scholarly journals Myocyte Enhancer Factor-2 and Serum Response Factor Binding Elements Regulate Fast Myosin Heavy Chain Transcriptionin Vivo

2005 ◽  
Vol 280 (17) ◽  
pp. 17126-17134 ◽  
Author(s):  
David L. Allen ◽  
Jesse N. Weber ◽  
Laura K. Sycuro ◽  
Leslie A. Leinwand
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Serum Response Factor ◽  
Response Factor ◽  
Myocyte Enhancer Factor 2 ◽  
Factor Binding ◽  
Fast Myosin ◽  
Fast Myosin Heavy Chain ◽  
Serum Response ◽  
Enhancer Factor

scholarly journals Identification of a New Hybrid Serum Response Factor and Myocyte Enhancer Factor 2-binding Element in MyoD Enhancer Required for MyoD Expression during Myogenesis

2007 ◽  
Vol 18 (6) ◽  
pp. 1992-2001 ◽  
Author(s):  
Aurore L'honore ◽  
Vanessa Rana ◽  
Nikola Arsic ◽  
Celine Franckhauser ◽  
Ned J. Lamb ◽  
...  
Keyword(s):  
Satellite Cells ◽  
Muscle Regeneration ◽  
Serum Response Factor ◽  
Response Factor ◽  
Dependent Manner ◽  
Myocyte Enhancer Factor 2 ◽  
Myocyte Enhancer Factor ◽  
Serum Response ◽  
Myod Expression ◽  
Enhancer Factor

MyoD is a critical myogenic factor induced rapidly upon activation of quiescent satellite cells, and required for their differentiation during muscle regeneration. One of the two enhancers of MyoD, the distal regulatory region, is essential for MyoD expression in postnatal muscle. This enhancer contains a functional divergent serum response factor (SRF)-binding CArG element required for MyoD expression during myoblast growth and muscle regeneration in vivo. Electrophoretic mobility shift assay, chromatin immunoprecipitation, and microinjection analyses show this element is a hybrid SRF- and MEF2 Binding (SMB) sequence where myocyte enhancer factor 2 (MEF2) complexes can compete out binding of SRF at the onset of differentiation. As cells differentiate into postmitotic myotubes, MyoD expression no longer requires SRF but instead MEF2 binding to this dual-specificity element. As such, the MyoD enhancer SMB element is the site for a molecular relay where MyoD expression is first initiated in activated satellite cells in an SRF-dependent manner and then increased and maintained by MEF2 binding in differentiated myotubes. Therefore, SMB is a DNA element with dual and stage-specific binding activity, which modulates the effects of regulatory proteins critical in controlling the balance between proliferation and differentiation.

scholarly journals Growth and differentiation of C2 myogenic cells are dependent on serum response factor.

1996 ◽  
Vol 16 (11) ◽  
pp. 6065-6074 ◽  
Author(s):  
M Soulez ◽  
C G Rouviere ◽  
P Chafey ◽  
D Hentzen ◽  
M Vandromme ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Antisense Rna ◽  
Serum Response Factor ◽  
Myogenic Differentiation ◽  
Receptor Expression ◽  
Rna Expression ◽  
Response Factor ◽  
Myogenic Cells ◽  
Serum Response

In order to study to what extent and at which stage serum response factor (SRF) is indispensable for myogenesis, we stably transfected C2 myogenic cells with, successively, a glucocorticoid receptor expression vector and a construct allowing for the expression of an SRF antisense RNA under the direction of the mouse mammary tumor virus long terminal repeat. In the clones obtained, SRF synthesis is reversibly down-regulated by induction of SRF antisense RNA expression by dexamethasone, whose effect is antagonized by the anti-hormone RU486. Two kinds of proliferation and differentiation patterns have been obtained in the resulting clones. Some clones with a high level of constitutive SRF antisense RNA expression are unable to differentiate into myotubes; their growth can be blocked by further induction of SRF antisense RNA expression by dexamethasone. Other clones are able to differentiate and are able to synthesize SRF, MyoD, myogenin, and myosin heavy chain at confluency. When SRF antisense RNA expression is induced in proliferating myoblasts by dexamethasone treatment, cell growth is blocked and cyclin A concentration drops. When SRF antisense RNA synthesis is induced in arrested confluent myoblasts cultured in a differentiation medium, cell fusion is blocked and synthesis of not only SRF but also MyoD, myogenin, and myosin heavy chain is inhibited. Our results show, therefore, that SRF synthesis is indispensable for both myoblast proliferation and myogenic differentiation.

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 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

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.

scholarly journals Serum response factor binding sites differ in three human cell types

2007 ◽  
Vol 17 (2) ◽  
pp. 136-144 ◽  
Author(s):  
S. J. Cooper ◽  
N. D. Trinklein ◽  
L. Nguyen ◽  
R. M. Myers
Keyword(s):  
Human Cell ◽  
Binding Sites ◽  
Serum Response Factor ◽  
Cell Types ◽  
Response Factor ◽  
Factor Binding ◽  
Serum Response
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