scholarly journals Feed restriction delays developmental fast skeletal muscle myosin heavy chain isoforms in turkey poults selected for differential growth

2012 ◽  
Vol 91 (12) ◽  
pp. 3178-3183 ◽  
Author(s):  
K. Huffman ◽  
I. Zapata ◽  
J.M. Reddish ◽  
M.S. Lilburn ◽  
M. Wick
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Feed Restriction ◽  
Fast Skeletal Muscle ◽  
Differential Growth ◽  
Skeletal Muscle Myosin ◽  
Turkey Poults ◽  
Muscle Myosin

Fast skeletal muscle myosin heavy chain gene cluster of medaka Oryzias latipes enrolled in temperature adaptation

2007 ◽  
Vol 29 (2) ◽  
pp. 201-214 ◽  
Author(s):  
Chun-Shi Liang ◽  
Atsushi Kobiyama ◽  
Atsushi Shimizu ◽  
Takashi Sasaki ◽  
Shuichi Asakawa ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Oryzias Latipes ◽  
Chain Gene ◽  
Cdna Clones ◽  
Fast Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
Expression Levels ◽  
Muscle Myosin

To disclose mechanisms involved in temperature acclimation of fish muscle, we subjected eurythermal fish of medaka Oryzias latipes to cloning of myosin heavy chain genes ( MYHs). We cloned cDNAs encoding fast skeletal muscle myosin heavy chain (MYH) isoforms from cDNA libraries of medaka acclimated to 10 and 30°C and observed that different MYH cDNA clones are expressed in the two temperature-acclimated fish. Subsequently, we isolated several overlapping MYH contigs by shotgun cloning strategy from a medaka genomic library. Contig assembly of the complete medaka MYH ( mMYH) locus of 219 kbp revealed a cluster of tandemly arrayed 11 mMYHs, in which eight genes are actually transcribed, with the remaining three being pseudogenes. Expression analysis of the transcribed genes revealed that two genes were each highly expressed in medaka acclimated to 10 and 30°C, whereas comparatively lower expression levels of the three genes were exclusively observed in medaka acclimated to 30°C. cDNAs of the remaining genes were too underrepresented in the libraries to determine the expression levels, and the transcripts could only be obtained by reverse transcription-polymerase chain reaction. Deduced amino acid sequences in the loop 1 and loop 2 regions of mMYHs were highly variable, suggesting that these isoforms were functionally different. The present findings consolidate our knowledge on teleost MYH multigene family and would provide further insight into the mechanisms by which expressions of individual MYH molecules are fine-tuned with environmental temperature fluctuations with further functional analysis of the genes concerned.

Isolation and mapping of two porcine skeletal muscle myosin heavy chain isoforms

1998 ◽  
Vol 29 (2) ◽  
pp. 91-97 ◽  
Author(s):  
R. Davoli ◽  
P. Zambonelli ◽  
D. Bigi ◽  
L. Fontanesi ◽  
V. Russo
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin

Effect of Dietary Creatine on Skeletal Muscle Myosin Heavy Chain Isoform Expression in an Animal Model of Uremia

2004 ◽  
Vol 96 (4) ◽  
pp. e103-e110 ◽  
Author(s):  
Youri E.C. Taes ◽  
Marijn Speeckaert ◽  
Evelien Bauwens ◽  
Marc R. De Buyzere ◽  
Johan Libbrecht ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Animal Model ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Skeletal Muscle Myosin ◽  
Myosin Heavy Chain Isoform ◽  
Isoform Expression ◽  
Muscle Myosin

Improving human skeletal muscle myosin heavy chain fiber typing efficiency

2016 ◽  
Vol 37 (1-2) ◽  
pp. 1-5 ◽  
Author(s):  
Kevin A. Murach ◽  
James R. Bagley ◽  
Kathryn A. McLeland ◽  
Jose A. Arevalo ◽  
Anthony B. Ciccone ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Human Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin
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