Heterogeneity and distribution of fast myosin heavy chains in some adult vertebrate skeletal muscles

1992 ◽  
Vol 97 (4) ◽  
pp. 361-370 ◽  
Author(s):  
K. Williams ◽  
G. K. Dhoot
Keyword(s):  
Skeletal Muscles ◽  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Fast Myosin

scholarly journals Heritability of percentage of fast myosin heavy chains in skeletal muscles and relationship with performance

2010 ◽  
Vol 31 (S30) ◽  
pp. 289-292 ◽  
Author(s):  
E. BARREY ◽  
J. P. VALETTE ◽  
M. JOUGLIN ◽  
C. BLOUIN ◽  
B. LANGLOIS
Keyword(s):  
Skeletal Muscles ◽  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Fast Myosin

scholarly journals Chronic denervation of rat hemidiaphragm: maintenance of fiber heterogeneity with associated increasing uniformity of myosin isoforms.

1985 ◽  
Vol 100 (1) ◽  
pp. 161-174 ◽  
Author(s):  
U Carraro ◽  
D Morale ◽  
I Mussini ◽  
S Lucke ◽  
M Cantini ◽  
...  
Keyword(s):  
Light And Electron Microscopy ◽  
Myosin Isoforms ◽  
Myosin Heavy Chains ◽  
Denervated Muscle ◽  
Slow Myosin ◽  
Heavy Chains ◽  
Fast Myosin ◽  
Long Time ◽  
Chronic Denervation

During several months of denervation, rat mixed muscles lose slow myosin, though with variability among animals. Immunocytochemical studies showed that all the denervated fibers of the hemidiaphragm reacted with anti-fast myosin, while many reacted with anti-slow myosin as well. This has left open the question as to whether multiple forms of myosin co-exist within individual fibers or a unique, possibly embryonic, myosin is present, which shares epitopes with fast and slow myosins. Furthermore, one can ask if the reappearance of embryonic myosin in chronically denervated muscle is related both to its re-expression in the pre-existing fibers and to cell regeneration. To answer these questions we studied the myosin heavy chains from individual fibers of the denervated hemidiaphragm by SDS PAGE and morphologically searched for regenerative events in the long term denervated muscle. 3 mo after denervation the severely atrophic fibers of the hemidiaphragm showed either fast or a mixture of fast and slow myosin heavy chains. Structural analysis of proteins sequentially extracted from muscle cryostat sections showed that slow myosin was still present 16 mo after denervation, in spite of the loss of the selective distribution of fast and slow features. Therefore muscle fibers can express adult fast myosin not only when denervated during their differentiation but also after the slow program has been expressed for a long time. Light and electron microscopy showed that the long-term denervated muscle maintained a steady-state atrophy for the rat's life span. Some of the morphological features indicate that aneural regeneration events continuously occur and significantly contribute to the increasing uniformity of the myosin gene expression in long-term denervated diaphragm.

Chronic denervation of rat diaphragm: Selective maintenance of adult fast myosin heavy chains

1982 ◽  
Vol 5 (7) ◽  
pp. 515-524 ◽  
Author(s):  
Ugo Carraro ◽  
Luciano Dalla Libera ◽  
Claudia Catani ◽  
Daniela Danieli-Betto
Keyword(s):  
Myosin Heavy Chains ◽  
Rat Diaphragm ◽  
Heavy Chains ◽  
Fast Myosin ◽  
Chronic Denervation ◽  
Selective Maintenance

Comparison of the molecular, antigenic and ATPase determinants of fast myosin heavy chains in rat and human: a single-fibre study

1997 ◽  
Vol 435 (1) ◽  
pp. 151-163 ◽  
Author(s):  
J. A. A. Pereira Sant'Ana ◽  
Steven Ennion ◽  
Anthony J. Sargeant ◽  
Antoon F. M. Moorman ◽  
G. Goldspink
Keyword(s):  
Single Fibre ◽  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Fast Myosin

Seasonal changes in the isoform composition of the myosin heavy chains in skeletal muscles of hibernating ground squirrels Spermophilus undulatus

BIOPHYSICS ◽  
2012 ◽  
Vol 57 (6) ◽  
pp. 764-768 ◽  
Author(s):  
M. V. Lazareva ◽  
K. O. Trapeznikova ◽  
I. M. Vikhlyantsev ◽  
A. G. Bobylev ◽  
A. A. Klimov ◽  
...  
Keyword(s):  
Seasonal Changes ◽  
Skeletal Muscles ◽  
Ground Squirrels ◽  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Spermophilus Undulatus

Relationship between calpastatin activity and the slow and fast myosin heavy chain content of ovine skeletal muscles

2002 ◽  
Vol 2002 ◽  
pp. 173-173
Author(s):  
A.Q. Sazili ◽  
P.L. Sensky ◽  
T. Parr ◽  
R.G. Bardsley ◽  
P.J. Buttery
Keyword(s):  
Atpase Activity ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Skeletal Muscles ◽  
Myofibrillar Atpase ◽  
Heavy Chains ◽  
Fast Myosin ◽  
Myofibrillar Atpase Activity ◽  
Fast Myosin Heavy Chain ◽  
The Relationship

Calpastatin, the specific endogenous inhibitor of the calpain system, is considered to be a principle contributor to variations in meat tenderisation (Parr et al., 1999). Previous studies have suggested that the differences in calpastatin activity in different ovine skeletal muscles could be influenced by muscle metabolic and contractile characteristics according to myofibrillar ATPase activity (Ouali and Talmant, 1990). The type of myofibrillar ATPase activity is largely determined by the content of slow or fast myosin heavy chains (Rivero et al., 1999). The present study was designed to investigate the relationship between calpastatin inhibitory activity and slow myosin heavy chain (MHC-s) and fast myosin heavy chain (MHC-f) expression.

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