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

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

scholarly journals The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit tibialis anterior muscle

1987 ◽  
Vol 243 (3) ◽  
pp. 695-699 ◽  
Author(s):  
R S Staron ◽  
D Pette
Keyword(s):  
Tibialis Anterior ◽  
Tibialis Anterior Muscle ◽  
Single Fibre ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Type I ◽  
Slow Myosin ◽  
Heavy Chains ◽  
Fast Myosin ◽  
Fast Light

1. Combined histochemical and biochemical single-fibre analyses [Staron & Pette (1987) Biochem. J. 243, 687-693], were used to investigate the rabbit tibialis-anterior fibre population. 2. This muscle is composed of four histochemically defined fibre types (I, IIC, IIA and IIB). 3. Type I fibres contain slow myosin light chains LC1s and LC2 and the slow myosin heavy chain HCI, and types IIA and IIB contain the fast myosin light chains LC1f, LC2f and LC3f and the fast heavy chains HCIIa and HCIIb respectively. 4. A small fraction of fibres (IIAB), histochemically intermediate between types IIA and IIB, contain the fast light myosin chains but display a coexistence of HCIIa and HCIIb. 5. Similarly to the soleus muscle, C fibres in the tibialis anterior muscle contain both fast and slow myosin light chains and heavy chains. The IIC fibres show a predominance of the fast forms and the IC fibres (histochemically intermediate between types I and IIC) a predominance of the slow forms. 6. A total of 60 theoretical isomyosins can be derived from these findings on the distribution of fast and slow myosin light and heavy chains in the fibres of rabbit tibialis anterior muscle.

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

Expression of slow and fast myosin heavy chains in overloaded muscles of the developing rat

1991 ◽  
Vol 12 (3) ◽  
pp. 247-253 ◽  
Author(s):  
J. M. Leferovich ◽  
N. A. Rubinstein ◽  
A. M. Kelly
Keyword(s):  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Fast Myosin ◽  
Developing Rat

Monospecific Antibodies against the Three Mammalian Fast Limb Myosin Heavy Chains

2000 ◽  
Vol 272 (1) ◽  
pp. 303-308 ◽  
Author(s):  
Christine A. Lucas ◽  
Lucia H.D. Kang ◽  
Joseph F.Y. Hoh
Keyword(s):  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Monospecific Antibodies
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