Spatial proteomics of skeletal muscle using thin cryosections reveals metabolic adaptation at the muscle-tendon transition zone
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Spatial proteomics of skeletal muscle using thin cryosections reveals metabolic adaptation at the muscle-tendon transition zone. / Schmidt, Luisa; Saynisch, Michael; Hoegsbjerg, Christian; Schmidt, Andreas; Mackey, Abigail; Lackmann, Jan Wilm; Müller, Stefan; Koch, Manuel; Brachvogel, Bent; Kjaer, Michael; Antczak, Philipp; Krüger, Marcus.
I: Cell Reports, Bind 43, Nr. 7, 114374, 2024.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - Spatial proteomics of skeletal muscle using thin cryosections reveals metabolic adaptation at the muscle-tendon transition zone
AU - Schmidt, Luisa
AU - Saynisch, Michael
AU - Hoegsbjerg, Christian
AU - Schmidt, Andreas
AU - Mackey, Abigail
AU - Lackmann, Jan Wilm
AU - Müller, Stefan
AU - Koch, Manuel
AU - Brachvogel, Bent
AU - Kjaer, Michael
AU - Antczak, Philipp
AU - Krüger, Marcus
N1 - Publisher Copyright: © 2024 The Author(s)
PY - 2024
Y1 - 2024
N2 - Morphological studies of skeletal muscle tissue provide insights into the architecture of muscle fibers, the surrounding cells, and the extracellular matrix (ECM). However, a spatial proteomics analysis of the skeletal muscle including the muscle-tendon transition zone is lacking. Here, we prepare cryotome muscle sections of the mouse soleus muscle and measure each slice using short liquid chromatography-mass spectrometry (LC-MS) gradients. We generate 3,000 high-resolution protein profiles that serve as the basis for a network analysis to reveal the complex architecture of the muscle-tendon junction. Among the protein profiles that increase from muscle to tendon, we find proteins related to neuronal activity, fatty acid biosynthesis, and the renin-angiotensin system (RAS). Blocking the RAS in cultured mouse tenocytes using losartan reduces the ECM synthesis. Overall, our analysis of thin cryotome sections provides a spatial proteome of skeletal muscle and reveals that the RAS acts as an additional regulator of the matrix within muscle-tendon junctions.
AB - Morphological studies of skeletal muscle tissue provide insights into the architecture of muscle fibers, the surrounding cells, and the extracellular matrix (ECM). However, a spatial proteomics analysis of the skeletal muscle including the muscle-tendon transition zone is lacking. Here, we prepare cryotome muscle sections of the mouse soleus muscle and measure each slice using short liquid chromatography-mass spectrometry (LC-MS) gradients. We generate 3,000 high-resolution protein profiles that serve as the basis for a network analysis to reveal the complex architecture of the muscle-tendon junction. Among the protein profiles that increase from muscle to tendon, we find proteins related to neuronal activity, fatty acid biosynthesis, and the renin-angiotensin system (RAS). Blocking the RAS in cultured mouse tenocytes using losartan reduces the ECM synthesis. Overall, our analysis of thin cryotome sections provides a spatial proteome of skeletal muscle and reveals that the RAS acts as an additional regulator of the matrix within muscle-tendon junctions.
KW - CP: Metabolism
KW - distance-based network
KW - myotendinous junction
KW - skeletal muscle
KW - spatial proteomics
U2 - 10.1016/j.celrep.2024.114374
DO - 10.1016/j.celrep.2024.114374
M3 - Journal article
C2 - 38900641
AN - SCOPUS:85196156521
VL - 43
JO - Cell Reports
JF - Cell Reports
SN - 2211-1247
IS - 7
M1 - 114374
ER -
ID: 396993805