scholarly journals Myosin heavy chains in extraocular muscle fibres: Distribution, regulation and function

2020 ◽  
Author(s):  
Joseph F. Y. Hoh
Keyword(s):  
Extraocular Muscle ◽  
Muscle Fibres ◽  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
And Function

Characterization of human skeletal muscle fibres according to the myosin heavy chains they express

1995 ◽  
Vol 16 (1) ◽  
pp. 35-43 ◽  
Author(s):  
Steven Ennion ◽  
Jos� Sant' Ana Pereira ◽  
Anthony J. Sargeant ◽  
Archie Young ◽  
Geoffrey Goldspink
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Muscle Fibres ◽  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Skeletal Muscle Fibres

scholarly journals Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibres. An electrophoretic study of single fibres

1982 ◽  
Vol 207 (2) ◽  
pp. 261-272 ◽  
Author(s):  
G Salviati ◽  
R Betto ◽  
D Danieli Betto
Keyword(s):  
Light Chain ◽  
Light Chains ◽  
Muscle Fibres ◽  
Myofibrillar Proteins ◽  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Single Fibres ◽  
Slow Twitch ◽  
Fast Twitch ◽  
Slow Twitch Fibre

Rabbit predominantly fast-twitch-fibre and predominantly slow-twitch-fibre skeletal muscles of the hind limbs, the psoas, the diaphragm and the masseter muscles were fibre-typed by one-dimensional polyacrylamide-gel electrophoresis of the myofibrillar proteins of chemically skinned single fibres. Investigation of the distribution of fast-twitch-fibre and slow-twitch-fibre isoforms of myosin light chains and the type of myosin heavy chains, based on peptide ‘maps’ published in Cleveland. Fischer, Kirschner & Laemmli [(1977) J. Biol. Chem. 252, 1102-1106], allowed a classification of muscle fibres into four classes, corresponding to histochemical types I, IIA, IIB and IIC. Type I fibres with a pure slow-twitch-type of myosin were found to be characterized by a unique set of isoforms of troponins I, C and T, in agreement with the immunological data of Dhoot & Perry [(1979) Nature (London) 278, 714-718], by predominance of the beta-tropomyosin subunit and by the presence of a small amount of an additional tropomyosin subunit, apparently dissimilar from fast-twitch-fibre alpha-tropomyosin subunit. The myofibrillar composition of type IIB fast-twitch white fibres was the mirror image of that found for slow-twitch fibres in that the fast-twitch-fibre isoforms only of the troponin subunits were present and the alpha-tropomyosin subunit predominated. Type IIA fast-twitch red fibres showed a troponin subunit composition identical with that of type IIB fast-twitch white fibres. On the other hand, a unique type of myosin heavy chains was found to be associated with type IIA fibres. Furthermore, the myosin light-chain composition of these fibres was invariably characterized by a small amount of LC3F light chain and by a pattern that was either a pure fast-twitch-fibre light-chain pattern or a hybrid LC1F/LC2F/LC3F/LC1Sb light-chain pattern. By these criteria type IIA fibres could be distinguished from type IIC intermediate fibres, which showed coexistence of fast-twitch-fibre and slow-twitch-fibre forms of myosin light chains and of troponin subunits.

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

scholarly journals Skeletal muscle hypertrophy and structure and function of skeletal muscle fibres in male body builders

2006 ◽  
Vol 570 (3) ◽  
pp. 611-627 ◽  
Author(s):  
Giuseppe D'Antona ◽  
Francesca Lanfranconi ◽  
Maria Antonietta Pellegrino ◽  
Lorenza Brocca ◽  
Raffaella Adami ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Hypertrophy ◽  
Structure And Function ◽  
Muscle Fibres ◽  
Male Body ◽  
Skeletal Muscle Hypertrophy ◽  
And Function ◽  
Skeletal Muscle Fibres
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