scholarly journals NO-Dependent Mechanisms of Myosin Heavy Chain Transcription Regulation in Rat Soleus Muscle After 7-Days Hindlimb Unloading

2020 ◽  
Vol 11 ◽  
Author(s):  
Kristina A. Sharlo ◽  
Inna I. Paramonova ◽  
Irina D. Lvova ◽  
Natalia A. Vilchinskaya ◽  
Anna E. Bugrova ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Transcription Regulation ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
Hindlimb Unloading ◽  
Rat Soleus Muscle

Distribution of myosin heavy chain isoforms in non-weight-bearing rat soleus muscle fibers

1996 ◽  
Vol 81 (6) ◽  
pp. 2540-2546 ◽  
Author(s):  
Robert J. Talmadge ◽  
Roland R. Roy ◽  
V. Reggie Edgerton
Keyword(s):  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
De Novo ◽  
Weight Bearing ◽  
Muscle Fibers ◽  
Myosin Heavy Chain Isoforms ◽  
Hindlimb Suspension ◽  
Type I ◽  
Rat Soleus Muscle

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.

Recovery of the soleus muscle after short- and long-term disuse induced by hindlimb unloading: effects on the electrical properties and myosin heavy chain profile

2005 ◽  
Vol 18 (2) ◽  
pp. 356-365 ◽  
Author(s):  
Jean-François Desaphy ◽  
Sabata Pierno ◽  
Antonella Liantonio ◽  
Annamaria De Luca ◽  
M. Paola Didonna ◽  
...  
Keyword(s):  
Electrical Properties ◽  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
Hindlimb Unloading ◽  
Short And Long Term

scholarly journals Changes in myosin heavy chain mRNA and protein isoforms in single fibers of unloaded rat soleus muscle

FEBS Letters ◽  
1999 ◽  
Vol 463 (1-2) ◽  
pp. 15-18 ◽  
Author(s):  
Laurence Stevens ◽  
Bärbel Gohlsch ◽  
Yvonne Mounier ◽  
Dirk Pette
Keyword(s):  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
Protein Isoforms ◽  
Single Fibers ◽  
Rat Soleus Muscle

Passive tension of rat skeletal soleus muscle fibers: effects of unloading conditions

2002 ◽  
Vol 92 (4) ◽  
pp. 1465-1472 ◽  
Author(s):  
Thierry Toursel ◽  
Laurence Stevens ◽  
Henk Granzier ◽  
Yvonne Mounier
Keyword(s):  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
Muscle Fibers ◽  
Thick Filament ◽  
Muscle Stiffness ◽  
Hindlimb Unloading ◽  
Passive Tension ◽  
Tension Development ◽  
Isoform Expression

In this work we studied changes in passive elastic properties of rat soleus muscle fibers subjected to 14 days of hindlimb unloading (HU). For this purpose, we investigated the titin isoform expression in soleus muscles, passive tension-fiber strain relationships of single fibers, and the effects of the thick filament depolymerization on passive tension development. The myosin heavy chain composition was also measured for all fibers studied. Despite a slow-to-fast transformation of the soleus muscles on the basis of their myosin heavy chain content, no modification in the titin isoform expression was detected after 14 days of HU. However, the passive tension-fiber strain relationships revealed that passive tension of both slow and fast HU soleus fibers increased less steeply with sarcomere length than that of control fibers. Gel analysis suggested that this result could be explained by a decrease in the amount of titin in soleus muscle after HU. Furthermore, the thick filament depolymerization was found to similarly decrease passive tension in control and HU soleus fibers. Taken together, these results suggested that HU did not change titin isoform expression in the soleus muscle, but rather modified muscle stiffness by decreasing the amount of titin.

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
Keyword(s):  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
Muscle Fibres ◽  
The Core ◽  
Rat Soleus Muscle ◽  
Hybridization In Situ

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.

Prominence of myosin heavy chain hybrid fibers in soleus muscle of spinal cord-transected rats

1995 ◽  
Vol 78 (4) ◽  
pp. 1256-1265 ◽  
Author(s):  
R. J. Talmadge ◽  
R. R. Roy ◽  
V. R. Edgerton
Keyword(s):  
Spinal Cord ◽  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
Type I ◽  
Type Ii ◽  
Hybrid Fibers ◽  
Normal Complement ◽  
Adult Rat ◽  
Rat Soleus Muscle

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.

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