Jump to content

User:Voortman.lukas/sandbox

From Wikipedia, the free encyclopedia

Sirtuin 1

Sirtuin 1 is a protein that is made by the SIRT1 gene. Genes are portions of a cell's DNA that show the cell how to make a particular protein, and proteins carry out all of the major functions of the cell. This protein's job is to remove the Acetyl groups from proteins in order to help regulate other protein’s function and Gene expression[1]. This protein usually works with other proteins in a multi-protein complex, and does not simply act alone.

Sirtuin 1 Dimer

Function[edit]

The SIRT1 gene is a turned on in response to strain on the body. It is mostly working when there is a lack of food, and the body still needs energy. The Sirtuin 1 protein increases the rate of fat breakdown, and stops the body from storing any extra for later use[2]. This allows for more energy right away when there is food present, and uses up any fat already stored. The protein is believed to be an emergency response in humans when food was much more scarce. It allows the body to continue working well even though it doesn't have as much energy as it should.

Regulation of Gene Expression[edit]

Sirtuin 1 is also responsible for removing the acetyl groups from proteins called Histones, which wrap up DNA into tighter bundles. When DNA is wrapped up tightly, it cannot be used to aid in creating new proteins[3]. When Sirtuin 1 removes the acetyl group, it allows the DNA to unravel from the histones, and become available for use. This is believed to have an impact on aging, as cells slowly wrap up more and more of their DNA the older they become. In allowing cells to live longer, important cells in the body are not lost, and things like arthritis, joint pain, neurological disorders, and loss of mobility are lessened even when a person ages. Additionally, swelling and some toxins found in food can speed up the aging of the body, and Sirtuin 1 has been shown to decrease Inflammation and reduce the levels of toxins in the blood by removing the acetyl group from particular proteins and changing their activity.

Cell Senescence[edit]

Sirtuin 1 also plays the important role of keeping cells alive for longer. Under stress, cells will undergo a programmed death called Apoptosis, and this becomes a problem when the cell is very important. A gene labeled BAX regulates this process[4]. When Sirtuin 1 interacts with Bax, it decreases its ability to begin the cell’s death. This allows for important cells to continue functioning and dividing, even under stressful conditions. With important cells living for longer, the effects of aging are delayed[5].

Miscellaneous[edit]

Sirtuin 1 has also been shown to aid in multiple cellular processes, such as the Cell cycle, and responding to DNA damage[6]. Additionally, this protein has been shown to have a large impact in theMetabolism, neurological function, and cell lifespan.

History[edit]

SIRT 1 was originally discovered in response to its Homolog, or twin in another species, found in yeast. More specifically, Saccharomyces cerevislae, and it contains the homolog Sir2. It was found that this protein would allow a yeast cell to live longer and divide a greater number of times when there was a lot of the Sirtuin protein. Because of this, research was started to determine if humans had the same gene, and if it had the same role in our bodies.

Potential Uses[edit]

There are already multiple diets and supplements that have been proposed in order to harness some of the benefits SIRT 1 has to offer. A new diet involving fasting, as a simulation of starvation, will activate SIRT1, as well as resveratrol supplements as an alternative to diet. Additionally, diets and supplements have been suggested as a way of reducing the effects of aging and reducing the severity of some Neurological disorders[7]. Lastly, there is research being done by pharmaceutical companies to try and replicate the benefits of Sirtuin 1 by making proteins and Molecules that are similar to it, and then testing their effect.

Additionally, the ability of this protein to help the cell monitor the amount of sugar in the blood stream is more recently being focused on as a way to help obese people lose weight and regulate the Insulin levels of people withDiabetes mellitus[8]. Recently researchers are looking into the activation of the SIRT1 gene through the use of red wine. Red wine contains Resveratrol, and this has been found to increase the activity of Sirtuin 1.


Recently, however, there has been some controversy involving researchers and resveratrol. Evidence has been brought forth that shows researchers have been falsely recording and even fabricating results. Because of this, the interaction between resveratrol and SIRT1 has recently been called into question.

Further Reading[edit]

  • Cohen, H., Miller, C., Bitterman, K., Wall, N., Hekking, B., Kessler, B., . . . Sinclair, D. (2004). Calorie restriction promotes mammalian cell survival cy inducing the SIRT 1 deacetylase. Science, 305, 390-392.
  • Li, X. (2013). SIRT1 and energy metabolism. Acta Biochim Biophys Sin, 45, 51-60. doi: 10.1093/abbs/gms108.
  • Salminen, A., & Kaarniranta, K. (2009). SIRT1: Regulation of longevity via autophagy. Cellular Signaling, 21, 1356-1360. doi: 10.1016/j.cellsig.2009.02.014

References[edit]

  1. ^ "Q96RB6". Retrieved 3 March 2013.
  2. ^ Cohen, H (2004). "Calorie restriction promotes mammalian cell survival by inducing the SIRT 1 deacetylase". Science. 305 (5682): 390–392. doi:10.1126/science.1099196. PMID 15205477. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)
  3. ^ "Q96RB6". Retrieved 3 March 2013.
  4. ^ Botden, Ilse P. G.; Oeseburg, Hisko; Durik, Matej; Leijten, Frank P. J.; Van Vark-Van Der Zee, Leonie C.; Musterd-Bhaggoe, Usha M.; Garrelds, Ingrid M.; Seynhaeve, Ann L. B.; Langendonk, Janneke G.; Sijbrands, Eric J. G.; Danser, A. H. Jan; Roks, Anton J. M. (2012). "Red wine extract protects against oxidative-stress induced endothelial senescence". Clinical Science. 123 (8): 499–507. doi:10.1042/CS20110679. PMID 22563892.{{cite journal}}: CS1 maint: date and year (link)
  5. ^ Wang, Jing; Zhang, Yun; Tang, Lu; Zhang, Nan; Fan, Dongsheng (2011). "Protective effects of resveratrol through the up-regulation of SIRT1 expression in the mutant hSOD1-G93A- bearing motor neuron-like cell culture model of amyotrophic lateral sclerosis". Neuroscience Letters. 503 (3): 250–255. doi:10.1016/j.neulet.2011.08.047. PMID 21896316.{{cite journal}}: CS1 maint: date and year (link)
  6. ^ Scalera, F (2009). "Red wine decreases asymmetric dimethylarginine via SIRT1 induction in human endothelial cells". Biochemical and Biophysical Research Communications. 390 (3): 703. doi:10.1016/j.bbrc.2009.10.033. PMID 19833096. {{cite journal}}: More than one of |pages= and |page= specified (help); Unknown parameter |coauthors= ignored (|author= suggested) (help)
  7. ^ Huber, K (2011). "After the grape rush, sirtuins as epigenetic disorders". Bioorganic and Medicinal Chemistry. 19 (12): 3616–3624. doi:10.1016/j.bmc.2011.01.018. PMID 21306906. {{cite journal}}: Unknown parameter |coauthors= ignored (|author= suggested) (help)
  8. ^ Knight, Colette M.; Gutierrez-Juarez, Roger; Lam, Tony K.T.; Arrieta-Cruz, Isabel; Huang, Loli; Schwartz, Gary; Barzilai, Nir; Rossetti, Luciano (2011). "Mediobasal hypothalmic SIRT1 is essential for resveratrol's effects on insulin action in rats". Diabetes. 60 (11): 2691–2700. doi:10.2337/db10-0987. PMC 3198094. PMID 21896928.{{cite journal}}: CS1 maint: date and year (link)