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Absence of heat shock transcription factor 1 retards the regrowth of atrophied soleus muscle in mice.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yasuhara, Kazuyuki Ohno, Yoshitaka Kojima, Atsushi Uehara, Kenji Beppu, Moroe Sugiura, Takao Fujimoto, Mitsuaki Nakai, Akira Ohira, Yoshinobu Yoshioka, Toshitada Goto, Katsumasa
Description	Country affiliation: Japan Author Affiliation: Yasuhara K ( Department of Orthopaedic Surgery, St. Marianna University School of Medicine, Kawasaki, Japan.)
Abstract	Effects of heat shock transcription factor 1 (HSF1) gene on the regrowth of atrophied mouse soleus muscles were studied. Both HSF1-null and wild-type mice were subjected to continuous hindlimb suspension for 2 wk followed by 4 wk of ambulation recovery. There was no difference in the magnitude of suspension-related decrease of muscle weight, protein content, and the cross-sectional area of muscle fibers between both types of mice. However, the regrowth of atrophied soleus muscle in HSF1-null mice was slower compared with that in wild-type mice. Lower baseline expression level of HSP25, HSC70, and HSP72 were noted in soleus muscle of HSF1-null mice. Unloading-associated downregulation and reloading-associated upregulation of HSP25 and HSP72 mRNA were observed not only in wild-type mice but also in HSF1-null mice. Reloading-associated upregulation of HSP72 and HSP25 during the regrowth of atrophied muscle was observed in wild-type mice. Minor and delayed upregulation of HSP72 at mRNA and protein levels was also seen in HSF1-null mice. Significant upregulations of HSF2 and HSF4 were observed immediately after the suspension in HSF1-null mice, but not in wild-type mice. Therefore, HSP72 expression in soleus muscle might be regulated by the posttranscriptional level, but not by the stress response. Evidence from this study suggested that the upregulation of HSPs induced by HSF1-associated stress response might play, in part, important roles in the mechanical loading (stress)-associated regrowth of skeletal muscle.
File Format	HTM / HTML
ISSN	87507587
e-ISSN	15221601
Journal	Journal of Applied Physiology
Issue Number	4
Volume Number	111
Language	English
Publisher	American Physiological Society
Publisher Date	2011-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Physiology Dna-binding Proteins Genetics Metabolism Muscle Fibers, Skeletal Muscular Atrophy Transcription Factors Animals Body Weight Down-regulation Hsc70 Heat-shock Proteins Hsp72 Heat-shock Proteins Heat-shock Proteins Hindlimb Suspension Mice Pathology Muscle Proteins Neoplasm Proteins Protein Processing, Post-translational Rna, Messenger Up-regulation Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Physiology Physiology (medical) Sports Science

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