scholarly journals Effects of gravitational hindlimb unloading and plantar mechanical stimulation on calcineurin/NFATc1 signaling pathway and slow myosin expression in rat soleus muscle

2018 ◽  
Vol 9 ◽  
Author(s):  
Christina Sharlo ◽  
Olga Turtikova ◽  
Inna Paramonova ◽  
Boris Shenkman
2018 ◽  
Vol 69 (2) ◽  
pp. 235-244 ◽  
Author(s):  
Toshinori Yoshihara ◽  
Toshiharu Natsume ◽  
Takamasa Tsuzuki ◽  
Shuo-wen Chang ◽  
Ryo Kakigi ◽  
...  

2019 ◽  
Vol 10 ◽  
Author(s):  
Anna Ulanova ◽  
Yuliya Gritsyna ◽  
Nikolai Salmov ◽  
Yuliya Lomonosova ◽  
Svetlana Belova ◽  
...  

2010 ◽  
Vol 110 (6) ◽  
pp. 1215-1224 ◽  
Author(s):  
Davide Basco ◽  
Grazia Paola Nicchia ◽  
Jean-François Desaphy ◽  
Diana Conte Camerino ◽  
Antonio Frigeri ◽  
...  

2002 ◽  
Vol 282 (5) ◽  
pp. C1025-C1030 ◽  
Author(s):  
Laurence Stevens ◽  
Bruno Bastide ◽  
Philippe Kischel ◽  
Dirk Pette ◽  
Yvonne Mounier

This study focuses on the effects of mechanical unloading of rat soleus muscle on the isoform patterns of the three troponin (Tn) subunits: troponin T (TnT), troponin I (TnI), and troponin C (TnC). Mechanical unloading was achieved by hindlimb unloading (HU) for time periods of 7, 15, and 28 days. Relative concentrations of slow and fast TnT, TnI, and TnC isoforms were assessed by electrophoretic and immunoblot analyses. HU induced profound slow-to-fast isoform transitions of all Tn subunits, although to different extents and with different time courses. The effectiveness of the isoform transitions was higher for TnT than for TnI and TnC. Indeed, TnI and TnC encompassed minor partial exchanges of slow isoforms with their fast counterparts, whereas the expression pattern of fast TnT isoforms (TnTf) was largely increased after HU. Moreover, slow and fast isoforms of the different Tn were not affected in the same manner by HU. This suggests that the slow and fast counterparts of the Tn subunit isoforms are regulated independently in response to HU. The changes in TnTf composition occurred in parallel with previously demonstrated transitions within the pattern of the fast myosin heavy chains in the same muscles.


2013 ◽  
Vol 89 (3) ◽  
pp. 220-227 ◽  
Author(s):  
Y Kanazawa ◽  
K Maekawa ◽  
Y Okumura ◽  
N Fujita ◽  
H Fujino

2019 ◽  
Vol 75 (4) ◽  
pp. 585-595
Author(s):  
Toshinori Yoshihara ◽  
Shuo-wen Chang ◽  
Takamasa Tsuzuki ◽  
Toshiharu Natsume ◽  
Ryo Kakigi ◽  
...  

2016 ◽  
Vol 39 (3) ◽  
pp. 1011-1020 ◽  
Author(s):  
Timur Mirzoev ◽  
Sergey Tyganov ◽  
Natalia Vilchinskaya ◽  
Yulia Lomonosova ◽  
Boris Shenkman

Background/Aims: The purpose of the study was to assess the amount of rRNA and phosphorylation status of the key markers of mTORC1-dependent (70s6k, 4E-BP1) and mTORC1-independent (GSK-3β, AMPK) signaling pathways controlling protein synthesis in rat soleus during early stages of mechanical unloading (hindlimb suspension (HS) for 1-, 3- and 7 days). Methods: The content of the key signaling molecules of various anabolic signaling pathways was determined by Western-blotting. The amount of 28S rRNA was evaluated by RT-PCR. The rate of protein synthesis was assessed using in-vivo SUnSET technique. Results: HS for 3 and 7 days induced a significant (p<0.05) decrease in the rate of global protein synthesis in soleus muscle in comparison with control. HS within 24 hours resulted in a significant (p<0.05) decrease in p-4E-BP1 content, p-AMPK content and increase in p-p70s6k content in rat soleus muscle. Following three days of HS the content of p-AKT was decreased (p<0.05). After 7 days of HS the phosphorylation level of AKT and GSK-3beta was significantly reduced (p<0.05) compared to control. We also observed a significant decrease in the amount of 28S rRNA in rat soleus following 1, 3 and 7 days of HS. Conclusion: Taken together, the results of our study suggest that a decline in the global rate of protein synthesis in rat soleus during early stages of simulated microgravity is associated with impaired ribosome biogenesis as well as reduced activity of mTORC1-independent signaling pathways.


Sign in / Sign up

Export Citation Format

Share Document