Effects of hypobaric hypoxia on histochemical fibre-type composition and myosin heavy chain isoform component in the rat soleus muscle

1995 ◽  
Vol 429 (5) ◽  
pp. 601-606 ◽  
Author(s):  
Akihiko Ishihara ◽  
Kazuo Itoh ◽  
Yasuharu Oishi ◽  
Minoru Itoh ◽  
Chiyoko Hirofuji ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
Fibre Type ◽  
Hypobaric Hypoxia ◽  
Fibre Type Composition ◽  
Myosin Heavy Chain Isoform ◽  
Type Composition ◽  
Rat Soleus Muscle

Myosin heavy-chain isoform distribution, fibre-type composition and fibre size in skeletal muscle of patients on haemodialysis

2007 ◽  
Vol 41 (6) ◽  
pp. 539-545 ◽  
Author(s):  
Stig Molsted ◽  
Inge Eidemak ◽  
Helle tauby Sorensen ◽  
Jens halkjaer Kristensen ◽  
Adrian Harrison ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fibre Type ◽  
Fibre Type Composition ◽  
Myosin Heavy Chain Isoform ◽  
Fibre Size ◽  
Type Composition

Influence of 12 weeks of hypobaric hypoxia on fibre type composition of the rat soleus muscle

1995 ◽  
Vol 154 (3) ◽  
pp. 417-418 ◽  
Author(s):  
K. ITOH ◽  
M. ITOH ◽  
A. ISHIHARA ◽  
C. HIROFUJI ◽  
H. HAYASHI
Keyword(s):  
Soleus Muscle ◽  
Fibre Type ◽  
Hypobaric Hypoxia ◽  
Fibre Type Composition ◽  
Type Composition ◽  
Rat Soleus Muscle

Myosin heavy chain fibre type composition in foals: analyses at the mRNA and protein level

2006 ◽  
Vol 38 (S36) ◽  
pp. 316-321 ◽  
Author(s):  
K. EIZEMA ◽  
D. E. WAL ◽  
M. M. M. BURG ◽  
E. G. DINGBOOM ◽  
M. E. EVERTS
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Protein Level ◽  
Fibre Type ◽  
Fibre Type Composition ◽  
Type Composition

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.

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

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.

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