Temperature-dependent enhancement of proteolysis in C2C12 myotubes in association with the activation of 26S proteasome.

The effect of temperature on protein metabolism of C2C12 myotubes was investigated in order to estimate the potential effect of fever on muscle catabolism. The half-life of long-lived proteins in C2C12 myotubes was significantly (13%) shorter when incubated at 40 degrees C than at 37 degrees. The activities of cathepsins B and L were not significantly different at 37 and 40 degrees C, nor were the levels of the protein and mRNA of the two cathepsins. In contrast, the chymotrypsin-like activity of 26S proteasome was elevated by 53% at 40 degrees C, compared to that at 37 degrees C, although it was not associated with an increase in the levels of the protein and mRNA of proteasome subunits. mRNA levels of calpain and ubiquitin were not affected by temperature. It is concluded that temperature-dependent enhancement of proteolysis in C2C12 myotubes is associated with an increase in 26S proteasome activity.