scholarly journals Expression of multiple slow myosin heavy chain genes reveals a diversity of zebrafish slow twitch muscle fibres with differing requirements for Hedgehog and Prdm1 activity

Development ◽  
2008 ◽  
Vol 135 (12) ◽  
pp. 2115-2126 ◽  
Author(s):  
S. Elworthy ◽  
M. Hargrave ◽  
R. Knight ◽  
K. Mebus ◽  
P. W. Ingham
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Fibres ◽  
Slow Myosin ◽  
Slow Myosin Heavy Chain ◽  
Slow Twitch Muscle ◽  
Myosin Heavy Chain Genes ◽  
Slow Twitch

Red and white muscle development in the trout (Oncorhynchus mykiss) as shown by in situ hybridisation of fast and slow myosin heavy chain transcripts

2001 ◽  
Vol 204 (12) ◽  
pp. 2097-2101 ◽  
Author(s):  
Pierre-Yves Rescan ◽  
Bertrand Collet ◽  
Cecile Ralliere ◽  
Chantal Cauty ◽  
Jean-Marie Delalande ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
In Situ Hybridisation ◽  
Slow Muscle ◽  
Fast Muscle ◽  
Slow Myosin ◽  
Slow Myosin Heavy Chain ◽  
And Migration ◽  
Slow Myhc

SUMMARY The axial muscle of most teleost species consists of a deep bulk of fast-contracting white fibres and a superficial strip of slow-contracting red fibres. To investigate the embryological development of fast and slow muscle in trout embryos, we carried out single and double in situ hybridisation with fast and slow myosin heavy chain (MyHC)-isoform-specific riboprobes. This showed that the slow-MyHC-positive cells originate in a region of the somite close to the notochord. As the somite matures in a rostrocaudal progression, the slow-MyHC-positive cells appear to migrate radially away from the notochord to the lateral surface of the myotome, where they form the superficial strip of slow muscle. Surprisingly, the expression pattern of the fast MyHC showed that the differentiation of fast muscle commences in the medial domain of the somite before the differentiation and migration of the slow muscle precursors. Later, as the differentiation of fast muscle progressively spreads from the inside to the outside of the myotome, slow-MyHC-expressing cells become visible medially. Our observations that the initial differentiation of fast muscle takes place in proximity to axial structures and occurs before the differentiation and migration of slow muscle progenitors are not in accord with the pattern of muscle formation in teleosts previously described in the zebrafish Danio rerio, which is often used as the model organism in fishes.

Slow myosin heavy chain isozyme in nemaline myopathy

Neurology ◽  
1985 ◽  
Vol 35 (9) ◽  
pp. 1360-1360 ◽  
Author(s):  
D. Biral ◽  
E. Damiani ◽  
A. Margreth ◽  
E. Scarpini ◽  
G. Scarlato
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Nemaline Myopathy ◽  
Slow Myosin ◽  
Slow Myosin Heavy Chain

KLF15 regulates slow myosin heavy chain expression through NFATc1 in C2C12 myotubes

2014 ◽  
Vol 446 (4) ◽  
pp. 1231-1236 ◽  
Author(s):  
Jie Wang ◽  
Ting Chen ◽  
Fu Feng ◽  
Huan Wei ◽  
Weijun Pang ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
C2c12 Myotubes ◽  
Slow Myosin ◽  
Slow Myosin Heavy Chain

scholarly journals Small-diameter white myotomal muscle fibres associated with growth hyperplasia in the carp (Cyprinus carpio) express a distinct myosin heavy chain gene.

1995 ◽  
Vol 198 (7) ◽  
pp. 1603-1611 ◽  
Author(s):  
S Ennion ◽  
L Gauvry ◽  
P Butterworth ◽  
G Goldspink
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
White Muscle ◽  
In Situ Hybridisation ◽  
Small Diameter ◽  
Chain Gene ◽  
Muscle Fibres ◽  
Heavy Chain Gene ◽  
Myosin Heavy Chain Gene ◽  
Myosin Heavy Chain Genes

A carp myosin heavy chain gene isoform was isolated from a genomic clone, restriction mapped and partially sequenced to reveal the location of various exons. The clone contains a complete gene of approximately 12.0 kb which is half the size of the corresponding mammalian and avian myosin heavy chain genes. The mRNA transcript of this gene, however, is the same size as mammalian and avian striated muscle myosin heavy chain genes (about 6000 nucleotides), illustrating that the difference in size at the genomic level is due to shorter introns. A 169 bp NsiI restriction fragment containing only the 3' untranslated region of this gene was subcloned and used as an isoform-specific probe to study the expression of this particular isoform. Hybridisation analysis could only detect expression of this myosin heavy chain gene in the white muscle of adult carp that had been subjected to an increased environmental temperature. No expression of this gene was detected in carp under 1 year of age. In situ hybridisation demonstrated that expression of this gene is limited to small-diameter white muscle fibres of adult carp, which are thought to be responsible for muscle growth by fibre hyperplasia.

Mutation of the slow myosin heavy chain rod domain underlies hyaline body myopathy

Neurology ◽  
2005 ◽  
Vol 64 (3) ◽  
pp. 580-581 ◽  
Author(s):  
A. Oldfors ◽  
H. Tajsharghi ◽  
L. E. Thornell ◽  
B. F. Meyer
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Slow Myosin ◽  
Slow Myosin Heavy Chain ◽  
Hyaline Body
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