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1 Department of Physiology and Biophysics, University of California, Irvine, Irvine, CA, USA
2 Brain Research Institute, University of California, Los Angeles, Los Angeles, CA, USA
3 Department of Physiological Sciences, University of California Los Angeles, Los Angeles, CA, USA
4 Brain Research Institute, University of California, Los Angeles, Los Angeles, CA, USA; Department of Physiological Sciences, University of California Los Angeles, Los Angeles, CA, USA
* To whom correspondence should be addressed. E-mail: kmbaldwi{at}uci.edu.
We examined the expression of several molecular markers of protein balance in response to skeletal muscle atrophy induced by spinal cord isolation (SI, i.e., a complete transection of the spinal cord at both a mid-thoracic and a high sacral level plus complete differentiation between the two transection sites). This treatment nearly eliminates neuromuscular activity (activation and loading) of the hindlimb muscles while maintaining neuromuscular connectivity. SI was associated with a reduced transcriptional activity (via pre-mRNA analyses) of myosin heavy chain (MHC) and actin. In addition, there was an increased gene expression of enzyme systems impacting protein degradation (calpain 1; plus enzymes associated with polyubquitination processes) that could further contribute to the protein deficits in the SI muscles via degradative pathways. IGF-I receptor and binding protein-5 (BP-5) mRNA expression was induced throughout the 15-day period of SI, while IGF-I mRNA was induced at 8 and 15 days. These responses occurred in the absence of an upregulation of translational regulatory proteins (p70-S6 kinase; 4EBP1) to compensate for the decreased protein translational capacity. These data collectively demonstrate that 1) the molecular changes accompanying SI-induced muscle atrophy are not necessarily the reverse of those occurring during muscle hypertrophy, and 2) the rapid and marked atrophy that defines this model of muscle inactivity is likely the result of multifactorial processes affecting transcription, translation and protein degradation.
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