scholarly journals Effect of selection for growth rate on myosin heavy chain temporal and spatial localization during turkey breast muscle development

2003 ◽  
Vol 82 (9) ◽  
pp. 1373-1377 ◽  
Author(s):  
SG Velleman ◽  
KE Nestor
Keyword(s):  
Growth Rate ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Development ◽  
Spatial Localization ◽  
Breast Muscle ◽  
Temporal And Spatial ◽  
Selection For

scholarly journals Six myosin heavy chain isoforms are expressed during chick breast muscle development

FEBS Letters ◽  
1988 ◽  
Vol 238 (2) ◽  
pp. 245-248 ◽  
Author(s):  
Sabine Hofmann ◽  
Sabine Düsterhöft ◽  
Dirk Pette
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Development ◽  
Myosin Heavy Chain Isoforms ◽  
Breast Muscle

scholarly journals Effect of selection for growth rate on embryonic breast muscle development in turkeys

2002 ◽  
Vol 81 (8) ◽  
pp. 1113-1121 ◽  
Author(s):  
SG Velleman ◽  
CS Coy ◽  
JW Anderson ◽  
RA Patterson ◽  
KE Nestor
Keyword(s):  
Growth Rate ◽  
Muscle Development ◽  
Breast Muscle ◽  
Selection For

scholarly journals Effect of selection for growth rate on muscle damage during turkey breast muscle development

2003 ◽  
Vol 82 (7) ◽  
pp. 1069-1074 ◽  
Author(s):  
SG Velleman ◽  
JW Anderson ◽  
CS Coy ◽  
KE Nestor
Keyword(s):  
Growth Rate ◽  
Muscle Damage ◽  
Muscle Development ◽  
Breast Muscle ◽  
Selection For

scholarly journals A screen for genetic loci required for body-wall muscle development during embryogenesis in Caenorhabditis elegans.

Genetics ◽  
1994 ◽  
Vol 137 (2) ◽  
pp. 483-498
Author(s):  
J Ahnn ◽  
A Fire
Keyword(s):  
Caenorhabditis Elegans ◽  
Myosin Heavy Chain ◽  
Muscle Cell ◽  
Heavy Chain ◽  
Body Wall ◽  
Muscle Development ◽  
Contractile Function ◽  
The Body ◽  
Body Wall Muscle ◽  
Genetic Loci

Abstract We have used available chromosomal deficiencies to screen for genetic loci whose zygotic expression is required for formation of body-wall muscle cells during embryogenesis in Caenorhabditis elegans. To test for muscle cell differentiation we have assayed for both contractile function and the expression of muscle-specific structural proteins. Monoclonal antibodies directed against two myosin heavy chain isoforms, the products of the unc-54 and myo-3 genes, were used to detect body-wall muscle differentiation. We have screened 77 deficiencies, covering approximately 72% of the genome. Deficiency homozygotes in most cases stain with antibodies to the body-wall muscle myosins and in many cases muscle contractile function is observed. We have identified two regions showing distinct defects in myosin heavy chain gene expression. Embryos homozygous for deficiencies removing the left tip of chromosome V fail to accumulate the myo-3 and unc-54 products, but express antigens characteristic of hypodermal, pharyngeal and neural development. Embryos lacking a large region on chromosome III accumulate the unc-54 product but not the myo-3 product. We conclude that there exist only a small number of loci whose zygotic expression is uniquely required for adoption of a muscle cell fate.

scholarly journals A novel positive selection for identifying cold-sensitive myosin II mutants in Dictyostelium.

Genetics ◽  
1995 ◽  
Vol 140 (2) ◽  
pp. 505-515 ◽  
Author(s):  
B Patterson ◽  
J A Spudich
Keyword(s):  
Positive Selection ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Time Scale ◽  
Myosin Ii ◽  
Rapid Onset ◽  
Chemical Mutagenesis ◽  
Wild Type ◽  
Cold Sensitive ◽  
Selection For

Abstract We developed a positive selection for myosin heavy chain mutants in Dictyostelium. This selection is based on the fact that brief exposure to azide causes wild-type cells to release from the substrate, whereas myosin null cells remain adherent. This procedure assays myosin function on a time scale of minutes and has therefore allowed us to select rapid-onset cold-sensitive mutants after random chemical mutagenesis of Dictyostelium cells. We developed a rapid technique for determining which mutations lie in sequences of the myosin gene that encode the head (motor) domain and localized 27 of 34 mutants to this domain. We recovered the appropriate sequences from five of the mutants and demonstrated that they retain their cold-sensitive properties when expressed from extrachromosomal plasmids.

The mutant not enough muscles (nem) reveals reduction of the Drosophila embryonic muscle pattern

1995 ◽  
Vol 108 (4) ◽  
pp. 1443-1454 ◽  
Author(s):  
S. Burchard ◽  
A. Paululat ◽  
U. Hinz ◽  
R. Renkawitz-Pohl
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Development ◽  
P Element ◽  
Dual Function ◽  
Methane Sulfonate ◽  
Visceral Mesoderm ◽  
Embryonic Muscle ◽  
Embryonic Muscle Development ◽  
Somatic Musculature

In a search for mutations affecting embryonic muscle development in Drosophila we identified a mutation caused by the insertion of a P-element, which we called not enough muscles (nem). The phenotype of the P-element mutation of the nem gene suggests that it may be required for the development of the somatic musculature and the chordotonal organs of the PNS, while it is not involved in the development of the visceral mesoderm and the dorsal vessel. Mutant embryos are characterized by partial absence of muscles, monitored by immunostainings with mesoderm-specific anti-beta 3 tubulin and anti-myosin heavy chain antibodies. Besides these muscle distortions, defects in the peripheral nervous system were found, indicating a dual function of the nem gene product. Ethyl methane sulfonate-induced alleles for the P-element mutation were created for a detailed analysis. One of these alleles is characterized by unfused myoblasts which express beta 3 tubulin and myosin heavy chain, indicating the state of cell differentiation.

The expression of multiple myosin heavy chain genes during skeletal muscle development of torafugu Takifugu rubripes embryos and larvae

Gene ◽  
2013 ◽  
Vol 515 (1) ◽  
pp. 144-154 ◽  
Author(s):  
Md. Asaduzzaman ◽  
Dadasaheb B. Akolkar ◽  
Shigeharu Kinoshita ◽  
Shugo Watabe
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Development ◽  
Takifugu Rubripes ◽  
Skeletal Muscle Development ◽  
Myosin Heavy Chain Genes

scholarly journals Type 2X-myosin heavy chain is coded by a muscle fiber type-specific and developmentally regulated gene.

1993 ◽  
Vol 123 (4) ◽  
pp. 823-835 ◽  
Author(s):  
C DeNardi ◽  
S Ausoni ◽  
P Moretti ◽  
L Gorza ◽  
M Velleca ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Muscle Development ◽  
Fiber Type ◽  
Muscle Fibers ◽  
Hindlimb Muscles ◽  
Isolation And Characterization ◽  
Skeletal Muscle Fibers ◽  
Myhc Isoforms

We have previously reported the identification of a distinct myosin heavy chain (MyHC) isoform in a major subpopulation of rat skeletal muscle fibers, referred to as 2X fibers (Schiaffino, S., L. Gorza, S. Sartore, L. Saggin, M. Vianello, K. Gundersen, and T. Lømo. 1989. J. Muscle Res. Cell Motil. 10:197-205). However, it was not known whether 2X-MyHC is the product of posttranslational modification of other MyHCs or is coded by a distinct mRNA. We report here the isolation and characterization of cDNAs coding a MyHC isoform that is expressed in type 2X skeletal muscle fibers. 2X-MyHC transcripts differ from other MyHC transcripts in their restriction map and 3' end sequence and are thus derived from a distinct gene. In situ hybridization analyses show that 2X-MyHC transcripts are expressed at high levels in the diaphragm and fast hindlimb muscles and can be coexpressed either with 2B- or 2A-MyHC transcripts in a number of fibers. At the single fiber level the distribution of each MyHC mRNA closely matches that of the corresponding protein, determined by specific antibodies on serial sections. In hindlimb muscles 2X-, 2A-, and 2B-MyHC transcripts are first detected by postnatal day 2-5 and display from the earliest stages a distinct pattern of distribution in different muscles and different fibers. The emergence of type 2 MyHC isoforms thus defines a distinct neonatal phase of fiber type differentiation during muscle development. The functional significance of MyHC isoforms is discussed with particular reference to the velocity of shortening of skeletal muscle fibers.

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