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Modulation of HSP25 and TNF- during the early stages of functional overload of a rat slow and fast muscle

¹Department of Kinesiology, University of Illinois, Urbana, Illinois; ²Department of Exercise Science, University of Puget Sound, Tacoma, Washington; and ³Brain Research Institute, University of California, Los Angeles, California

Submitted 5 January 2007 ; accepted in final form 16 March 2007

Early events in response to abrupt increases in activation and loading with muscle functional overload (FO) are associated with increased damage and inflammation. Heat shock protein 25 (HSP25) may protect against these stressors, and its expression can be regulated by muscle loading and activation. The purpose of this study was to investigate the responses of HSP25, phosphorylated HSP25 (pHSP25), and tumor necrosis factor- (TNF-) during FO of the slow soleus and fast plantaris. We compared the HSP25 mRNA, HSP25 protein, pHSP25, and TNF- responses in the soleus and plantaris after 0.5, 1, 2, 3, and 7 days of FO. HSP25 and pHSP25 were quantified in soluble and insoluble fractions. HSP25 mRNA increased immediately in both muscles and decreased with continued FO. However, HSP25 mRNA levels were consistently higher in the muscles of FO than control rats. In the soluble fraction, HSP25 increased in the plantaris after 2–7 days of FO with the greatest response at 3 and 7 days. The pHSP25 response to FO was greater in the plantaris than soleus at all points in the soluble fraction and at 0.5 days in the insoluble fraction. TNF- levels in the plantaris, but not soleus, were higher than control at 0.5–2 days of FO. This may have contributed to the greater FO response in pHSP25 in the plantaris than soleus as TNF- increased pHSP25 in C₂C₁₂ myotubes. These results suggest that the initial responses of pHSP25 and TNF- to mechanical stress and inflammation associated with FO are greater in a fast than slow extensor muscle.

heat shock protein 25; phosphorylation; tumor necrosis factor-alpha; skeletal muscle

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