scholarly journals A new congenital multicore titinopathy associated with fast myosin heavy chain deficiency

2020 ◽  
Vol 7 (5) ◽  
pp. 846-854
Author(s):  
Aurélien Perrin ◽  
Corinne Metay ◽  
Marcello Villanova ◽  
Robert‐Yves Carlier ◽  
Elena Pegoraro ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fast Myosin ◽  
Fast Myosin Heavy Chain

The relationship between slow and fast myosin heavy chain content, calpastatin and meat tenderness in different ovine skeletal muscles

Meat Science ◽  
2005 ◽  
Vol 69 (1) ◽  
pp. 17-25 ◽  
Author(s):  
A.Q. Sazili ◽  
T. Parr ◽  
P.L. Sensky ◽  
S.W. Jones ◽  
R.G. Bardsley ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Skeletal Muscles ◽  
Meat Tenderness ◽  
Fast Myosin ◽  
Fast Myosin Heavy Chain ◽  
The Relationship

scholarly journals Slow and fast myosin heavy chain content defines three types of myotubes in early muscle cell cultures.

1985 ◽  
Vol 101 (5) ◽  
pp. 1643-1650 ◽  
Author(s):  
J B Miller ◽  
M T Crow ◽  
F E Stockdale
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Pectoral Muscle ◽  
Myosin Heavy Chain Isoforms ◽  
Fiber Formation ◽  
Single Type ◽  
Fast Myosin ◽  
Slow Myosin Heavy Chain ◽  
Fast Myosin Heavy Chain ◽  
Different Populations

We prepared monoclonal antibodies specific for fast or slow classes of myosin heavy chain isoforms in the chicken and used them to probe myosin expression in cultures of myotubes derived from embryonic chicken myoblasts. Myosin heavy chain expression was assayed by gel electrophoresis and immunoblotting of extracted myosin and by immunostaining of cultures of myotubes. Myotubes that formed from embryonic day 5-6 pectoral myoblasts synthesized both a fast and a slow class of myosin heavy chain, which were electrophoretically and immunologically distinct, but only the fast class of myosin heavy chain was synthesized by myotubes that formed in cultures of embryonic day 8 or older myoblasts. Furthermore, three types of myotubes formed in cultures of embryonic day 5-6 myoblasts: one that contained only a fast myosin heavy chain, a second that contained only a slow myosin heavy chain, and a third that contained both a fast and a slow heavy chain. Myotubes that formed in cultures of embryonic day 8 or older myoblasts, however, were of a single type that synthesized only a fast class of myosin heavy chain. Regardless of whether myoblasts from embryonic day 6 pectoral muscle were cultured alone or mixed with an equal number of myoblasts from embryonic day 12 muscle, the number of myotubes that formed and contained a slow class of myosin was the same. These results demonstrate that the slow class of myosin heavy chain can be synthesized by myotubes formed in cell culture, and that three types of myotubes form in culture from pectoral muscle myoblasts that are isolated early in development, but only one type of myotube forms from older myoblasts; and they suggest that muscle fiber formation probably depends upon different populations of myoblasts that co-exist and remain distinct during myogenesis.

scholarly journals Electrophoretic analysis of proteins from single bovine muscle fibres

1981 ◽  
Vol 195 (1) ◽  
pp. 317-327 ◽  
Author(s):  
O A Young ◽  
C L Davey
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Fibre Types ◽  
Type I ◽  
Slow Fibre ◽  
Slow Myosin ◽  
Fast Myosin ◽  
Fast Myosin Heavy Chain

A number of single fibres were isolated by dissection of four bovine masseter (ma) muscles, three rectus abdominis (ra) muscles and eight sternomandibularis (sm) muscles. By histochemical criteria these muscles contain respectively, solely slow fibres (often called type I), predominantly fast fibres (type II), and a mixture of fast and slow. The fibres were analysed by conventional sodium dodecyl sulphate/polyacrylamide-gel electrophoresis and the gels stained with Coomassie Blue. Irrespective of the muscle, every fibre could be classed into one of two broad groups based on the mobility of proteins in the range 135000-170000 daltons. When zones containing myosin heavy chain were cut from the single-fibre gel tracks and ‘mapped’ [Cleveland, Fischer, Kirschner & Laemmli (1977) J. Biol. Chem. 252, 1102-1106] with Staphylococcus proteinase, it was found that one group always contained fast myosin heavy chain, whereas the second group always contained the slow form. Moreover, a relatively fast-migrating alpha-tropomyosin was associated with the fast myosin group and a slow-migrating form with the slow myosin group. All fibres also contained beta-tropomyosin; the coexistence of alpha- and beta-tropomyosin is at variance with evidence that alpha-tropomyosin is restricted to fast fibres [Dhoot & Perry (1979) Nature (London) 278, 714-718]. Fast fibres containing the expected fast light chains and troponins I and C fast were identified in the three ra muscles, but in only four sm muscles. In three other sm muscles, all the fast fibres contained two troponins I and an additional myosin light chain that was more typical of myosin light chain 1 slow. The remaining sm muscle contained a fast fibre type that was similar to the first type, except that its myosin light chain 1 was more typical of the slow polymorph. Troponin T was bimorphic in all fast fibres from a ra muscles and in at least some fast fibres from one sm muscle. Peptide ‘mapping’ revealed two forms of fast myosin heavy chain distributed among fast fibres. Each form was associated with certain other proteins. Slow myosin heavy chain was unvarying in three slow fibre types identified. Troponin I polymorphs were the principal indicator of slow fibre types. The myofibrillar polymorphs identified presumably contribute to contraction properties, but beyond cud chewing involving ma muscle, nothing is known of the conditions that gave rise to the variable fibre composites in sm and ra muscles.

A vitamin D analogue, eldecalcitol, enhances expression of fast myosin heavy chain subtypes in differentiated C2C12 myoblasts

2017 ◽  
Vol 22 (2) ◽  
pp. 345-350 ◽  
Author(s):  
Hideo Saito ◽  
Koshi N. Kishimoto ◽  
Yu Mori ◽  
Hiroshi Okuno ◽  
Masahiko Tanaka ◽  
...  
Keyword(s):  
Vitamin D ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
C2c12 Myoblasts ◽  
Fast Myosin ◽  
Fast Myosin Heavy Chain ◽  
Vitamin D Analogue

scholarly journals Fast myosin heavy chain diversity in skeletal muscles of the rabbit: heavy chain IId, not IIb predominates

1993 ◽  
Vol 211 (1-2) ◽  
pp. 367-372 ◽  
Author(s):  
Sigrid AIGNER ◽  
Barbel GOHLSCH ◽  
Nina HAMALAINEN ◽  
Robert S. STARON ◽  
Andreas UBER ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Skeletal Muscles ◽  
Fast Myosin ◽  
Fast Myosin Heavy Chain

scholarly journals De-phosphorylation of MyoD is linking nerve-evoked activity to fast myosin heavy chain expression in rodent adult skeletal muscle

2007 ◽  
Vol 584 (2) ◽  
pp. 637-650 ◽  
Author(s):  
Merete Ekmark ◽  
Zaheer Ahmad Rana ◽  
Greg Stewart ◽  
D. Grahame Hardie ◽  
Kristian Gundersen
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Adult Skeletal Muscle ◽  
Fast Myosin ◽  
Fast Myosin Heavy Chain ◽  
Evoked Activity
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