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Longevity Briefs: In Search Of An ‘Exercise Drug’

Posted on 1 August 2022

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Longevity briefs provides a short summary of novel research in biology, medicine, or biotechnology that caught the attention of our researchers in Oxford, due to its potential to improve our health, wellbeing, and longevity.

Why is this research important: Regular exercise is one of the most effective ways of improving health and longevity. In particular, high muscle strength achieved through exercise is linked to lower mortality at a given age. If we could produce a drug that mimicked just a fraction of these benefits, we would be able to significantly improve human health. Unfortunately, the necessary understanding of how exactly exercise exerts its health benefits is currently lacking.

What did the researchers do: In this study, researchers set out to investigate the signalling molecules involved in the response to exercise, using a technique called phosphoproteomics. This is a technique that identifies and catalogues proteins that have been modified through the addition of a phosphate group. Phosphate groups are added or removed from proteins in order to alter their activity, so measuring proteins in this way gives scientists clues as to whether a protein is being activated as part of some signal – in this case the signals that occur during and following exercise.

How the addition of a phosphate group activates a protein. Other proteins are instead deactivated by the addition of phosphate groups.
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Researchers used this technique to analyse the muscle of humans who underwent sprint, endurance, or resistance exercise.

Key takeaway(s) from this research: Throughout the proteins identified, the researchers found 5486 locations at which phosphate groups could be added that were associated with at least one of the three exercise types. Only 420 phosphorylation sites were associated with all three exercise types. Among these, the researchers were able to single out a site of particular importance called S67, which is located on the memorably named protein C18ORF25. When they genetically modified mice to lack C18ORF25, they found that these mice had smaller, weaker muscles and reduced exercise capacity.

They then investigated whether they could restore the mice’s muscles by reintroducing a protein similar to phosphorylated C18ORF25. To do this, they gave the mice a virus containing genetic material coding for a altered version of C18ORF25 that is always active. They found that this partially restored the mice’s lost muscle function.

C18ORF25 appears to be important, at least in mice, but we will still need to confirm whether manipulating C18ORF25 in healthy mice has any beneficial effects.

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    Phosphoproteomics of three exercise modalities identifies canonical signaling and C18ORF25 as an AMPK substrate regulating skeletal muscle function:

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