What is SIRT1?

SIRT1, a sirtuin, is commonly associated with resveratrol but I never really understood what one had to do with the other.  The answer is rather an in-depth topic that I will do my best to simplify in terms I was able to understand. 

Friendly disclaimer: Just as a reminder I am not a doctor, nor do I have any background in medicine or supplement science other than what I've learned through my own research.  When I read medical journals it takes me hours to get through one report because so much of my time is spent looking up strange words and trying to understand the definition.  It gets overwhelming and at times I find myself completely lost.  I am sure others can relate.

So here we go...

SIRT1 can be explained as our bodies "judge and jury" as to whether or not a cell should live or die.  When our body ages or is under attack our cells have to make a decision.  That decision is basically to either give up and die or to fight and try to repair itself from the damage thats being done to it.  SIRT1 is an enzyme that can help tell the cell what it should do.  So if there is more SIRT1 available, or activated, there is a better chance for that cell to try and repair itself and live on.

So what can cause damage to our cells?  Well, it seems the list is endless so to shorten it I'll point out a high calorie, high fat diet can cause cells to become damaged and eventually die off.  Certain diseases (type II diabetes is one) often caused by these two diet habits causes cells to become damaged and inhibit SIRT1 activation.  This brings in another cell factor, mitochondria, aka "cellular power plants".  The mitochondria are important for many reasons but as it relates to poor diet, they are effective in burning fat.  The more efficiently functioning mitochondria you have in a cell the more fat that will be burned and the greater the chance for cell survival.

So here is how this all comes together...

Resveratrol has been shown in studies to activate the SIRT1 enzyme which in turn helps tell a cell it should try to survive and repair itself.  The resveratrol in turn also helps to increase the function of the mitochondria within a cell.  This can help a cell, and in turn our bodies, to burn more fat, recover faster, increase endurance, mimic the effects of calorie restriction diets, and improve insulin sensitivity, among many other things.

Resveratrol and SIRT1 has become so important in research that it is said to have the potential to cure or treat numerous diseases such as prostate cancer, diabetes, MELAS syndrome,  anti-aging, and numerous other possibilities.  Only time will tell and I am going to do my best to be here when we find out.

Live Longer,

Markus

If you would like to learn more about SiRT1 please vist our sister site www.whatissirt1.com

Other Links and references:

http://www.jbc.org/cgi/content/abstract/280/17/17187
http://www.futurepundit.com/archives/003926.html
http://www.futurepundit.com/archives/003896.html
http://www.sirtrispharma.com/news.html
http://juvenon.com/jhj/vol3no08.htm
http://www.nature.com/nature/journal/v450/n7170/full/nature06261.html

Note:  the topic of SIRT1 is so expanse and ever changing that it is very difficult to describe in one post.  I encourage you to check out the links above and on our resource page to further research SIRT1 and Resveratrol.

Resveratrol Related Web Search

Comments

[FYH]

Resveratrol is a plant polyphenol capable of exerting beneficial metabolic effects which are thought to be mediated in large by the activation of the NAD(+)-dependent protein deacetylase SIRT1. Although resveratrol has been claimed to be a bona fide SIRT1 activator using a peptide substrate (Fluor de Lys-SIRT1 peptide substrate), recent reports indicate that this finding might be an experimental artifact and need to be clarified. Here, we show that: (i) the Fluor de Lys-SIRT1 peptide is an artificial SIRT1 substrate because in the absence of the covalently linked fluorophore the peptide itself is not a substrate of the enzyme, (ii) resveratrol does not activate SIRT1 in vitro in the presence of either a p53-derived peptide substrate or acetylated PGC-1alpha isolated from cells, and (iii) although SIRT1 deacetylates PGC-1alpha in both in vitro and cell-based assays, resveratrol did not activate SIRT1 under these conditions. Based on these observations, we conclude that the pharmacological effects of resveratrol in various models are unlikely to be mediated by a direct enhancement of the catalytic activity of the SIRT1 enzyme. In consequence, our data challenge the overall utility of resveratrol as a pharmacological tool to directly activate SIRT1.