scholarly journals Myosin heavy-chain mRNA is present in both myofibrillar and subsarcolemmal regions of muscle fibres

1991 ◽  
Vol 279 (1) ◽  
pp. 309-310 ◽  
Author(s):  
J Hesketh ◽  
G Campbell ◽  
N Loveridge

Hybridization in situ with riboprobes to the myosin heavy-chain slow isoform showed that, in the rat soleus muscle, the myosin heavy-chain mRNA was distributed throughout the myofibres. There was greater density of autoradiographic grains in the subsarcolemmal regions of the fibres, but there was also a considerable number of grains in the core myofibrillar region of the fibres. Microdensitometry showed that the grain density in the myofibrillar region was approximately half that in the subsarcolemmal rim; this would correspond to some 70% of the mRNA being present in the myofibrillar region. The results are consistent with the hypothesis that myosin is synthesized on polyribosomes present in the intermyofibrillar cytoplasm.

1996 ◽  
Vol 81 (6) ◽  
pp. 2540-2546 ◽  
Author(s):  
Robert J. Talmadge ◽  
Roland R. Roy ◽  
V. Reggie Edgerton

Talmadge, Robert J., Roland R. Roy, and V. Reggie Edgerton.Distribution of myosin heavy chain isoforms in non-weight-bearing rat soleus muscle fibers. J. Appl. Physiol. 81(6): 2540–2546, 1996.—The effects of 14 days of spaceflight (SF) or hindlimb suspension (HS) (Cosmos 2044) on myosin heavy chain (MHC) isoform content of the rat soleus muscle and single muscle fibers were determined. On the basis of electrophoretic analyses, there was a de novo synthesis of type IIx MHC but no change in either type I or IIa MHC isoform proportions after either SF or HS compared with controls. The percentage of fibers containing only type I MHC decreased by 26 and 23%, and the percentage of fibers with multiple MHCs increased from 6% in controls to 32% in HS and 34% in SF rats. Type IIx MHC was always found in combination with another MHC or combination of MHCs; i.e., no fibers contained type IIx MHC exclusively. These data suggest that the expression of the normal complement of MHC isoforms in the adult rat soleus muscle is dependent, in part, on normal weight bearing and that the absence of weight bearing induces a shift toward type IIx MHC protein expression in the preexisting type I and IIa fibers of the soleus.


FEBS Letters ◽  
1999 ◽  
Vol 463 (1-2) ◽  
pp. 15-18 ◽  
Author(s):  
Laurence Stevens ◽  
Bärbel Gohlsch ◽  
Yvonne Mounier ◽  
Dirk Pette

1995 ◽  
Vol 78 (4) ◽  
pp. 1256-1265 ◽  
Author(s):  
R. J. Talmadge ◽  
R. R. Roy ◽  
V. R. Edgerton

The effect of a midthoracic spinal cord transection (ST) on myosin heavy chain (MHC) isoform expression in the rat soleus muscle was studied. Electrophoretic analyses demonstrated that 15 days after ST there were significant proportional increases in type IIx, decreases in type IIa, and no change in type I MHC composition. Thirty days after ST, some type IIb MHC was expressed, there were further proportional increases in type IIx, an increase in type IIa (compared with 15-day ST), and a decrease in type I MHC. At both time periods after ST, many fibers expressed multiple MHCs, as demonstrated by immunohistochemistry where a battery of monoclonal antibodies specific to MHC isoforms was used. Fibers were observed containing types I and II together or multiple type II MHC isoforms. These data suggest that the expression of the normal complement of MHC isoforms in the adult rat soleus muscle is dependent, in part, on normal neuromuscular activation.


2020 ◽  
Vol 11 ◽  
Author(s):  
Kristina A. Sharlo ◽  
Inna I. Paramonova ◽  
Irina D. Lvova ◽  
Natalia A. Vilchinskaya ◽  
Anna E. Bugrova ◽  
...  

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