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Exercise translocates RIP140 to the cytoplasm in human skeletal muscle
Author(s) -
Sällstedt Eva-karin Sara,
Ydfors Mia,
Norrbom Jessica,
Sundberg Carl Johan
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.734.5
Subject(s) - cytoplasm , mitochondrial biogenesis , chemistry , microbiology and biotechnology , skeletal muscle , mitochondrion , messenger rna , receptor , medicine , endocrinology , gene , biology , biochemistry
In response to exercise, muscles adapt with a multitude of gene expression changes and protein modifications. One of the most profound changes is an increased mitochondrial biogenesis. The co‐repressor RIP140 interacts with several nuclear receptors and is recruited by transcription factors and co‐activators such as PGC‐1α and NRF‐1. Therefore, RIP140 may take part in the regulation of mitochondrial biogenesis. Purpose To investigate 1. if an acute bout of exercise reduces the inhibitory action of RIP140 through translocation from the nucleus to the cytoplasm and 2. the temporal resolution of RIP140 mRNA expression before and up to 24h after exercise. Methods Healthy men (n=4) and women (n=3) performed 1h of cycling exercise at 70 % of VO2max. Skeletal muscle biopsies were obtained before and after exercise (pre, 30′, 2h, 6h and 24h). Results RIP140 protein abundance increased in the cytoplasmic fraction 24h after exercise (n=3). RIP140 mRNA expression (n=7) was significantly increased 6h after exercise and returned to baseline values at 24h. Conclusion An acute bout of exercise appears to translocate RIP140 protein from the nucleus to the cytoplasm. This would decrease the inhibitory action of RIP140 on nuclear genes encoding mitochondrial proteins and might therefore be part of the adaptive mitochondrial response seen with training.