Document Detail

Subcellular movement and expression of HSP27, alphaB-crystallin, and HSP70 after two bouts of eccentric exercise in humans.
MedLine Citation:
PMID:  19498098     Owner:  NLM     Status:  MEDLINE    
The aims of this study were to investigate the sarcomeric accumulation and expression of heat shock proteins (HSPs) after two bouts of maximal eccentric exercise. Twenty-four subjects performed two bouts of 70 maximal voluntary eccentric actions using the elbow flexors in one arm. The bouts were separated by 3 wk. The changes in concentric (60 degrees/s) and isometric (90 degrees) force-generating capacity were monitored for 9 days after each bout, and biopsies were taken 1 and 48 h and 4 and 7 days after bout 1 and 1 and 48 h after bout 2. The content of HSP27, alphaB-crystallin, HSP70, and desmin in the cytosolic and cytoskeleton/myofibrillar fractions of homogenized muscle samples was determined by immunoassays, and the cellular and subcellular localization of the HSPs in the myofibrillar structure was analyzed by conventional and confocal immunofluorescence microscopy and quantitative electron microscopy. The force-generating capacity was reduced by approximately 50% and did not recover completely during the 3 wk following bout 1. After bout 2, the subjects recovered within 4 days. The HSP levels increased in the cytosolic fraction after bout 1, especially HSP70 (approximately 300% 2-7 days after exercise). Increased levels of HSP27, alphaB-crystallin, and HSP70 were found in the cytoskeletal/myofibrillar fraction after both bouts, despite reduced damage after bout 2. At the ultrastructural level, HSP27 and alphaB-crystallin accumulated in Z-disks, in intermediate desmin-like structures (alphaB-crystallin), and in areas of myofibrillar disruption. In conclusion, HSP27 and alphaB-crystallin accumulated in myofibrillar structures, especially in the Z-disks and the intermediate structures (desmin). The function of the small HSPs is possibly to stabilize and protect the myofibrillar structures during and after unaccustomed eccentric exercise. The large amount of HSP27, alphaB-crystallin, and HSP70 in the cytoskeletal/myofibrillar fraction after a repeated bout of exercise suggests a protective role as part of the repeated-bout effect.
G Paulsen; F Lauritzen; M L Bayer; J M Kalhovde; I Ugelstad; S G Owe; J Hallén; L H Bergersen; T Raastad
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Publication Detail:
Type:  Controlled Clinical Trial; Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-06-04
Journal Detail:
Title:  Journal of applied physiology (Bethesda, Md. : 1985)     Volume:  107     ISSN:  8750-7587     ISO Abbreviation:  J. Appl. Physiol.     Publication Date:  2009 Aug 
Date Detail:
Created Date:  2009-07-31     Completed Date:  2009-09-17     Revised Date:  2013-09-26    
Medline Journal Info:
Nlm Unique ID:  8502536     Medline TA:  J Appl Physiol (1985)     Country:  United States    
Other Details:
Languages:  eng     Pagination:  570-82     Citation Subset:  IM    
Norwegian School of Sport Sciences, Department of Anatomy, University of Oslo, P.O. Box 4014 U.S., N-0806 Oslo, Norway.
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MeSH Terms
Blotting, Western
Cell Membrane / metabolism
Cell Nucleus / metabolism
Cyclooxygenase 2 Inhibitors / administration & dosage
Cytosol / metabolism
Desmin / metabolism
Enzyme-Linked Immunosorbent Assay
HSP27 Heat-Shock Proteins / metabolism*
HSP70 Heat-Shock Proteins / metabolism*
Microscopy, Confocal
Microscopy, Electron, Transmission
Microscopy, Fluorescence
Muscle Contraction*
Muscle Strength
Muscle, Skeletal / drug effects,  metabolism*,  ultrastructure
Myofibrils / metabolism
Protein Transport
Pyrazoles / administration & dosage
Sarcomeres / drug effects,  metabolism*,  ultrastructure
Sulfonamides / administration & dosage
Time Factors
Young Adult
alpha-Crystallin B Chain / metabolism*
Reg. No./Substance:
0/CRYAB protein, human; 0/Cyclooxygenase 2 Inhibitors; 0/Desmin; 0/HSP27 Heat-Shock Proteins; 0/HSP70 Heat-Shock Proteins; 0/HSPB1 protein, human; 0/Pyrazoles; 0/Sulfonamides; 0/alpha-Crystallin B Chain; 169590-42-5/celecoxib
Erratum In:
J Appl Physiol. 2010 Mar;108(3):762

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