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Reliable determination of training‐induced alterations in muscle fiber composition in human skeletal muscle using quantitative polymerase chain reaction
Author(s) -
Ellefsen S.,
Vikmoen O.,
Zacharoff E.,
Rauk I.,
Slettaløkken G.,
Hammarström D.,
Strand T. A.,
Whist J. E.,
Hanestadhaugen M.,
Vegge G.,
Fagernes C. E.,
Nygaard H.,
Hollan I.,
Rønnestad B. R.
Publication year - 2014
Publication title -
scandinavian journal of medicine and science in sports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.575
H-Index - 115
eISSN - 1600-0838
pISSN - 0905-7188
DOI - 10.1111/sms.12185
Subject(s) - myosin , skeletal muscle , biceps , muscle fibre , vastus lateralis muscle , immunohistochemistry , biology , real time polymerase chain reaction , reverse transcription polymerase chain reaction , polymerase chain reaction , gene expression , medicine , anatomy , gene , microbiology and biotechnology , biochemistry
Determination of muscle fiber composition in human skeletal muscle biopsies is often performed using immunohistochemistry, a method that tends to be both time consuming, technically challenging, and complicated by limited availability of tissue. Here, we introduce quantitative reverse transcriptase polymerase chain reaction ( qRT ‐ PCR) ‐based Gene‐family profiling ( G ene F am) of myosin heavy chain ( MyHC ) mRNA expression as a high‐throughput, sensitive, and reliable alternative. We show that G ene F am and immunohistochemistry result in similar disclosures of alterations in muscle fiber composition in biopsies from musculus vastus lateralis and musculus biceps brachii of previously untrained young women after 12 weeks of progressive strength training. The adaptations were evident as (a) consistent increases in MyHC2A abundance; (b) consistent decreases in MyHC2X abundance; and (c) consistently stable MyHC1 abundance, and were not found using traditional reference gene‐based qRT ‐ PCR analyses. Furthermore, muscle fiber composition found using each of the two approaches was correlated with each other ( r = 0.50, 0.74, and 0.78 for MyHC1 , A , and X , respectively), suggesting that G ene F am may be suitable for ranking of individual muscle phenotype, particularly for MyHC2 fibers. In summary, G ene F am of MyHC mRNA resulted in reliable assessment of alterations in muscle fiber composition in skeletal muscle of previously untrained women after 12 weeks of strength training.