The proteomic profile of the human myotendinous junction
Research output: Contribution to journal › Journal article › Research › peer-review
Documents
- Fulltext
Final published version, 3.05 MB, PDF document
Summary 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.
Original language | English |
---|---|
Journal | iScience |
Volume | 25 |
Issue number | 2 |
Number of pages | 19 |
ISSN | 2589-0042 |
DOIs | |
Publication status | Published - 2022 |
- Skeletal muscle injury, strain injury, myofiber domain, myotendinous junction, musculotendinous, tendon, LCMS, proteomics, proteome, human
Research areas
Number of downloads are based on statistics from Google Scholar and www.ku.dk
No data available
ID: 290959707