Document Detail


Heat shock transcription factor activation and hsp72 accumulation in aged skeletal muscle.
MedLine Citation:
PMID:  10701839     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Induction of the protective heat shock proteins (Hsps), and of Hsp72 in particular, has been reported to be decreased in certain tissues from aged animals. To determine if both fast and slow skeletal muscles from aged animals demonstrate an altered ability to induce and accumulate Hsp72, adult (age, 6 months) and aged (age, 20 months) Fischer 344 rats were subjected to heat stress. At selected times (0, 1, 3, and 24 hours) after a 10-minute, 41 degrees C heat stress, fast (white gastrocnemius [WG]) and slow (soleus) skeletal muscles were examined for either heat shock transcription factor (HSF) activation (trimerization and DNA-binding activity) or Hsp72 content using electrophoretic gel mobility shift assays and Western blotting, respectively. Immediately after heat stress, the level of HSF activation between aged and adult animals was similar for both muscles. HSF activation was undetectable at 1 and 3 hours after heat stress in all cases. Twenty-four hours after heat stress, Hsp72 content in the WG muscles from both aged and adult animals was significantly increased compared with unstressed, age-matched controls (P < 0.05). In contrast, perhaps because of their high constitutive Hsp72 levels, soleus muscles from both aged and adult animals did not demonstrate a significant increase in Hsp72 content after heat shock, but there was a trend toward increased levels. Hsp72 content in both the soleus and WG muscles demonstrated no significant differences between adult and aged animals in either the unstressed state (controls) or after heat shock. These results suggest that skeletal muscles from aged animals are capable of inducing the heat shock response and accumulating Hsp72.
Authors:
M Locke
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Cell stress & chaperones     Volume:  5     ISSN:  1355-8145     ISO Abbreviation:  Cell Stress Chaperones     Publication Date:  2000 Jan 
Date Detail:
Created Date:  2000-04-11     Completed Date:  2000-04-11     Revised Date:  2013-04-18    
Medline Journal Info:
Nlm Unique ID:  9610925     Medline TA:  Cell Stress Chaperones     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  45-51     Citation Subset:  IM    
Affiliation:
Faculty of Physical Education and Health, University of Toronto, Ontario, Canada. marius.locke@utoronto.ca
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MeSH Terms
Descriptor/Qualifier:
Aging / genetics,  metabolism*
Animals
DNA-Binding Proteins / physiology*
Gene Expression Regulation
HSP72 Heat-Shock Proteins
Heat-Shock Proteins / biosynthesis*,  genetics
Hot Temperature*
Male
Muscle Development
Muscle Proteins / biosynthesis*,  genetics
Muscle, Skeletal / growth & development,  metabolism*
Rats
Rats, Inbred F344
Stress, Physiological / genetics,  metabolism
Transcription Factors
Transcription, Genetic
Chemical
Reg. No./Substance:
0/DNA-Binding Proteins; 0/HSP72 Heat-Shock Proteins; 0/Heat-Shock Proteins; 0/Muscle Proteins; 0/Transcription Factors; 0/heat shock transcription factor
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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