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expression are increased in human skeletal muscle after physical exercise
1 Clinique romande de réadaptation, SUVACare, Sion, Switzerland
2 Department of Cell Biology, The Scripps Research Institute, La Jolla, USA
3 IRBB-Parc Cientific de Barcelona and Departament de Bioquímica i Biologia Molecular, Universitat de Barcelona, Spain
Mitochondrial impairment is hypothesized to contribute to the pathogenesis of insulin resistance. Mitofusin (Mfn) proteins regulate the biogenesis and maintenance of the mitochondrial network, and when inactivated, cause a failure in the mitochondrial architecture and decreases in oxidative capacity and glucose oxidation. Exercise increases muscle mitochondrial content, size, oxidative capacity and aerobic glucose oxidation. To address if Mfn proteins are implicated in these exercise-induced responses, we measured Mfn1 and Mfn2 mRNA levels, pre-, post-, 2 and 24 h post-exercise. Additionally, we measured the expression levels of transcriptional regulators that control mitochondrial biogenesis and functions, including PGC-1
, NRF-1, NRF-2 and the recently implicated ERR. We show that Mfn1, Mfn2, NRF-2 and COX IV mRNA were increased 24 h post-exercise, while PGC-1 and ERR mRNA increased 2 h post-exercise. Finally, using in vitro cellular assays, we demonstrate that Mfn2 gene expression is driven by a PGC-1 programme dependent on ERR. The PGC-1/ERR-mediated induction of Mfn2 suggests a role of these two factors in mitochondrial fusion. Our results provide evidence that PGC-1 not only mediates the increased expression of oxidative phosphorylation genes but also mediates alterations in mitochondrial architecture in response to aerobic exercise in humans.
(Received 3 June 2005;
accepted after revision 15 June 2005;
first published online 16 June 2005)
Corresponding author A. P. Russell: Clinique Romande de Réadaptation, Case postale 352, Av. Gd-Champsec 90, 1951 Sion, Switzerland. Email: aaron.russell{at}crr-suva.ch
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