Analysis by two-dimensional Blue Native/SDS-PAGE of membrane protein alterations in rat soleus muscle after hindlimb unloading

2010 ◽  
Vol 110 (6) ◽  
pp. 1215-1224 ◽  
Author(s):  
Davide Basco ◽  
Grazia Paola Nicchia ◽  
Jean-François Desaphy ◽  
Diana Conte Camerino ◽  
Antonio Frigeri ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Soleus Muscle ◽  
Hindlimb Unloading ◽  
Two Dimensional ◽  
Sds Page ◽  
Rat Soleus Muscle ◽  
Protein Alterations ◽  
Blue Native

scholarly journals Sex differences in forkhead box O3a signaling response to hindlimb unloading in rat soleus muscle

2018 ◽  
Vol 69 (2) ◽  
pp. 235-244 ◽  
Author(s):  
Toshinori Yoshihara ◽  
Toshiharu Natsume ◽  
Takamasa Tsuzuki ◽  
Shuo-wen Chang ◽  
Ryo Kakigi ◽  
...  
Keyword(s):  
Sex Differences ◽  
Soleus Muscle ◽  
Hindlimb Unloading ◽  
Forkhead Box ◽  
Rat Soleus Muscle ◽  
Forkhead Box O3a

scholarly journals Effect of L-Arginine on Titin Expression in Rat Soleus Muscle After Hindlimb Unloading

2019 ◽  
Vol 10 ◽  
Author(s):  
Anna Ulanova ◽  
Yuliya Gritsyna ◽  
Nikolai Salmov ◽  
Yuliya Lomonosova ◽  
Svetlana Belova ◽  
...  
Keyword(s):  
Soleus Muscle ◽  
Hindlimb Unloading ◽  
Rat Soleus Muscle

Time-dependent changes in expression of troponin subunit isoforms in unloaded rat soleus muscle

2002 ◽  
Vol 282 (5) ◽  
pp. C1025-C1030 ◽  
Author(s):  
Laurence Stevens ◽  
Bruno Bastide ◽  
Philippe Kischel ◽  
Dirk Pette ◽  
Yvonne Mounier
Keyword(s):  
Soleus Muscle ◽  
Troponin I ◽  
Troponin T ◽  
Hindlimb Unloading ◽  
Heavy Chains ◽  
Mechanical Unloading ◽  
Fast Myosin ◽  
Rat Soleus Muscle ◽  
Subunit Isoforms ◽  
Time Courses

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.

Two-dimensional blue native/SDS-PAGE analysis of whole cell lysate protein complexes of rice in response to salt stress

2016 ◽  
Vol 200 ◽  
pp. 90-101 ◽  
Author(s):  
Amenehsadat Hashemi ◽  
Javad Gharechahi ◽  
Ghorbanali Nematzadeh ◽  
Faezeh Shekari ◽  
Seyed Abdollah Hosseini ◽  
...  
Keyword(s):  
Salt Stress ◽  
Protein Complexes ◽  
Two Dimensional ◽  
Whole Cell ◽  
Whole Cell Lysate ◽  
Cell Lysate ◽  
Sds Page ◽  
Blue Native
Sign in / Sign up

Export Citation Format

Share Document