Immunohistochemical studies on regulation of alternative splicing of fast skeletal muscle troponin T: non-uniform distribution of the exon x3 epitope in a single muscle fiber

2000 ◽  
Vol 299 (2) ◽  
pp. 263-271 ◽  
Author(s):  
Kazuto Nakada ◽  
Fuminori Kimura ◽  
Tamio Hirabayashi ◽  
Jun-Ichi Miyazaki
2009 ◽  
Vol 39 (3) ◽  
pp. 141-159 ◽  
Author(s):  
Varuna C. Banduseela ◽  
Julien Ochala ◽  
Yi-Wen Chen ◽  
Hanna Göransson ◽  
Holly Norman ◽  
...  

Skeletal muscle wasting and impaired muscle function in response to mechanical ventilation and immobilization in intensive care unit (ICU) patients are clinically challenging partly due to 1) the poorly understood intricate cellular and molecular networks and 2) the unavailability of an animal model mimicking this condition. By employing a unique porcine model mimicking the conditions in the ICU with long-term mechanical ventilation and immobilization, we have analyzed the expression profile of skeletal muscle biopsies taken at three time points during a 5-day period. Among the differentially regulated transcripts, extracellular matrix, energy metabolism, sarcomeric and LIM protein mRNA levels were downregulated, while ubiquitin proteasome system, cathepsins, oxidative stress responsive genes and heat shock proteins (HSP) mRNAs were upregulated. Despite 5 days of immobilization and mechanical ventilation single muscle fiber cross-sectional areas as well as the maximum force generating capacity at the single muscle fiber level were preserved. It is proposed that HSP induction in skeletal muscle is an inherent, primary, but temporary protective mechanism against protein degradation. To our knowledge, this is the first study that isolates the effect of immobilization and mechanical ventilation in an ICU condition from various other cofactors.


Cell Reports ◽  
2017 ◽  
Vol 19 (11) ◽  
pp. 2396-2409 ◽  
Author(s):  
Marta Murgia ◽  
Luana Toniolo ◽  
Nagarjuna Nagaraj ◽  
Stefano Ciciliot ◽  
Vincenzo Vindigni ◽  
...  

1994 ◽  
Vol 17 (11) ◽  
pp. 1301-1307 ◽  
Author(s):  
Daniel Dumitru ◽  
John C. King ◽  
William van der Rijt ◽  
Dick F. Stegeman

1982 ◽  
Vol 76 (1) ◽  
pp. 12-24 ◽  
Author(s):  
A. Gydikov ◽  
P. Gatev ◽  
G.V. Dimitrov ◽  
L. Gerilovsky

2009 ◽  
Vol 39 (1) ◽  
pp. 3-9 ◽  
Author(s):  
Lisa S. Krivickas ◽  
Ronan Walsh ◽  
Anthony A. Amato

2005 ◽  
Vol 26 (5) ◽  
pp. 339-343 ◽  
Author(s):  
U. Raue ◽  
B. Terpstra ◽  
D. L. Williamson ◽  
P. M. Gallagher ◽  
S. W. Trappe

2000 ◽  
Vol 279 (4) ◽  
pp. C1067-C1077 ◽  
Author(s):  
Jian-Ping Jin ◽  
Aihua Chen ◽  
Ozgur Ogut ◽  
Qi-Quan Huang

Troponin T (TnT) is an essential element in the thin filament Ca2+-regulatory system controlling striated muscle contraction. Alternative RNA splicing generates developmental and muscle type-specific TnT isoforms differing in the hypervariable NH2-terminal region. Using avian fast skeletal muscle TnT containing a metal-binding segment, we have demonstrated a role of the NH2-terminal domain in modulating the conformation of TnT (Wang J and Jin JP. Biochemistry 37: 14519–14528, 1998). To further investigate the structure-function relationship of TnT, the present study constructed and characterized a recombinant protein in which the metal-binding peptide present in avian fast skeletal muscle TnT was fused to the NH2 terminus of mouse slow skeletal muscle TnT. Metal ion or monoclonal antibody binding to the NH2-terminal extension induced conformational changes in other domains of the model TnT molecule. This was shown by the altered affinity to a monoclonal antibody against the COOH-terminal region and a polyclonal antiserum recognizing multiple epitopes. Protein binding assays showed that metal binding to the NH2-terminal extension had effects on the interaction of TnT with troponin I, troponin C, and most significantly, tropomyosin. The data indicate that the NH2-terminal Tx [4–7 repeats of a sequence motif His-(Glu/Ala)-Glu-Ala-His] extension confers a specific conformational modulation in the slow skeletal muscle TnT.


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