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- Title
DHA Inhibits Protein Degradation More Efficiently than EPA by Regulating the PPAR[gamma]/NF[kappa]B Pathway in C2C12 Myotubes.
- Authors
Wang, Yue; Lin, Qiao-Wei; Zheng, Pei-Pei; Zhang, Jian-Song; Huang, Fei-Ruo
- Abstract
This study was conducted to evaluate the mechanism by which n-3 PUFA regulated the protein degradation in C2C12 myotubes. Compared with the BSA control, EPA at concentrations from 400 to 600 µM decreased total protein degradation (P < 0.01). However, the total protein degradation was decreased when the concentrations of DHA ranged from 300 µM to 700 µM (P < 0.01). DHA (400 µM, 24 h) more efficiently decreased the I ¿ B ¿ phosphorylation and increased in the I ¿ B ¿ protein level than 400 µM EPA (P < 0.01). Compared with BSA, 400 µM EPA and DHA resulted in a 47% or 68% induction of the NF ¿ B DNA binding activity, respectively (P < 0.01). Meanwhile, 400 µM EPA and DHA resulted in a 1.3-fold and 2.0-fold induction of the PPAR ¿ expression, respectively (P < 0.01). In C2C12 myotubes for PPAR ¿ knockdown, neither 400 µM EPA nor DHA affected the levels of p-I ¿ B ¿ , total I ¿ B ¿ or NF ¿ B DNA binding activity compared with BSA (P > 0.05). Interestingly, EPA and DHA both still decreased the total protein degradation, although PPAR ¿ knockdown attenuated the suppressive effects of EPA and DHA on the total protein degradation (P < 0.01). These results revealed that DHA inhibits protein degradation more efficiently than EPA by regulating the PPAR ¿ /NF- ¿ B pathway in C2C12 myotubes.
- Publication
BioMed Research International, 2013, Vol 2013, p318981
- ISSN
2314-6133
- Publication type
Journal Article
- DOI
2013/318981