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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  µ M decreased total protein degradation ( P  < 0.01). However, the total protein degradation was decreased when the concentrations of DHA ranged from 300  µ M to 700  µ M ( P  < 0.01). DHA (400  µ M, 24 h) more efficiently decreased the I  κ  B  α   phosphorylation and increased in the I  κ  B  α   protein level than 400  µ M EPA ( P  < 0.01). Compared with BSA, 400  µ M EPA and DHA resulted in a 47% or 68% induction of the NF  κ  B DNA binding activity, respectively ( P  < 0.01). Meanwhile, 400  µ M EPA and DHA resulted in a 1.3-fold and 2.0-fold induction of the PPAR  γ   expression, respectively ( P  < 0.01). In C2C12 myotubes for PPAR  γ   knockdown, neither 400  µ M EPA nor DHA affected the levels of p-I  κ  B  α  , total I  κ  B  α   or NF  κ  B DNA binding activity compared with BSA ( P  > 0.05). Interestingly, EPA and DHA both still decreased the total protein degradation, although PPAR  γ   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  γ  /NF-  κ  B pathway in C2C12 myotubes.

DHA Inhibits Protein Degradation More Efficiently than EPA by Regulating the PPARγ/NFκB Pathway in C2C12 Myotubes