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PMID:14627610
| Citation |
Koh, TJ and Escobedo, J (2004) Cytoskeletal disruption and small heat shock protein translocation immediately after lengthening contractions. Am. J. Physiol., Cell Physiol. 286:C713-22 |
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| Abstract |
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 alpha-actinin and plectin and membrane scaffolding proteins dystrophin and beta-spectrin in muscle exposed to lengthening contractions compared with contralateral control muscle. Lengthening contractions also resulted in immediate translocation of constitutively expressed HSP25 and alphaB-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 alphaB-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 alphaB-crystallin to the z-disk, which may help to stabilize or repair cytoskeletal elements at this site. |
| Links |
PubMed Online version:10.1152/ajpcell.00341.2003 |
| Keywords |
Animals; Cytoskeleton/metabolism; Fluorescent Antibody Technique; Heat-Shock Proteins; Male; Mice; Mice, Inbred C57BL; Muscle Contraction/physiology; Muscle Fibers, Skeletal/physiology; Neoplasm Proteins/metabolism; Phosphorylation; Specific Pathogen-Free Organisms; alpha-Crystallin B Chain/metabolism |
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Significance
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