What does Sirtuins do?

Sirtuins helps regulate your cell health. This is what you need to know how they work, what they can do for your body, and why they rely on NAD plus to work.

Sirtuins is a family of proteins that regulate cell health. Sirtuins plays a key role in regulating cell stability. In vivo balance involves maintaining cell balance. However, Sirtuins functions only if coenzyme NAD plus (niacin adenine dinucleotide) is present in all living cells.

How Sirtuins
thinks about the body's cells like an office by Using NAD plus regulating cell health. In the office, there are many people who do a variety of tasks with the ultimate goal of staying profitable and fulfilling the company's mission as efficiently as possible for as long as possible. In cells, much remains to be done to achieve the ultimate goal of staying healthy and functioning as effectively as possible. Just as the company's priorities change due to a variety of internal and external factors, so do the priorities in the cell. Someone must run the office and specify when to accomplish what, who to do and when to change course. In the office, that will be your CEO. In the body, at the cellular level, it's your silence.

Sirtuins is a family of seven proteins that play a role in cell health. Sirtuins only works if coenzyme NAD plus (niacin adenine dinucleotide) is present in all living cells. NAD plus is critical for cell metabolism and hundreds of other biological processes. If sirtuins are the CEO of the company, then NAD plus is the money to pay the CEO and employees' salaries while keeping the lights on and paying the rent for office space. Without it, companies and institutions would not be able to function. But the level of NAD-plus decreases with age, which also limits the function of the silent regulating protein. Like everything in the human body, it's not that simple. Sirtuins manages everything that happens in your cells.

Sirtuins is a protein. What does that mean? Sirtuins is a protein family.
Protein may sound like a protein in the diet - found in legumes and meats as well as in protein shakes - but in this case, we're talking about molecules called proteins that work in many different functions in human cells. Think of proteins as part of a company, each focusing on its specific functions while coordinating with other departments.

A well-known protein in the body is hemoglobin, which is part of the globulin family of proteins that transport oxygen throughout the bloodstream. Myoglobin is a counterpart to hemoglobin, which together form the globulin family. Your body has nearly 60,000 protein families. Hemoglobin is one of two protein families, while Cerseiin is one of seven. Of the seven silent regulatory proteins in the cells, three play a role in the mitochondria, three of which play a role in the nucleus, and one plays a role in the cytoplasm, each playing multiple roles. However, the basic function of silent regulatory proteins is that they remove acetylyl from other proteins.

Acetyl controls a specific reaction. They are physical labels on proteins, and other proteins can also identify proteins that react with them. If the protein is the cell's department and the DNA is the CEO, acetyl is the availability status of each department head. For example, if a protein is available, sirtuin can work with the protein to make something happen, just as the CEO can make something happen with the available department head.

Sirtuins works with acetyl groups by performing so-called deacetylation. This means that they recognize that there is an acetyl base on the molecule and then remove the acetyl base, thus preparing the molecule for work. One way sirtuins work is by removing acetylyl (making acetylation) bioproteins (e.g. histones). Sirtuins, for example, deacetylates histones, which are part of a concentrated form of DNA that is chromate-stained. Histein is a large chunk of protein wrapped in DNA itself. Think of it as a Christmas tree, and the DNA chain is a beam of light. When the histone has acetyl base, the chromium is turned on or untied.

This untangled chromosome means that DNA is transcribed, an essential process. But it doesn't need to be untangled because it's easy to damage in that location, just as Christmas lights can tangle together, or light bulbs are clumsy or damaged for too long. When histones are deacetyl-based by Cersei, the chromium is closed or tightly entangled, which means that gene expression is stopped or silenced.

We've only known Sirtuins for 20 years, and its main function was discovered in the 1990s. Since then, researchers have flocked to study them to determine their importance, while also raising questions about what else we can learn.

Sirtuins' discovery and history
Geneticist Dr.
Amar Klar discovered the first Cersei protein, or SIR2, in the 1970s and identified it as the gene that controls the mating capacity of yeast cells. A few years later, in the 1990s, researchers found other genes of the same origin (structurally similar) as SIR2 in other organisms, such as worms and fruit flies, and named them sirtuins. The number of silent regulated proteins in each organism is different. For example, yeast has five silent regulatory proteins, bacteria have one silent regulatory protein, mice have seven silent regulatory proteins, and humans have seven silent regulatory proteins.

The fact that sirtuins were discovered across species meant that they were "conservative" in evolution. "Conservative" genes have universal functions in many or all species. However, it is not clear how important sirtuins really are. In 1991, Leonard Guarente, a biologist at the Massachusetts Institute of Technology and a graduate student, Nick Augusto and Brian Kennedy, co-founder of Elysium, conducted experiments to better understand how yeast ages.

By chance, Austria tried to create a stressful environment by growing various yeast strains from samples he had stored in the refrigerator for months. Only a fraction of these strains can grow from here, but Guarent and his team have identified a pattern: the best yeast strains that survive in the refrigerator live the longest. This provides guidance for Guarente, so he can focus only on these long-lived yeast strains.

This led to the identification of SIR2 as the gene that promotes yeast life. It is important to note that, to date, there is no evidence to extend this study to humans, and more research is needed on the effects of SIR2 on humans. As a result, the Gualent laboratory found that removing SIR2 could significantly shorten the life of yeast and, most importantly, increase the number of copies of the SIR2 gene from one to two, which could extend the life of yeast. However, natural methods of activating SIR2 have not yet been found.

This is where acetylyl works. Initially, sir2 was thought to be a deacetylase - meaning it could remove those acetylyls from other molecules - but no one knows if that's true because all attempts to prove this activity in test tubes have proved negative. Guarente and his team were able to find that SIR2 in yeast deacetylation of other proteins is only possible if coenzyme NAD plus (niacin adenine dinucleotide) is present.

In Guarente's own words: "SIR2 would not have done anything without NAD plus." This is a key finding in Sirtuins biology. ”

future research is largely related to aging and metabolic activity. "There could be 12,000 papers on Sirtuin right now," Guarent said. "When we found the activity of THE Decacetylase that NAD plus depends on, the number of papers was within 100s."
As the field of sirtuins continues to expand, this leaves incredible research opportunities for how the activation of sirtuins using NAD plus precursors leads to more exciting discoveries.

Source (Chinese)

What does Sirtuins do? - Know (zhihu.com)