Source:http://linkedlifedata.com/resource/pubmed/id/21499714
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1-2
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pubmed:dateCreated |
2011-6-29
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pubmed:abstractText |
The aim of this study was to determine whether or not over-activation of calpains during running exercise or tetanic contractions was a major factor to induce sarcomere lesions in atrophic soleus muscle. Relationship between the degrees of desmin degradation and sarcomere lesions was also elucidated. We observed ultrastructural changes in soleus muscle fibers after 4-week unloading with or without running exercise. Calpain activity and desmin degradation were measured in atrophic soleus muscles before or after repeated tetani in vitro. Calpain-1 activity was progressively increased and desmin degradation was correspondingly elevated in 1-, 2-, and 4-week of unloaded soleus muscles. Calpain-1 activity and desmin degradation had an additional increase in unloaded soleus muscles after repeated tetani in vitro. PD150606, an inhibitor of calpains, reduced calpain activity and desmin degradation during tetanic contractions in unloaded soleus muscles. The 4-week unloading decreased the width of myofibrils and Z-disk in soleus fibers. After running exercise in unloaded group, Z-disks of adjacent myofibrils were not well in register but instead were longitudinally displaced. Calpain inhibition compromised exercise-induced misalignment of the Z-disks in atrophic soleus muscle. These results suggest that tetanic contractions induce an over-activation of calpains which lead to higher degrees of desmin degradation in unloaded soleus muscle. Desmin degradation may loose connections between adjacent myofibrils, whereas running exercise results in sarcomere injury in unloaded soleus muscle.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acrylates,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calpain,
http://linkedlifedata.com/resource/pubmed/chemical/Desmin,
http://linkedlifedata.com/resource/pubmed/chemical/PD 150606,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin,
http://linkedlifedata.com/resource/pubmed/chemical/calpastatin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1573-4919
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
354
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
171-80
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pubmed:meshHeading |
pubmed-meshheading:21499714-Acrylates,
pubmed-meshheading:21499714-Animals,
pubmed-meshheading:21499714-Calcium-Binding Proteins,
pubmed-meshheading:21499714-Calpain,
pubmed-meshheading:21499714-Desmin,
pubmed-meshheading:21499714-Enzyme Assays,
pubmed-meshheading:21499714-Male,
pubmed-meshheading:21499714-Motor Activity,
pubmed-meshheading:21499714-Muscle, Skeletal,
pubmed-meshheading:21499714-Muscle Contraction,
pubmed-meshheading:21499714-Muscular Disorders, Atrophic,
pubmed-meshheading:21499714-Rats,
pubmed-meshheading:21499714-Rats, Sprague-Dawley,
pubmed-meshheading:21499714-Sarcomeres,
pubmed-meshheading:21499714-Signal Transduction,
pubmed-meshheading:21499714-Troponin,
pubmed-meshheading:21499714-Weightlessness Simulation
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pubmed:year |
2011
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pubmed:articleTitle |
Tetanic contractions impair sarcomeric Z-disk of atrophic soleus muscle via calpain pathway.
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pubmed:affiliation |
Department of Aerospace Physiology, Fourth Military Medical University, 169# Changlexi Road, Xi'an 710032, China.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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