Document Detail


Induction, modification and accumulation of HSP70s in the rat liver after acute exercise: early and late responses.
MedLine Citation:
PMID:  14754995     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Liver cells synthesize HSP72, the cytosolic highly stress-inducible member of the 70 kDa family of heat-shock proteins (HSP70s), in response to acute exercise. This study was aimed at obtaining further insight into the physiological relevance of the hepatic stress response to exercise by investigating the induction and long-term maintenance of increased levels of HSP70s of the HSP and glucose-regulated protein (GRP) families, their post-translational modifications during or after exercise and the possible relation of HSP induction to oxidative stress. In a running rat model, acute exercise activated the synthesis and accumulation of HSP72, GRP75 and GRP78 in liver cells, pointing towards a multifactorial origin of this response. A peak HSP72 accumulation was observed shortly after exercise as a result of transcriptional activation. HSP72 was reduced shortly after exercise preceding the disappearance of its mRNA. Two further waves of HSP72 accumulation peaked 8 and 48 h after exercise without transcriptional activation. A transient increase in the proportion of acidic variants of HSP72 and HSP73 was also observed shortly after exercise as a result, at least in part, of protein phosphorylation. Free and protein-bound lipid peroxidation derivatives (TBARS) showed a tendency to increase in the early post-exercise and the free-to-protein-bound TBARS ratio decreased significantly after 2 h. During the early post-exercise period, protein-bound TBARS correlated positively with HSP72 and 73, but not with GRP75 or GRP78. Altogether, the reported results indicate that the early induction and post-translational modification of HSP70s in liver cells following exercise is a preliminary step of a series of long-lasting HSP70-related events, possibly designed to preserve liver cell homeostasis and to help provide a concerted response of the whole organism to physical stress.
Authors:
Beatriz González; Rafael Manso
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2004-01-30
Journal Detail:
Title:  The Journal of physiology     Volume:  556     ISSN:  0022-3751     ISO Abbreviation:  J. Physiol. (Lond.)     Publication Date:  2004 Apr 
Date Detail:
Created Date:  2004-04-15     Completed Date:  2004-11-09     Revised Date:  2013-06-09    
Medline Journal Info:
Nlm Unique ID:  0266262     Medline TA:  J Physiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  369-85     Citation Subset:  IM    
Affiliation:
Centro de Biología Molecular 'Severo Ochoa' (CSIC-UAM), Universidad Autónoma de Madrid, E-28049 Cantoblanco, Madrid, Spain. rmanso@cbm.uam.es
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MeSH Terms
Descriptor/Qualifier:
Animals
Cytosol / metabolism
HSP70 Heat-Shock Proteins / metabolism*
Heat-Shock Proteins*
Lipid Peroxidation / physiology
Liver / metabolism*
Male
Membrane Proteins / metabolism
Molecular Chaperones*
Oxidative Stress / physiology
Physical Exertion / physiology*
Proteins / metabolism
Rats
Rats, Wistar
Thiobarbituric Acid Reactive Substances / metabolism
Time Factors
Chemical
Reg. No./Substance:
0/HSP70 Heat-Shock Proteins; 0/Heat-Shock Proteins; 0/Hspa5 protein, rat; 0/Membrane Proteins; 0/Molecular Chaperones; 0/Proteins; 0/Thiobarbituric Acid Reactive Substances; 0/glucose-regulated proteins
Comments/Corrections

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