TY - JOUR
T1 - Reduced ATP turnover during hibernation in relaxed skeletal muscle
AU - De Napoli, Cosimo
AU - Schmidt, Luisa
AU - Montesel, Mauro
AU - Cussonneau, Laura
AU - Sanniti, Samuele
AU - Marcucci, Lorenzo
AU - Germinario, Elena
AU - Kindberg, Jonas
AU - Evans, Alina Lynn
AU - Gauquelin-Koch, Guillemette
AU - Narici, Marco
AU - Bertile, Fabrice
AU - Lefai, Etienne
AU - Krüger, Marcus
AU - Nogara, Leonardo
AU - Blaauw, Bert
N1 - Publisher Copyright:
© The Author(s) 2024.
PY - 2025/12
Y1 - 2025/12
N2 - Hibernating brown bears, due to a drastic reduction in metabolic rate, show only moderate muscle wasting. Here, we evaluate if ATPase activity of resting skeletal muscle myosin can contribute to this energy sparing. By analyzing single muscle fibers taken from the same bears, either during hibernation or in summer, we find that fibers from hibernating bears have a mild decline in force production and a significant reduction in ATPase activity. Single fiber proteomics, western blotting, and immunohistochemical analyses reveal major remodeling of the mitochondrial proteome during hibernation. Furthermore, using bioinformatical approaches and western blotting we find that phosphorylated myosin light chain, a known stimulator of basal myosin ATPase activity, is decreased in hibernating and disused muscles. These results suggest that skeletal muscle limits energy loss by reducing myosin ATPase activity, indicating a possible role for myosin ATPase activity modulation in multiple muscle wasting conditions.
AB - Hibernating brown bears, due to a drastic reduction in metabolic rate, show only moderate muscle wasting. Here, we evaluate if ATPase activity of resting skeletal muscle myosin can contribute to this energy sparing. By analyzing single muscle fibers taken from the same bears, either during hibernation or in summer, we find that fibers from hibernating bears have a mild decline in force production and a significant reduction in ATPase activity. Single fiber proteomics, western blotting, and immunohistochemical analyses reveal major remodeling of the mitochondrial proteome during hibernation. Furthermore, using bioinformatical approaches and western blotting we find that phosphorylated myosin light chain, a known stimulator of basal myosin ATPase activity, is decreased in hibernating and disused muscles. These results suggest that skeletal muscle limits energy loss by reducing myosin ATPase activity, indicating a possible role for myosin ATPase activity modulation in multiple muscle wasting conditions.
UR - http://www.scopus.com/inward/record.url?scp=85213836182&partnerID=8YFLogxK
U2 - 10.1038/s41467-024-55565-4
DO - 10.1038/s41467-024-55565-4
M3 - Article
AN - SCOPUS:85213836182
SN - 2041-1723
VL - 16
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 80
ER -