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 Changes in myosin heavy chain mRNA and protein isoforms in single fibers of unloaded rat soleus muscle

FEBS Letters ◽  
1999 ◽  
Vol 463 (1-2) ◽  
pp. 15-18 ◽  
Author(s):  
Laurence Stevens ◽  
Bärbel Gohlsch ◽  
Yvonne Mounier ◽  
Dirk Pette
Keyword(s):  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
Protein Isoforms ◽  
Single Fibers ◽  
Rat Soleus Muscle

scholarly journals Changes in myosin heavy chain mRNA and protein isoforms of rat muscle during forced contractile activity

1998 ◽  
Vol 274 (2) ◽  
pp. C365-C370 ◽  
Author(s):  
Frank Jaschinski ◽  
Michael Schuler ◽  
Heidemarie Peuker ◽  
Dirk Pette
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Protein Level ◽  
Contractile Activity ◽  
Low Frequency ◽  
Myosin Heavy Chain Isoforms ◽  
Protein Isoforms ◽  
Low Frequency Stimulation ◽  
Frequency Stimulation ◽  
Induced Changes

A quantitative reverse transcriptase-polymerase chain reaction was established to determine absolute amounts of mRNAs specific to four myosin heavy chain isoforms [MHCIIb, MHCIId(x), MHCIIa, and MHCIβ] in rat extensor digitorum longus muscle during forced contractile activity by chronic (10 h/day) low-frequency stimulation (CLFS). The induced changes in absolute and relative mRNA amounts were similar. MHCIIb mRNA decreased rapidly after 1 day, and MHCIIa mRNA increased after 3 days. MHCIId(x) started to decrease at day 7. After 42 days, the MHCIIb, MHCIId(x), MHCIIa, and MHCIβ mRNAs amounted to 2, 6, 90, and 2% of total MHC mRNAs, respectively. Changes at the protein level were studied in a second experimental series increasing CLFS (24 h/day, up to 100 days). Also under these conditions, MHCIβ reached only a fraction of 12% (2-fold elevation). The changes at the protein level remained restricted to the MHCIIb to MHCIIa transition, which agrees with the notion that the induced changes in MHC isoform expression primarily resulted from altered pretranslational activities. Rat fast-twitch muscle thus exhibits a restricted capacity for fast-to-slow conversion.

scholarly journals Isolation of multiple genomic sequences coding for chicken myosin heavy chain protein.

1982 ◽  
Vol 257 (1) ◽  
pp. 549-556
Author(s):  
J. Robbins ◽  
G.A. Freyer ◽  
D. Chisholm ◽  
T.C. Gilliam
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Genomic Sequences ◽  
Myosin Heavy Chain Protein
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