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Articles in PresS, published online ahead of print January 9, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00252.2001
Submitted on June 6, 2001
Accepted on December 20, 2001
1 Lab. Plasticite Neuromusculaire, Univ. de Lille1, Villeneuve d'Ascq, France
* To whom correspondence should be addressed. E-mail: Laurence.Stevens{at}univ-lille1.fr.
This study was concerned with the effects of mechanical unloading of rat soleus muscle on the isoform patterns of the three troponin (Tn) subunits, troponin T (TnT), troponin I (TnI) and troponin C (TnC). Mechanical unloading was achieved by hindlimb unloading (HU) for time periods of 7, 14, and 28 days. Relative concentrations of slow and fast TnT, TnI, and TnC isoforms were assessed by electrophoretic and immunoblot analyses. HU induced profound slow-to-fast isoforms transitions of all Tn subunits, although to different extents and with different time-courses. The effectiveness of the isoform transitions was higher for TnT than for TnI and TnC. Indeed, TnI and TnC encompassed minor partial exchanges of slow with their fast counterparts while the expression pattern of TnTf was largely increased after HU. Moreover, slow and fast isoforms of the different Tn were not affected in a same manner by HU This suggested that the slow and fast counterparts of the Tn subunit isoforms are regulated independently in response to HU. The changes in TnTf composition occurred in parallel with previously demonstrated transitions within the pattern of the fast myosin heavy chains in the same muscles.
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