The proteomic profile of the human myotendinous junction

iScience

Alba Gonzalez-Franquesa¹  Atul S. Deshmukh¹  Stefano Schiaffino²  Michael Kjaer³  Abigail L. Mackey⁴  Anders Karlsen⁴  Jens R. Jakobsen⁵  Manuel Koch⁶  Michael R. Krogsgaard⁶ 

[1] Center for Healthy Aging, Department of Clinical Medicine, University of Copenhagen, Copenhagen, Denmark;Center for Molecular Medicine Cologne (CMMC), Faculty of Medicine and University Hospital Cologne, University of Cologne, Cologne, Germany;Institute for Dental Research and Oral Musculoskeletal Biology, Center for Biochemistry, Faculty of Medicine and University Hospital Cologne, University of Cologne, Cologne, Germany;Institute of Sports Medicine Copenhagen, Department of Orthopedic Surgery, Copenhagen University Hospital-Bispebjerg and Frederiksberg, Denmark and Part of IOC Research Center, Copenhagen, Denmark;Novo Nordisk Foundation Center for Basic Metabolic Research, University of Copenhagen, Copenhagen, Denmark;Section for Sports Traumatology M51, Department of Orthopedic Surgery, Copenhagen University Hospital-Bispebjerg and Frederiksberg, Denmark and Part of IOC Research Center, Copenhagen, Denmark;

关键词: Biology experimental methods;    Molecular physiology;    Musculoskeletal anatomy;    Proteomics;   

DOI  :  

来源: DOAJ

【 摘 要 】

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.

【 授权许可】

Unknown