • Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Meat and Animal Product Quality
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
Keywords
cinnamaldehyde, skeletal muscle atrophy, hydrogen peroxide, reactive oxygen species, oxidative stress, proteolytic system, ubiquitin-proteasome system, autophagy, antioxidant defense, myotubes, redox homeostasis, myosin heavy chain, MuRF1, atrogin-1, calpain, cathepsin L, mitochondrial function
MeSH terms
Acrolein, Animals, Antioxidants, Cell Line, Hydrogen Peroxide, Muscular Atrophy, Muscle, Skeletal, Mice, Proteolysis

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