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J Appl Physiol (October 11, 2002). doi:10.1152/japplphysiol.00408.2002
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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

Profiles of connectin (titin) in atrophied soleus muscle induced by unloading of rats

Katsumasa Goto1, Ryoko Okuyama1, Masanori Honda1, Hiroshi Uchida1, Tatsuo Akema1, Yoshinobu Ohira2*, and Toshitada Yoshioka3

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 {alpha} - 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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