HSP72 expression is specific to skeletal muscle contraction type

Exercise is capable of inducing the cellular stress response and increasing skeletal muscle heat shock protein (HSP) content. HSPs function as molecular chaperones and play roles in facilitating protein folding thereby contributing to muscle proteostasis. To determine the relationship between muscle contraction types, muscle damage, and HSP content, one tibialis anterior (TA) muscle from male Sprague-Dawley rats (n=5/group) was electrically stimulated while actively lengthening (LC), shortening (SC), or remaining to stagnate (IC) for 15 repetitions (3 sets of five). Two additional LC groups underwent 5 and 10 repetitions. Maximal tetanic tension (MTT) was recorded prior to (pre) and at 5min after (post) the last contraction. Twenty-four hours after stimulation, TA muscles were removed, processed, and assessed for damage and for HSP25 and HSP72 content. Post-MTT was significantly decreased following 15 LCs, (24%; p<0.05) but not following 15 SCs or 15 ICs. Post-MTT was also decreased by 8% (p<0.05), and 18% (p<0.05) for muscles subjected to 5 and 10 LCs, respectively. HSP72 content increased after all LCs conditions but not following ICs or SCs. HSP25 content remained unchanged following all contractions. Similarly, muscle damage was observed only after LCs and not after other contraction types. In conclusion, muscle HSP72 content can be increased with as few as 5 maximal lengthening contractions and appears to be related to muscle damage. This may have important implications for muscle rehabilitation and exercise training programs.