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* To whom correspondence should be addressed. E-mail: tjkoh{at}uic.edu.
The purposes of this study were to determine whether, immediately after lengthening contractions, (a) levels of specific force-transmitting cytoskeletal elements are reduced in skeletal muscle cells and (b) cytosolic small heat shock proteins (HSPs) translocate to structures prone to disruption. Western blot analysis demonstrated decreased concentrations of z-disk proteins 
-actinin and plectin, and membrane scaffolding proteins dystrophin and 
-spectrin, in muscle exposed to lengthening contractions compared with contralateral control muscle. Lengthening contractions also resulted in immediate translocation of constitutively expressed HSP25 and B-crystallin from the soluble to the insoluble fraction of muscle homogenates, and cryosections showed translocation from a diffuse, cytosolic localization to striations that corresponded to z-disks. Lengthening contraction-induced translocation of HSP25 and B-crystallin was associated with phosphorylation of these small HSPs, which may trigger their protective activity. In summary, these findings demonstrate loss of z-disk and membrane scaffolding proteins immediately after lengthening contractions, and concomitant translocation of HSP25 and B-crystallin to the z-disk, which may help to stabilize or repair cytoskeletal elements at this site.
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