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Ubiquitin ligase gene expression in healthy volunteers with 20‐day bedrest
Author(s) -
Ogawa Takayuki,
Furochi Harumi,
Mameoka Mai,
Hirasaka Katsuya,
Onishi Yuko,
Suzue Naoto,
Oarada Motoko,
Akamatsu Motoki,
Akima Hiroshi,
Fukunaga Tetsuo,
Kishi Kyoichi,
Yasui Natsuo,
Ishidoh Kazumi,
Fukuoka Hideoki,
Nikawa Takeshi
Publication year - 2006
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.20611
Subject(s) - ubiquitin ligase , ubiquitin , muscle atrophy , skeletal muscle , gene expression , atrophy , biology , downregulation and upregulation , protein degradation , gene , endocrinology , medicine , microbiology and biotechnology , genetics
In animal models, several ubiquitin ligases play an important role in skeletal muscle atrophy caused by unloading. In this study we examined protein ubiquitination and ubiquitin ligase gene expression in quadriceps femoris muscle from healthy volunteers after 20‐day bedrest to clarify ubiquitin‐dependent proteolysis in human muscles after unloading. During bedrest, thickness and cross‐sectional area of the quadriceps femoris muscle decreased significantly by 4.6% and 3.7%, respectively. Ubiquitinated proteins accumulated in these atrophied human muscles. A real‐time reverse transcription–polymerase chain reaction system showed that bedrest significantly upregulated expression of two ubiquitin ligase genes, Cbl‐b and atrogin‐1. We also performed DNA microarray analysis to examine comprehensive gene expression in the atrophied muscle. Bedrest mainly suppressed the expression of muscle genes associated with control of gene expression in skeletal muscle. Our results suggest that, in humans, Cbl‐b– or atrogin‐1–mediated ubiquitination plays an important role in unloading‐induced muscle atrophy, and that unloading stress may preferentially inhibit transcriptional responses in skeletal muscle. Muscle Nerve, 2006