The proteomic profile of the human myotendinous junction.
Biology experimental methods
Molecular physiology
Musculoskeletal anatomy
Proteomics
Journal
iScience
ISSN: 2589-0042
Titre abrégé: iScience
Pays: United States
ID NLM: 101724038
Informations de publication
Date de publication:
18 Feb 2022
18 Feb 2022
Historique:
received:
01
12
2021
revised:
12
01
2022
accepted:
24
01
2022
entrez:
24
2
2022
pubmed:
25
2
2022
medline:
25
2
2022
Statut:
epublish
Résumé
Proteomics analysis of skeletal muscle has recently progressed from whole muscle tissue to single myofibers. Here, we further focus on a specific myofiber domain crucial for force transmission from muscle to tendon, the myotendinous junction (MTJ). To overcome the anatomical constraints preventing the isolation of pure MTJs, we performed in-depth analysis of the MTJ by progressive removal of the muscle component in semitendinosus muscle-tendon samples. Using detergents with increasing stringency, we quantified >3000 proteins across all samples, and identified 112 significantly enriched MTJ proteins, including 24 known MTJ-enriched proteins. Of the 88 novel MTJ markers, immunofluorescence analysis confirmed the presence of tetraspanin-24 (CD151), kindlin-2 (FERMT2), cartilage intermediate layer protein 1 (CILP), and integrin-alpha10 (ITGA10), at the human MTJ. Together, these human data constitute the first detailed MTJ proteomics resource that will contribute to advance understanding of the biology of the MTJ and its failure in pathological conditions.
Identifiants
pubmed: 35198892
doi: 10.1016/j.isci.2022.103836
pii: S2589-0042(22)00106-7
pmc: PMC8851264
doi:
Types de publication
Journal Article
Langues
eng
Pagination
103836Informations de copyright
© 2022 The Author(s).
Déclaration de conflit d'intérêts
The authors declare no conflicts of interest.
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