ArticlePloS one2016
Denervation-Induced Activation of the Standard Proteasome and Immunoproteasome.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 16 citations in OpenAlex.
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- Shikonin Induces Glioma Necroptosis, Stemness Decline, and Impedes (Immuno)Proteasome Activity.Stem cells international · 2024Article
- Diet-induced obesity augments ischemic myopathy and functional decline in a murine model of peripheral artery disease.Translational research : the journal of laboratory and clinical medicine · 2023Article
- Skeletal Muscle Denervation: Sciatic and Tibial Nerve Transection Technique.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Immunoproteasome Inhibition Ameliorates Aged Dystrophic Mouse Muscle Environment.International journal of molecular sciences · 2022Article
- Growth hormone secretagogue receptor-1a mediates ghrelin's effects on attenuating tumour-induced loss of muscle strength but not muscle mass.Journal of cachexia, sarcopenia and muscle · 2021Article
- Out of Control: The Role of the Ubiquitin Proteasome System in Skeletal Muscle during Inflammation.Biomolecules · 2021Review
- Docosahexaenoic Acid, a Potential Treatment for Sarcopenia, Modulates the Ubiquitin-Proteasome and the Autophagy-Lysosome Systems.Nutrients · 2020Review
- Short-Term ONX-0914 Administration: Performance and Muscle Phenotype inInternational journal of environmental research and public health · 2020Article
- Skeletal muscle denervation investigations: selecting an experimental control wisely.American journal of physiology. Cell physiology · 2019Article
- Downhill exercise alters immunoproteasome content in mouse skeletal muscle.Cell stress & chaperones · 2018Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The standard 26S proteasome is responsible for the majority of myofibrillar protein degradation leading to muscle atrophy. The immunoproteasome is an inducible form of the proteasome. While its function has been linked to conditions of atrophy, its contribution to muscle proteolysis remains unclear. Therefore, the purpose of this study was to determine if the immunoproteasome plays a role in skeletal muscle atrophy induced by denervation. Adult male C57BL/6 wild type (WT) and immunoproteasome knockout lmp7-/-/mecl-1-/- (L7M1) mice underwent tibial nerve transection on the left hindlimb for either 7 or 14 days, while control mice did not undergo surgery. Proteasome activity (caspase-, chymotrypsin-, and trypsin- like), protein content of standard proteasome (β1, β5 and β2) and immunoproteasome (LMP2, LMP7 and MECL-1) catalytic subunits were determined in the gastrocnemius muscle. Denervation induced significant atrophy and was accompanied by increased activities and protein content of the catalytic subunits in both WT and L7M1 mice. Although denervation resulted in a similar degree of muscle atrophy between strains, the mice lacking two immunoproteasome subunits showed a differential response in the extent and duration of proteasome features, including activities and content of the β1, β5 and LMP2 catalytic subunits. The results indicate that immunoproteasome deficiency alters the proteasome's composition and activities. However, the immunoproteasome does not appear to be essential for muscle atrophy induced by denervation.
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