Atrogin1-induced loss of aquaporin 4 in myocytes leads to skeletal muscle atrophy.
Adult
Animals
Aquaporin 4
/ metabolism
Female
HMGB1 Protein
/ metabolism
Humans
Male
Mice
Mice, Inbred C57BL
Muscle Fibers, Skeletal
/ metabolism
Muscle Proteins
/ metabolism
Muscle, Skeletal
/ metabolism
Muscular Atrophy
/ metabolism
NF-kappa B
/ metabolism
SKP Cullin F-Box Protein Ligases
/ metabolism
Signal Transduction
Tripartite Motif Proteins
/ metabolism
Ubiquitin
/ metabolism
Ubiquitin-Protein Ligases
/ metabolism
Ubiquitination
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
25 08 2020
25 08 2020
Historique:
received:
17
02
2020
accepted:
10
08
2020
entrez:
27
8
2020
pubmed:
28
8
2020
medline:
12
1
2021
Statut:
epublish
Résumé
The water channel aquaporin 4 (AQP4) regulates the flux of water across the cell membrane, maintaining cellular homeostasis. Since AQP4 is enriched in the sarcolemma of skeletal muscle, a functional defect in AQP4 may cause skeletal muscle dysfunction. To investigate a novel mechanism underlying skeletal muscle atrophy, we examined AQP4 expression and its regulation in muscle using the rotator cuff tear (RCT) model. Human and mouse AQP4 expression was significantly decreased in atrophied muscle resulting from RCT. The size and the number of myotubes were reduced following AQP4 knockdown. Atrogin 1-mediated ubiquitination of AQP4 was verified with an ubiquitination assay after immunoprecipitation of AQP4 with an anti-AQP4 antibody. In this study, we identified high mobility group box 1 (HMGB1) as a potent upstream regulator of atrogin 1 expression. Atrogin 1 expression was increased by recombinant mouse HMGB1 protein, and the HMGB1-induced atrogin 1 expression was mediated via NF-κB signaling. Our study suggests that loss of AQP4 appears to be involved in myocyte shrinkage after RCT, and its degradation is mediated by atrogin 1-dependent ubiquitination. HMGB1, in its function as a signaling molecule upstream of the ubiquitin ligase atrogin 1, was found to be a novel regulator of muscle atrophy.
Identifiants
pubmed: 32843684
doi: 10.1038/s41598-020-71167-8
pii: 10.1038/s41598-020-71167-8
pmc: PMC7447774
doi:
Substances chimiques
Aquaporin 4
0
HMGB1 Protein
0
Muscle Proteins
0
NF-kappa B
0
Tripartite Motif Proteins
0
Ubiquitin
0
Fbxo32 protein, mouse
EC 2.3.2.27
SKP Cullin F-Box Protein Ligases
EC 2.3.2.27
Ubiquitin-Protein Ligases
EC 2.3.2.27
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
14189Références
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