Identification and distribution of some developmental isoforms of myosin heavy chains in avian muscle fibres

1988 ◽  
Vol 9 (6) ◽  
pp. 516-524 ◽  
Author(s):  
Karen Kilby ◽  
Gurtej K. Dhoot
Keyword(s):  
Muscle Fibres ◽  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Avian Muscle

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 Carbonylation of myosin heavy chains in rat heart during diabetes

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

scholarly journals Shortening velocity and myosin heavy chains of developing rabbit muscle fibers.

1985 ◽  
Vol 260 (27) ◽  
pp. 14403-14405 ◽  
Author(s):  
P J Reiser ◽  
R L Moss ◽  
G G Giulian ◽  
M L Greaser
Keyword(s):  
Muscle Fibers ◽  
Rabbit Muscle ◽  
Myosin Heavy Chains ◽  
Shortening Velocity ◽  
Heavy Chains

Modulation of Myosin Heavy Chains in Rat Laryngeal Muscle

2001 ◽  
Vol 111 (3) ◽  
pp. 472-477 ◽  
Author(s):  
Akihiro Shiotani ◽  
Hideki Nakagawa ◽  
Paul W. Flint
Keyword(s):  
Myosin Heavy Chains ◽  
Laryngeal Muscle ◽  
Heavy Chains

scholarly journals Comprehensive Analytics of Actovegin® and Its Effect on Muscle Cells

2017 ◽  
Vol 38 (11) ◽  
pp. 809-818 ◽  
Author(s):  
Franz-Xaver Reichl ◽  
Lesca Holdt ◽  
Daniel Teupser ◽  
Gregor Schütze ◽  
Alan Metcalfe ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Muscle Cell ◽  
Muscle Cells ◽  
Primary Antibody ◽  
Myosin Heavy Chains ◽  
C2c12 Myoblasts ◽  
Heavy Chains ◽  
Human Adult ◽  
Differentiation Medium ◽  
The Mean

AbstractThe ingredients of Actovegin® were analyzed and its effects on the muscle cell proliferation were investigated. C2C12 myoblasts were cultured in medium. Actovegin® was added in five different concentrations (1, 5, 25, 125, and 250 µg) to the differentiation medium. The formations of proliferation factor Ki67 and myosin heavy chains were measured by immunofluorescence. The first primary antibody was anti-Ki67 and anti-Mf20. Cells were washed and treated with the second fluorochrome. Thirty-one Actovegin® ingredients were found to contain significantly higher concentrations and twenty-nine ingredients were found to contain significantly lower concentrations, compared to the mean ranges as described in the literature for the normal physiological concentrations in human adult serum/plasma. A significant increase in the formation of Ki67 was observed in Actovegin® groups, compared to controls. The mean area of myotubes was significantly increased in Actovegin® groups. A significant decrease in the number of myotubes was observed. An increased myotube size (fusion) was observed. The intensity of Mf20 was significantly increased in Actovegin® groups. It could be demonstrated that Actovegin® contains many physiological substances in significantly higher and some in lower concentrations compared to human adult serum. Furthermore, it could be shown that Actovegin® improves muscle cell proliferation.

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