Source:http://linkedlifedata.com/resource/pubmed/id/10863996
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2000-8-16
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pubmed:abstractText |
Skeletal muscle fibres of untrained animals experience a stress response following exercise. This study was aimed at investigating whether chronic exercise modulates stress proteins of 70 kDa (HSP70s) in skeletal muscle. In the soleus muscle of Wistar rats, adherence to an incremental programme of treadmill running (IPTR) of 3 months duration up-regulated the levels of the beta-subunit of the mitochondrial F1-ATPase and those of HSP72, GRP75 and GRP78. Neither beta-F1-ATPase nor sarcoplasmic reticulum Ca2+-ATPase levels changed with training in the extensor digitorum longus (EDL) muscle. However, HSP70s increased during training. In soleus muscle slices of animals sacrificed 3 days after completing the IPTR, HSP72 and GRP75 were synthesized at lower rates than in sedentary animals while the GRP78 synthesis rate increased. Trained, rested animals also experienced a stress response following acute exercise of lower intensity than that of the actual training sessions. The data suggest that up-regulation of HSP70s by chronic exercise depends upon continued physical activity. Furthermore, the inverse correlation between levels and rates of synthesis of HSP72 during rest periods suggests the operation of a feedback regulatory loop aimed at reestablishing the threshold levels characteristic of unstressed fibres.
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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/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP72 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/glucose-regulated proteins,
http://linkedlifedata.com/resource/pubmed/chemical/molecular chaperone GRP78
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0031-6768
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
440
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
42-9
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:10863996-Animals,
pubmed-meshheading:10863996-Body Weight,
pubmed-meshheading:10863996-Carrier Proteins,
pubmed-meshheading:10863996-HSP70 Heat-Shock Proteins,
pubmed-meshheading:10863996-HSP72 Heat-Shock Proteins,
pubmed-meshheading:10863996-Heat-Shock Proteins,
pubmed-meshheading:10863996-Male,
pubmed-meshheading:10863996-Membrane Proteins,
pubmed-meshheading:10863996-Mitochondria, Muscle,
pubmed-meshheading:10863996-Molecular Chaperones,
pubmed-meshheading:10863996-Muscle, Skeletal,
pubmed-meshheading:10863996-Physical Exertion,
pubmed-meshheading:10863996-Proton-Translocating ATPases,
pubmed-meshheading:10863996-Rats,
pubmed-meshheading:10863996-Rats, Wistar,
pubmed-meshheading:10863996-Running,
pubmed-meshheading:10863996-Time
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pubmed:year |
2000
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pubmed:articleTitle |
Stress proteins of 70 kDa in chronically exercised skeletal muscle.
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pubmed:affiliation |
Departamento de Biología Molecular, Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Universidad Autónoma de Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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