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MUSCLE CELL BIOLOGY AND CELL MOTILITY

Cytoskeletal disruption and small heat shock protein translocation immediately after lengthening contractions

School of Kinesiology, University of Illinois at Chicago, Chicago, Illinois 60608

Submitted 7 August 2003 ; accepted in final form 13 November 2003

The purposes of this study were to determine whether, immediately after lengthening contractions, 1) levels of specific force-transmitting cytoskeletal elements are reduced in skeletal muscle cells and 2) 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.

skeletal muscle injury; heat shock protein 25; B-crystallin; dystrophin; desmin

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