Sirtuin ActivationScientists have found a naturally occuring chemical called nicotinamide that interferes with the functioning of the sirtuin (also called Sir2) enzyme. Sirtuin has been shown to play a role in extending the lifespan of yeasts, worms and flies, and is known to have some effect on diabetes, inflammation and cancers in humans. Controlling sirtuin's functioning could lead to treatments for these diseases, and possibly even have anti-aging applications. Sirtuin works by removing acetyl groups from certain proteins, which turns the protein on or off. When a nicotinamide molecule binds with sirtuin, it fills a depression in the enzyme where the acetyl groups fit, thus deactivation the enzyme. Molecules that mimic nicotinamide and block sirtuin's activity might be useful in treating diabetes, based on Puigserver's recent discoveries. Or the structural clues could be used to do the opposite, to turn up sirtuin's activity, which might restart a tumor suppressor gene called p53 that is erroneously shut off in many cancers. But those are just two examples. This is just one example of promising work being done to better understand the way enzymes work in our bodies, which is key to controlling those processes. Every year there are hundreds of reports like this that add incrementally to our picture of how we function, but we wonder if there are enough people who understand the bigger picture and can synthesize all these facts into a coherent and useful picture. Too often the biochemists don't know what is going on in bio-nanotech, and the lab researchers don't know what clinical trials are on-going. It used to be that information was difficult to gain access to -- now it so readily available that we have information overload. |
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