The effects of eccentric contraction on myofibrillar proteins in rat skeletal muscle

European Journal of Applied Physiology Volume 110 Issue 5 Page 943-952 published_at 2010-11
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Title ( eng )
The effects of eccentric contraction on myofibrillar proteins in rat skeletal muscle
Creator
Kanzaki Keita
Kuratani Mai
Mishima Takaaki
Matsunaga Satoshi
Source Title
European Journal of Applied Physiology
Volume 110
Issue 5
Start Page 943
End Page 952
Abstract
The present study investigated the effects of eccentric muscle contractions (ECC) on the content of myofibrillar proteins (my-proteins) and the catalytic activity of myofibrillar ATPase (my-ATPase) in skeletal muscles. Rat extensor digitorum longus and tibialis anterior muscles were exposed to 200-repeated ECC or isometric contractions (ISC) and used for measures of force output and for biochemical analyses, respectively. Whereas in ISC-treated muscles, full restoration of tetanic force was attained after 2 days of recovery, force developed by ECC-treated muscles remained depressed (P<0.05) after 6 days. The total my-protein content and the relative content of myosin heavy chain (MHC) in total my-proteins were unaltered during 4 days of recovery after ECC, but fell (P<0.05) to 55.9 and 63.4% after 6 days of recovery, respectively. my-ATPase activity expressed on a my-protein weight basis was unaltered immediately after ECC. However, it decreased (P<0.05) to 75.3, 45.3, and 49.3% after 2, 4 and 6 days of recovery, respectively. Total maximal calpain activity measured at 5 mM Ca2+ was significantly augmented (P<0.05) after 2 days of recovery, reaching a level of threefold higher after 6 days. These alterations were specific for ECC and not observed for ISC. These results suggest that depressions in my-ATPase activity contribute to ECC-induced decreases in force and power which can take a number of days to recover.
Keywords
Myosin heavy chain
Muscle damage
Stretched contraction
Proteolysis
Myofibrillar ATPase
NDC
Medical sciences [ 490 ]
Language
eng
Resource Type journal article
Publisher
Springer
Date of Issued 2010-11
Rights
Copyright (c) 2010 Springer
Publish Type Author’s Original
Access Rights open access
Source Identifier
The original publication is available at www.springerlink.com
[ISSN] 1439-6319
[DOI] 10.1007/s00421-010-1579-3
[NCID] AA11413391
[DOI] http://dx.doi.org/10.1007/s00421-010-1579-3