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- Title
DHA Inhibits Protein Degradation More Efficiently than EPA by Regulating the PPARγ/NFκB Pathway in C2C12 Myotubes.
- Authors
Yue Wang; Qiao-wei Lin; Pei-pei Zheng; Jian-song Zhang; Fei-ruo Huang
- 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 IxBa phosphorylation and increased in the IκBα protein level than 400 μM EPA (P < 0.01). Compared with BSA, 400 pM EPA and DHA resulted in a 47% or 68% induction of the NFκB 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 PPARγ expression, respectively (P < 0.01). In C2C12 myotubes for PPARy knockdown, neither 400 μM EPA nor DHA affected the levels of p-IκBα, total IκBα or NFκB DNA binding activity compared with BSA (P > 0.05). Interestingly, EPA and DHA both still decreased the total protein degradation, although PPARγ 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 PPARα/NF-κB pathway in C2C12 myotubes.
- Publication
BioMed Research International, 2013, Vol 2013, p1
- ISSN
2314-6133
- Publication type
Article
- DOI
10.1155/2013/318981