4.5 Article

HSP25 can modulate myofibrillar desmin cytoskeleton following the phosphorylation at Ser15 in rat soleus muscle

期刊

JOURNAL OF APPLIED PHYSIOLOGY
卷 112, 期 1, 页码 176-186

出版社

AMER PHYSIOLOGICAL SOC
DOI: 10.1152/japplphysiol.00783.2011

关键词

unloading and reloading; myofibril; Z-disc; protein-to-protein interaction

资金

  1. Japan Society for the Promotion of Sciences [19100009, C-20500577]
  2. Ministry of Education, Culture, Sports, Science and Technology [19700521, B-21700656]
  3. Grants-in-Aid for Scientific Research [19700521] Funding Source: KAKEN

向作者/读者索取更多资源

Kawano F, Fujita R, Nakai N, Terada M, Ohira T, Ohira Y. HSP25 can modulate myofibrillar desmin cytoskeleton following the phosphorylation at Ser15 in rat soleus muscle. J Appl Physiol 112: 176-186, 2012. First published October 13, 2011; doi:10.1152/japplphysiol.00783.2011.-The main purpose of the present study was to investigate the role(s) of 25-kDa heat shock protein (HSP25) in the regulation and integration of myofibrillar Z-disc structure during down-or upregulation of the size in rat soleus muscle fibers. Hindlimb unloading by tail suspension was performed in adult rats for 7 days, and reloading was allowed for 5 days after the termination of suspension. Interaction of HSP25 and Z-disc proteins, phosphorylation status, distribution, and complex formation of HSP25 were investigated. Non- and single-phosphorylated HSP25s were generally expressed in the cytoplasmic fraction of normal muscle. The level of total HSP25, as well as the phosphorylation ratio, did not change significantly in response to atrophy. Increased expressions of HSP25, phosphorylated at serine 15 (p-Ser15) and dual-phosphorylated form, were noted, when atrophied muscles were reloaded. Myofibrillar HSP25 was also noted in reloaded muscle. Histochemical analysis further indicated the localization of p-Ser15 in the regions with disorganization of Z-disc structure in reloaded muscle fibers. HSP25 formed a large molecular complex in the cytoplasmic fraction of normal muscle, whereas dissociation of free HSP25 with Ser15 phosphorylation was noted in reloaded muscle. The interaction of p-Ser15 with desmin and actinin was detected in Z-discs by proximity ligation assay. Strong interaction between p-Ser15 and desmin, but not actinin, was noted in the disorganized areas. These results indicated that HSP25 contributed to the desmin cytoskeletal organization following the phosphorylation at Ser15 during reloading and regrowing of soleus muscle.

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