+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Regulation of the ubiquitin proteasome system in mechanically injured human skeletal muscle



Regulation of the ubiquitin proteasome system in mechanically injured human skeletal muscle



Physiological Research 56(2): 227-233



Metabolic consequences of direct muscle trauma are insufficiently defined. Their effects on the ubiquitin-proteasome pathway (UPP) of protein degradation in human skeletal muscles are as yet unknown. Thus, we investigated whether the UPP is involved in the metabolic response evoked in directly traumatized human skeletal muscles. Biopsies were obtained from contused muscles after fractures and from normal muscles during elective implant removal (control). As estimated by western blot analyses, concentrations of free ubiquitin and ubiquitin protein conjugates were similar in extracts from injured and uninjured muscles. Ubiquitin protein ligation rates were reduced after injury (1.5+/-0.2 vs. 1.0+/-0.15 fkat/microg; p=0.04). Chymotryptic-, tryptic- and caspase-like proteasome peptidase activities (total activity minus activity in the presence of proteasome inhibitors) increased significantly after trauma (p=0.04 - 0.001). Significant increases in total chymotryptic- and caspase-like activities were attributable to proteasome activation. Our results extend the possible role of the UPP in muscle wasting to direct muscle trauma. They further suggest that the effects of direct mechanical trauma are not limited to the proteasome and imply that ubiquitin protein ligase systems are also involved. Based on the potential role of the UPP in systemic diseases, it might also be a therapeutic target to influence muscle loss in critically ill blunt trauma patients, in which large proportions of muscle are exposed to direct trauma.

Please choose payment method:






(PDF emailed within 1 workday: $29.90)

Accession: 050151666

Download citation: RISBibTeXText

PMID: 16555940


Related references

The ubiquitin proteasome system in atrophying skeletal muscle: roles and regulation. American Journal of Physiology. Cell Physiology 311(3): C392, 2016

Regulation of the ubiquitin-proteasome system and myofibrillar protein degradation in C2C12 skeletal muscle cells. Biochemical Society Transactions 24(4): 630S, 1996

The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy. Biochimica et Biophysica Acta 1782(12): 730-743, 2008

Regulation of the catabolic ubiquitin-proteasome system in end-stage chronic heart failure: Impact of physical exercise training and association to skeletal muscle mass. 2007

The ubiquitin-proteasome system and skeletal muscle wasting. Essays in Biochemistry 41: 173-186, 2005

IGF-I has no effect on postexercise suppression of the ubiquitin-proteasome system in rat skeletal muscle. Journal of Applied Physiology 92(6): 2277-2284, 2002

Regulation of Akt-mTOR, ubiquitin-proteasome and autophagy-lysosome pathways in response to formoterol administration in rat skeletal muscle. International Journal of Biochemistry and Cell Biology 45(11): 2444-2455, 2013

Effects on the ubiquitin proteasome system after closed soft-tissue trauma in rat skeletal muscle. European Journal of Trauma and Emergency Surgery 37(6): 645-654, 2011

Activating cAMP/PKA signaling in skeletal muscle suppresses the ubiquitin-proteasome-dependent proteolysis: implications for sympathetic regulation. Journal of Applied Physiology 117(1): 11-19, 2014

Contributions of the ubiquitin-proteasome pathway and apoptosis to human skeletal muscle wasting with age. Pflugers Archiv 450(6): 437-446, 2005

Denervation-Induced Activation of the Ubiquitin-Proteasome System Reduces Skeletal Muscle Quantity Not Quality. Plos one 11(8): E0160839, 2016

Supplementation with l-carnitine downregulates genes of the ubiquitin proteasome system in the skeletal muscle and liver of piglets. Animal 6(1): 70-78, 2013

Sepsis is associated with increased mRNAs of the ubiquitin-proteasome proteolytic pathway in human skeletal muscle. Journal of Clinical Investigation 99(2): 163-168, 1997

Weight gain does not preclude activation of the ubiquitin-proteasome system in skeletal muscle of tumor-bearing mice. Proceedings of the American Association for Cancer Research Annual Meeting (41): 200, 2000

Mechanisms involved in 3',5'-cyclic adenosine monophosphate-mediated inhibition of the ubiquitin-proteasome system in skeletal muscle. Endocrinology 150(12): 5395-5404, 2009