Neurodegenerative Diseases

Biologist talks about mutations of proteins, Alzheimer's disease and the role of chaperones in the human body.What is the cause of neurodegenerative diseases? What role in the human body play a chaperone? What are the different approaches to the treatment of Alzheimer's disease and mad cow disease?

Quite a lot of neurodegenerative diseases attributed to the so-called amyloid diseases, or conformational diseases. Their essence is, that cells surrounding nerve cells fall amyloid aggregates - a protein aggregates, which have a specific structure. For a long time it was thought that it is because of the emergence of these units and having these diseases. Sometimes they are called conformational because it is associated with proteins.

Of course, if we have in a certain protein or a mutation occurs simply by changing the structure of the modification, for example chemical, such proteins alter their conformation and start to form aggregates. A frequent case is the so-called prion diseases, an infectious protein - the so-called prion - is attached to the native prion protein, native protein, changing its conformation, is also converted into the infectious protein, and further formed aggregates.

Such diseases are quite a few, but I will mention only two. Firstly, it is Alzheimer's disease - perhaps the most unpleasant disease because so many sick people, tens of millions, especially in developed countries; when life expectancy increases, these patients become very much. Somewhere in the half of the people who reach the age of 90 years, already developing Alzheimer's disease. It is very expensive, because these people can not be left alone, we must always take care of them, sometimes they are even inclined to suicide. In addition, the disease itself is very annoying, because physically it is the person that you know well, and due to the fact that he does not remember, do not know you and behaves inappropriately, this is a big problem for the family.

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In a world of many institutions working, a lot of labs are going to a conference on 5-10 thousand people associated with the study of this disease. Molecular mechanisms almost completely known, but no medication is still no, just a little removed symptoms.

The second amyloid disease, too, is also a conformational disease, which has made a lot of noise about 10-15 years ago, when there was. They began to talk about this disease, like mad cow disease, or scientifically called bovine spongiform encephalopathy. In humans, the disease is almost does not occur, there is a hereditary form, but it's very rare cases, a few cases in the whole of Russia in the year. A contagious disease is, but sick people usually 10-15 years, because very long incubation period.

Compare course of Alzheimer's disease and prion disease incidence or costs can not be, but it is very frustrating today ate some contaminated meat, and 10-15 years sick strange disease. I remember in those days, when all the newspapers wrote about it, even the old woman 90-year-old stopped eating meat. This disease is slightly different, because there is a prion that transmits the disease. And here, too, almost everything we know about this disease, but how to prevent the disease - still do not know.

About 15 years ago, it has been suggested that these diseases can be treated with so-called chaperones.

Chaperones have opened a long time ago - in the early '90s, and even a little earlier. It is the proteins that help other proteins to fold correctly, or do not give to aggregate with each other. The name comes from the French word: it is such a governess who accompanied women in society, not that anything bad happened to them. Approximately the same function are believed to operate chaperones: the proteins are not aggregated, not changed, and so forth..
If amyloid diseases are associated with the fact that very large aggregates are formed in the brain of humans or animals, it is clear that if we have a chaperone, they are chopped into small pieces of these units, and the disease will disappear. It was assumed that they would enter the chaperones in the brain, although this is not an easy task, it would be possible even transgenic animals, in principle, for the sake of such a noble task to create.

It turned out that all is not so simple. Around the same time, it became clear that these large aggregates, which are in the brain, there is nothing particularly wrong with do not, and are dangerous just small units, so-called prion oligomers or of the same beta-amyloid that cause Alzheimer's disease. They are dangerous and cause cell death. So if we cut into small pieces of aggregates, it will be even worse. And it became clear that it is unlikely using chaperones can be cured.
Information on the effects of chaperones was very contradictory, because one thought that they destroy the units, another felt that they, on the contrary, make bad from good protein amyloid aggregates. It was connected with the fact that using chaperones from different sources. For example, a look at how will affect chaperones derived from the cells of microorganisms on prions, which are in the brain of animals. Clearly, they do not seem to be encountered in the brain, these two protein. Gradually it became clear that it depends not only on the fact that there is a chaperone, some protein conformational changes and aggregation of their interaction, and all connected with the fact, in what conformation, in which the state itself is the chaperone.

If you have this protein in the cell in an active state, if it has a sufficient amount of energy - it needs energy, adenosine triphosphate, - in order to function, then everything is fine, nothing wrong with it either prion or the beta-amyloid does not. And if something spoiled, promodifitsirovan, for example, oxidation of some proteins, there may occur special forms of these proteins, they are connected to the chaperone and spoil it. As in the two-cylinder engine, if one cylinder is blocked, the second seems to be normal, but the work as it should not. So it is with chaperones.

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Good, functionally active chaperones nothing wrong with prion amyloid proteins and other do not. On the contrary, it may even prevent their aggregation. And if he chaperone a little spoiled, then when it is joined by even a good prion protein with unchanged conformation, he then can take the wrong conformation, and it can be collected fibrils bad units, and so on. D. It is important not just to give proteins as additional chaperones in animal or human brain, but it is necessary that the system worked well. This is much easier than creating transgenic animals or attempt to enter any proteins in the brain. Therefore it is sufficient, as has been known to drink a good oxidants that do not occur correctly folded proteins to give a lot of energy in order to make them operational, and then all will be well with prions. The main thing, chaperones to keep in good condition. We are talking about the chaperone, who is in all cells. I mentioned earlier that there chaperones microorganisms, and they may have slightly different function playing the infection of animals, especially in the case of prion proteins.

The fact that the BSE contamination occurs if one eats poorly processed meat animal patient, even if it is well-roasted, and prions are first hit in the gastrointestinal tract and then into the brain and cause disease. The probability of this process is low, the disease is rare, even topically infectious prions, but nevertheless it happens.
How is the process of penetration of infectious prions in the brain, do not know really. It is possible that this play a role microorganisms that live in the gastrointestinal tract. Because they are those microorganisms most chaperones, and if the cells are destroyed, are constantly subjected to autolysis, these chaperones may enter the gastrointestinal tract and there meet prions. It has been shown that if these chaperones meet prion protein, they are, firstly, to bring them more pronounced amyloid condition and make the small particles a few nanometers in size, which will make it easier to penetrate the intestinal wall. It is possible that just infecting human major role played by those microorganisms which have live in the gastrointestinal tract, they are very much, they can be different, and chaperones they may be different. Therefore, depending on the microflora contamination can occur or not occur.

The main problem, which now appears in the study of amyloid diseases is the fact that it is necessary to find those compounds that will prevent the aggregation of amyloid. Such compounds are, they can be found even in a well-known drugs, not even in the preparations, but simply in spices such as turmeric - it pretty well prevents protein aggregation. There are connections to more pronounced antiagregatsionnym action antiplatelet agents. And quite possibly, it will be possible to find some connection that will prevent this aggregation, translate, for example, in the form of a very large unit, stimulating aggregation, preventing thereby killing the cell.