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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.
The goal of this study was to use the model of spinal cord isolation (SI), which blocks nearly all neuromuscular activity while leaving the motoneuron-muscle fiber connections intact, to characterize the cellular processes linked to marked muscle atrophy. Rats randomly assigned to normal control and SI groups were studied at 0, 2, 4, 8, and 15 days after SI surgery. The slow soleus muscle atrophied by ~50%, with the greatest degree of loss occurring during the first 8 days. Throughout the SI duration, muscle protein concentration was maintained at the control level, while myofibrillar protein concentration steadily decreased between 4 and 15 days of SI, and this was associated with a 50% decrease in myosin heavy chain (MHC) normalized to total protein. Actin relative to the total protein was maintained at the control level. Marked reductions occurred in total RNA and DNA content, and in total MHC and actin mRNA expressed relative to 18S ribosomal RNA. These findings suggest that two key factors contributing to the muscle atrophy in the SI model are 1) a reduction in ribosomal ribosomal RNA that is consistent with a reduction in protein translational capacity, and 2) insufficient mRNA substrate for translating key sarcomeric proteins comprising the myofibril fraction, such as MHC and actin. In addition, the marked selective depletion of MHC protein in the muscles of SI rats suggests that this protein is more vulnerable to inactivity than actin protein. This selective MHC loss could be a major contributor for the previously reported loss in the functional integrity of SI muscles. Collectively, these data are consistent with the involvement of pretranslational and translational processes in muscle atrophy due to SI.
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