scholarly journals Influence of Myosin Heavy Chain Protein Isoforms on Akt/mTOR Signaling and mRNA Expression Following Resistance Exercise in Trained Men

2015 ◽  
Vol 29 (S1) ◽  
Author(s):  
Adam Gonzalez ◽  
Jay Hoffman ◽  
Jeremy Townsend ◽  
Adam Jajtner ◽  
Adam Wells ◽  
...  
Keyword(s):  
Resistance Exercise ◽  
Mrna Expression ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Mtor Signaling ◽  
Protein Isoforms ◽  
Myosin Heavy Chain Protein

scholarly journals Association between myosin heavy chain protein isoforms and intramuscular anabolic signaling following resistance exercise in trained men

2015 ◽  
Vol 3 (1) ◽  
pp. e12268 ◽  
Author(s):  
Adam M. Gonzalez ◽  
Jay R. Hoffman ◽  
Jeremy R. Townsend ◽  
Adam R. Jajtner ◽  
Adam J. Wells ◽  
...  
Keyword(s):  
Resistance Exercise ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Protein Isoforms ◽  
Myosin Heavy Chain Protein

Denervation-induced changes in myosin heavy chain expression in the rat diaphragm muscle

2003 ◽  
Vol 95 (2) ◽  
pp. 611-619 ◽  
Author(s):  
Paige C. Geiger ◽  
Jeffrey P. Bailey ◽  
Wen-Zhi Zhan ◽  
Carlos B. Mantilla ◽  
Gary C. Sieck
Keyword(s):  
Protein Expression ◽  
Mrna Expression ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Protein Isoforms ◽  
Diaphragm Muscle ◽  
Northern Analysis ◽  
Mrna Levels ◽  
Rat Diaphragm ◽  
Mrna Isoforms

Unilateral denervation (Dnv) of the rat diaphragm muscle (Diam) markedly alters expression of myosin heavy chain (MHC) isoforms. After 2 wk of Diam Dnv, MHC content per half-sarcomere decreases in fibers expressing MHC2X and MHC2B. We hypothesized that changes in MHC protein expression parallel changes in MHC mRNA expression. Relative MHC isoform mRNA levels were determined by Northern analysis after 1, 3, 7, and 14 days of Dnv of the rat Diam. MHC protein expression was determined by SDS-PAGE. Changes in MHC isoform protein and mRNA expression were not concurrent. Expression of MHCSlow and MHC2X mRNA isoforms decreased dramatically by 3 days of Dnv, whereas that of MHC2A and MHC2B did not change. Expression of all MHC protein isoforms decreased by 3 days of Dnv. We observed a differential effect of rat Diam Dnv on MHC isoform protein and mRNA expression. The time course of the changes in MHC isoform mRNA and protein expression suggests a predominant effect of altered protein turnover rates on MHC protein expression instead of altered transcription after Dnv.

529 MYOSIN HEAVY CHAIN PROTEIN AND mRNA EXPRESSION IN RESPONSE TO SPACEFLIGHT

1994 ◽  
Vol 26 (Supplement) ◽  
pp. S94
Author(s):  
Karyn Esser ◽  
Samuel Fauteck ◽  
Susan Kandarlan ◽  
Edna Hardeman
Keyword(s):  
Mrna Expression ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Myosin Heavy Chain Protein

scholarly journals Differential Expression of Equine Myosin Heavy-chain mRNA and Protein Isoforms in a Limb Muscle

2003 ◽  
Vol 51 (9) ◽  
pp. 1207-1216 ◽  
Author(s):  
Karin Eizema ◽  
Maarten van den Burg ◽  
Arpna Kiri ◽  
Elizabeth G. Dingboom ◽  
Hans van Oudheusden ◽  
...  
Keyword(s):  
Mrna Expression ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Gluteus Medius ◽  
Protein Isoforms ◽  
Transcriptional Level ◽  
Structural Protein ◽  
Hybrid Fibers ◽  
Skeletal Muscle Myosin ◽  
Slow Type

The horse is one of the few animals kept and bred for its athletic performance and is therefore an interesting model for human sports performance. The regulation of the development of equine locomotion in the first year of life, and the influence of early training on later performance, are largely unknown. The major structural protein in skeletal muscle, myosin heavy-chain (MyHC), is believed to be primarily transcriptionally controlled. To investigate the expression of the MyHC genes at the transcriptional level, we isolated cDNAs encoding the equine MyHC isoforms type 1 (slow), type 2a (fast oxidative), and type 2d/x (fast glycolytic). cDNAs encoding the 2b gene were not identified. The mRNA expression was compared to the protein expression on a fiber-to-fiber basis using in situ hybridization (non-radioactive) and immunohistochemistry. Marked differences were detected between the expression of MyHC transcripts and MyHC protein isoforms in adult equine gluteus medius muscle. Mismatches were primarily due to the presence of hybrid fibers expressing two fast (2ad) MyHC protein isoforms, but only one fast (mainly 2a) MyHC RNA isoform. This discrepancy was most likely not due to differential mRNA expression of myonuclei.

Effects of triiodo-thyronine on angiotensin-induced cardiomyocyte hypertrophy: reversal of increased β-myosin heavy chain gene expression

2006 ◽  
Vol 84 (8-9) ◽  
pp. 935-941 ◽  
Author(s):  
Baohua Wang ◽  
Jingping Ouyang ◽  
Zhengyuan Xia
Keyword(s):  
Gene Expression ◽  
Angiotensin Ii ◽  
Thyroid Hormone ◽  
Cardiac Hypertrophy ◽  
Atpase Activity ◽  
Mrna Expression ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Ang Ii ◽  
Hypertrophic Growth

Thyroid hormone-induced cardiac hypertrophy is similar to that observed in physiological hypertrophy, which is associated with high cardiac contractility and increased α-myosin heavy chain (α-MHC, the high ATPase activity isoform) expression. In contrast, angiotensin II (Ang II) induces an increase in myocardial mass with a compromised contractility accompanied by a shift from α-MHC to the fetal isoform β-MHC (the low ATPase activity isoform), which is considered as a pathological hypertrophy and inevitably leads to the development of heart failure. The present study is designed to assess the effect of thyroid hormone on angiotensin II-induced hypertrophic growth of cardiomyocytes in vitro. Cardiomyocytes were prepared from hearts of neonatal Wistar rats. The effects of Ang II and 3,3′,5-triiodo-thyronine (T3) on incorporations of [3H]-thymine and [3H]-leucine, MHC isoform mRNA expression, PKC activity, and PKC isoform protein expression were studied. Ang II enhanced [3H]-leucine incorporation, β-MHC mRNA expression, PKC activity, and PKCε expression and inhibited α-MHC mRNA expression in cardiomyocytes. T3 treatment prevented Ang II-induced increases in PKC activity, PKCε, and β-MHC mRNA overexpression and favored α-MHC mRNA expression. Thyroid hormone appears to be able to reprogram gene expression in Ang II-induced cardiac hypertrophy, and a PKC signal pathway may be involved in such remodeling process.

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