Correlation of myosin heavy chains with ATPase staining of skeletal- and cardiac-muscle fibres

1984 ◽  
Vol 12 (5) ◽  
pp. 825-826 ◽  
Author(s):  
W. T. PERRIE ◽  
SANDRA J. BUMFORD
1995 ◽  
Vol 16 (1) ◽  
pp. 35-43 ◽  
Author(s):  
Steven Ennion ◽  
Jos� Sant' Ana Pereira ◽  
Anthony J. Sargeant ◽  
Archie Young ◽  
Geoffrey Goldspink

1982 ◽  
Vol 207 (2) ◽  
pp. 261-272 ◽  
Author(s):  
G Salviati ◽  
R Betto ◽  
D Danieli Betto

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.


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

2010 ◽  
Vol 80 (2) ◽  
pp. 205-217 ◽  
Author(s):  
Chun-Hong Shao ◽  
George J. Rozanski ◽  
Ryoji Nagai ◽  
Frank E. Stockdale ◽  
Kaushik P. Patel ◽  
...  

1985 ◽  
Vol 260 (27) ◽  
pp. 14403-14405 ◽  
Author(s):  
P J Reiser ◽  
R L Moss ◽  
G G Giulian ◽  
M L Greaser

2001 ◽  
Vol 111 (3) ◽  
pp. 472-477 ◽  
Author(s):  
Akihiro Shiotani ◽  
Hideki Nakagawa ◽  
Paul W. Flint

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