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Articles in PresS, published online ahead of print October 11, 2002
J Appl Physiol, 10.1152/jap.00408.2002
Submitted on May 10, 2002
Accepted on September 3, 2002
1 Department of Physiology, St. Marianna University, Kawasaki, Kanagawa, Japan
2 School of Health and Sport Sciences, Osaka University, Toyonaka, Osaka, Japan
3 Department of Physiology, St. Marianna University, Kawasaki, Kanagawa, Japan; Aomori University of Health and Welfare, Aomori, Aomori, Japan
* To whom correspondence should be addressed. E-mail: ohira{at}space.hss.osaka-u.ac.jp.
Responses of the properties of connectin molecules in the slow-twitch soleus (SOL) and fast-twitch extensor digitorum longus (EDL) muscles of rats to 3 days of unloading with or without 3-day reloading were investigated. The wet weight (relative to body weight) of SOL, not of EDL, in the unloaded group was significantly less than the age-matched control (p<0.05). Immunoelectron microscopic analyses showed that a monoclonal antibody against connectin (SM1) bound to the I-band region close to the edge of the A-band at resting length and moved reversibly away from the Z-line as the muscle fibers were stretched. In SOL, the displacement of the SM1-bound dense spots in response to stretching decreased following hindlimb suspension. There were no changes in the molecular weights and the percent distributions of
- and ß -connectin in both muscles following hindlimb suspension. A significant increment of percent ß -connectin in SOL was observed after 3-day reloading following hindlimb suspension (p<0.05). It is suggested that the elasticity of connectin filaments in the I-band region of the atrophied SOL fibers was reduced relative to that of the control. The lack of the elasticity in atrophied muscle fibers may cause a decrease in contractile function.
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