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• W1967950775 abstract "PURPOSE: The diaphragm muscle (DIAm) is the most important inspiratory muscle with a high duty cycle (∼40%) relative to limb muscles such as the soleus (∼14%) or extensor digitorum longus (∼2%). In this regard, DIAm cross-sectional area, tetanic force, and myosin heavy chain expression have been observed to be particularly sensitive to inactivity. Two distinct types of rat DIAm inactivity were investigated in this study, namely spinal isolation (SI) by hemisection of the spinal cord at C2 and unilateral phrenic nerve denervation (DNV). With SI, excitatory respiratory drive to the phrenic motor neurons is absent resulting in muscle paralysis. With DNV, there is a complete neuromuscular disruption resulting in muscle paralysis. In both cases, the diaphragm is mechanically unloaded and not mediating contractions. Therefore, the major difference between SI and DNV is the disruption of neuromuscular interactions. The purpose of this study was to investigate the state of protein ubiquitination as an indicator of DIAm protein degradation and to elucidate whether the degree of ubiquitination varies following two different conditions of DIAm inactivity (SI versus DNV). METHODS: Sprague-Dawley rats underwent SI, DNV, or sham surgery. DIAm was removed at three, seven, or fourteen days post surgery, homogenized, and protein analyzed by SDS-PAGE and immunoblotting techniques. Metamorph software was used to quantitate proteins immunoreacting with ubiquitin-specific antibodies. RESULTS: DIAm protein ubiquitination increased following DNV surgery. Compared to sham-treated animals, ubiquitination increased approximately four, ten, and seven-fold following three, seven, or fourteen days of DIAm DNV. In contrast, there was no apparent change in protein ubiquitination following SI at each of the three times points analyzed. CONCLUSIONS: The findings in this study are consistent with prior reports that DIAm cross-sectional area, tetanic force, and myosin heavy chain expression significantly decrease acutely following DNV, but do not significantly decrease following SI. This observation further emphasizes the critical role of neuromuscular interactions for DIAm homeostasis beyond maintenance by mechanical contraction per se. We hypothesize that neuromuscular interactions, such as trophic factor signaling, may delay protein ubiquitination and resultant muscle deficits following acute periods of inactivity." @default.
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• W1967950775 date "2006-11-01" @default.
• W1967950775 modified "2023-10-18" @default.
• W1967950775 title "Activity-dependent Protein Ubiquitination in Diaphragm Muscle" @default.
• W1967950775 doi "https://doi.org/10.1249/00005768-200611001-00059" @default.
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