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bp(MESHPP:Exercise) -> tscript(p(RGD:Nrf1))
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Approximately 61,000 statements.
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The magnitude of this increase was twofold (Fig. 3). An increase in PGC-1 protein of similar magnitude was seen 18 h after the fifth bout of exercise (data not shown). This finding is important because increases in mRNA do not always result in a parallel increase in protein. There was an increase in a smaller protein, which, like the full-length form, was completely competed away with a PGC-1 blocking peptide. The size of this smaller PGC-1 protein (34 kDa) is consistent with that of the smaller PGC-1 mRNA, which appears to be missing exon 8. Antibodies directed at the amino terminus (Fig. 3A) and the carboxyl terminus (Fig. 3A) recognized the shorter PGC-1 protein. It will be interesting to determine whether this smaller PGC-1 protein is in fact the translation product of the shortened PGC-1 mRNA and whether it has functional significance. Effect of exercise on expression of NRF-1 and NRF-2 NRF-1 protein binding was detected by electrophoretic mobility shift assay using an oligonucleotide containing a NRF-1 binding site from the ALA synthase promoter. NRF-2 protein binding was determined using an oligonucleotide containing the NRF-2 protein-binding site from the cytochrome oxidase subunit IV promoter. The NRF-1-specific band is shown by the arrow in Fig. 4A; quantitative analysis is shown in Fig. 4C. There was a 50% increase in NRF-1 binding in eight of nine muscles 18 h after the exercise; in other muscle, an increase was evident 12 h after exercise. This finding of an increase in NRF-1 DNA binding is in keeping with the observation of Murakami et al. (37) of a 50% increase in NRF-1 mRNA in soleus muscle of rats 6 h after a bout of running.
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