The proteomic profile of the human myotendinous junction

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The proteomic profile of the human myotendinous junction. / Karlsen, Anders; Gonzalez-Franquesa, Alba; Jakobsen, Jens R.; Krogsgaard, Michael R.; Koch, Manuel; Kjaer, Michael; Schiaffino, Stefano; Mackey, Abigail L.; Deshmukh, Atul S.

In: iScience, Vol. 25, No. 2, 2022.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Karlsen, A, Gonzalez-Franquesa, A, Jakobsen, JR, Krogsgaard, MR, Koch, M, Kjaer, M, Schiaffino, S, Mackey, AL & Deshmukh, AS 2022, 'The proteomic profile of the human myotendinous junction', iScience, vol. 25, no. 2. https://doi.org/10.1016/j.isci.2022.103836

APA

Karlsen, A., Gonzalez-Franquesa, A., Jakobsen, J. R., Krogsgaard, M. R., Koch, M., Kjaer, M., Schiaffino, S., Mackey, A. L., & Deshmukh, A. S. (2022). The proteomic profile of the human myotendinous junction. iScience, 25(2). https://doi.org/10.1016/j.isci.2022.103836

Vancouver

Karlsen A, Gonzalez-Franquesa A, Jakobsen JR, Krogsgaard MR, Koch M, Kjaer M et al. The proteomic profile of the human myotendinous junction. iScience. 2022;25(2). https://doi.org/10.1016/j.isci.2022.103836

Author

Karlsen, Anders ; Gonzalez-Franquesa, Alba ; Jakobsen, Jens R. ; Krogsgaard, Michael R. ; Koch, Manuel ; Kjaer, Michael ; Schiaffino, Stefano ; Mackey, Abigail L. ; Deshmukh, Atul S. / The proteomic profile of the human myotendinous junction. In: iScience. 2022 ; Vol. 25, No. 2.

Bibtex

@article{2af524a495a54683a0bf34e3cad111d7,
title = "The proteomic profile of the human myotendinous junction",
abstract = "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.",
keywords = "Skeletal muscle injury, strain injury, myofiber domain, myotendinous junction, musculotendinous, tendon, LCMS, proteomics, proteome, human",
author = "Anders Karlsen and Alba Gonzalez-Franquesa and Jakobsen, {Jens R.} and Krogsgaard, {Michael R.} and Manuel Koch and Michael Kjaer and Stefano Schiaffino and Mackey, {Abigail L.} and Deshmukh, {Atul S.}",
year = "2022",
doi = "10.1016/j.isci.2022.103836",
language = "English",
volume = "25",
journal = "iScience",
issn = "2589-0042",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - The proteomic profile of the human myotendinous junction

AU - Karlsen, Anders

AU - Gonzalez-Franquesa, Alba

AU - Jakobsen, Jens R.

AU - Krogsgaard, Michael R.

AU - Koch, Manuel

AU - Kjaer, Michael

AU - Schiaffino, Stefano

AU - Mackey, Abigail L.

AU - Deshmukh, Atul S.

PY - 2022

Y1 - 2022

N2 - 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.

AB - 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.

KW - Skeletal muscle injury

KW - strain injury

KW - myofiber domain

KW - myotendinous junction

KW - musculotendinous

KW - tendon

KW - LCMS

KW - proteomics

KW - proteome

KW - human

U2 - 10.1016/j.isci.2022.103836

DO - 10.1016/j.isci.2022.103836

M3 - Journal article

C2 - 35198892

VL - 25

JO - iScience

JF - iScience

SN - 2589-0042

IS - 2

ER -

ID: 290959707