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J Appl Physiol 94: 897-902, 2003. First published October 11, 2002; doi:10.1152/japplphysiol.00408.2002
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Vol. 94, Issue 3, 897-902, March 2003

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 Yoshioka1,3

1 Department of Physiology, St. Marianna University School of Medicine, Miyamae, Kawasaki City, Kanagawa 216-8511; 2 School of Health and Sport Sciences, Osaka University, Osaka 560-0043; and 3 Aomori University of Health and Welfare, Aomori 030-8505, Japan

Responses of the properties of connectin molecules in the slow-twitch soleus (Sol) and fast-twitch extensor digitorum longus muscles of rats to 3 days of unloading with or without 3-day reloading were investigated. The wet weight (relative to body wt) of Sol, not of extensor digitorum longus, in the unloaded group was significantly less than in 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 after hindlimb suspension. There were no changes in the molecular weights and the percent distributions of alpha - and beta -connectin in both muscles after hindlimb suspension. A significant increment of percent beta -connectin in Sol was observed after 3 days of reloading after 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 fibers. The lack of the elasticity in atrophied muscle fibers may cause a decrease in contractile function.

fast and slow muscles of rat; hindlimb suspension


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