Cinnamaldehyde regulates H 2 O 2 -induced skeletal muscle atrophy by ameliorating the proteolytic and antioxidant defense systems

Academic Article

Abstract

  • © 2018 Wiley Periodicals, Inc. 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 2 O 2 -induced atrophy is examined. Myotubes were treated with H 2 O 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 2 O 2 -induced atrophy by inhibiting/resisting the amendments in proteolytic systems and maintains cellular redox-balance.
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    Author List

  • Kaur N; Gupta P; Saini V; Sherawat S; Gupta S; Dua A; Kumar V; Injeti E; Mittal A
  • Start Page

  • 6194
  • End Page

  • 6208
  • Volume

  • 234
  • Issue

  • 5