What is protein thermal shock? Can proteins help us fight cancer?

Russian scientists claim to have successfully tested a protein thermal shock drug that cures all types of cancer. While this drug still has to be tested in practice, what should we know about thermal shock protein? And how does it treat cancer?

According to the definition of the National Cancer Institute (USA), a thermal shock protein is one of a group of proteins that helps protect cells from stresses such as heat, cold, and lack of glucose (sugar) or oxygen. Thermal shock proteins help other proteins to function in normal cells and can be present at high levels in cancer cells. Blocking the action of a thermal shock protein called HSP90 is being investigated for cancer treatment. Other thermal shock proteins including HSP70 and gp96 are being studied in vaccines for cancer treatment. Heat shock proteins are also known as HSP or protein stress.

According to Wikipedia, thermal shock proteins (HSP) are a family of proteins produced by cells in response to stressful conditions. They are first described in relation to thermal shock but are now also expressed in other shocks including cold exposure, UV rays, and during wound healing or tissue replacement. Many members of this group perform chaperone functions (accompanied) by stabilizing new proteins to ensure accurate folding or by helping to regenerate proteins that have been damaged by stress cells. This increase in expression is regulated at the transcription level. The sudden increase in thermal shock proteins is an important part of the thermal shock response and is caused mainly by the thermal shock factor (HSF). HSP is found in most living organisms, from bacteria to humans.

Heat shock protein is one of a group of proteins that helps protect cells from stress.

Thermal shock proteins are named after their molecular weight . For example, HSP60, HSP70 and HSP90 (the most studied HSP) indicate the families of thermal shock proteins in turn are 60, 70 and 90 kilodalton respectively. Based on molecular weight, HSP is divided into 5 main groups: HSP27, HSP60, HSP70, HSP90 and HSP110 / 104.

According to Science Direct, thermal shock proteins prevent the formation of nonspecific protein tumors and they support proteins in acquiring their normal architecture. In addition, heat shock proteins may have dead cell antigens and actively participate in various processes such as tumor cell proliferation, invasion, metastasis and death.

Remarkably, these proteins have been reported to increase significantly in a variety of human cancers. Their overexpression is closely related to treatment resistance and low survival. In this way, the HSP can have significant therapeutic significance and they can be targeted according to specific drugs.

In short, scientists have long known that thermal shock proteins are present in each cell to combat stress. Researchers later discovered its new use when it played an active role in helping the immune system identify cancer cells in response to it in time. However, its synthesis for cancer treatment is still in the process of research.

Stresses of physical, chemical or biological origin, as well as diseases such as cancer can cause the accumulation of heat shock proteins necessary for the survival of cancer cells.In the picture is illustrated for the main localization of HSP60, present in mitochondria, and 3 stimulating nuclear thermal shock proteins: HSP27, HSP70 (also found in cell membranes) and HSP90.(Source: Frontiers).

Role of thermal shock protein

Main role: Keep order

Thermal shock proteins come with other cellular proteins, protecting them from being lost, improperly folded or incorrectly inserted while forming larger blocks, as in the examples below:

1. HSP40 provides a new series of amino acids formed for HSP70, this protein "grabs" the molecule, helps it fold into a proper functional form and then releases it.
2. HSP60 attracts a new series of amino acids or a protein that has lost its structure and receives it. The chemical bonds in the cage make the protein assume that the folding roll shape is correct.
3. HSP90 receives folded proteins from chaperone molecules and helps combine them into a larger protein structure, such as a cell receptor.

Second task: Activating the immune response

When a cell is cancerous or infected by a pathogen, it produces proteins that are not present in normal cells. The fragmentation of such cells may then be able to act as antigens, which stimulate the immune response. But immune cells must first be aware of the problem. Heat shock proteins, mainly members of the HSP90 and HSP70 families, engage in alarms and identify culprits.

1. HSP provides antigens from diseased cells to antigen-presenting cells (APC) of the immune system, through a surface receptor called CD91.
2. After capturing antigens, APC transmits inflammatory signals to recruit other immune cells and presents that antigen on its surface to a T cell.
3. By prioritizing detection of target antigens, T cells proliferate and together with their brothers seek to kill disease cells.

According to Discovery Medicine magazine, the relationship between HSP and tumor immunity was revealed about three decades ago, when researchers found that vaccination of animals with HSPs was purified from tumor cells. has caused specific immunity against tumors. However, HSPs that are available from normal cells do not produce immunity. Since then, some HSPs originated from tumors that were investigated as tumor vaccines or in animal models or melanoma patients. These HSPs include HSP70, HSP110, GRP78, GRP94 (also called gp96) protein and GRP170 and laperate whole chaperone cells.

Even so, cancer treatment using thermal shock protein has not made much progress. Until early March, Russian media reported that scientists in the country have claimed to find a cure for all types of cancer, including terminal cancer. It is a measure of thermal shock protein.

Russian scientist Andrei Simbirtsev.

Andrei Simbirtsev, deputy director of the Federal Institute of Biomedical Sciences, said that the amount of natural heat shock protein that exists in humans is very small, but so far Russian scientists have successfully synthesized it. They created a human gene that produces this protein and then cloned it.

Russian scientists say they have tested clinically this drug successfully in mice with melanoma, and noted that thermal shock protein works very well for every stage of the disease without Any side effects or toxicity.

The success of the new drug was discovered by Russian scientists thanks to experiments in space, where there is a suitable environment (without the attraction of the Earth) to create a kind of super-pure crystal serving for X-ray analysis. Russian scientists have put the ultrapure protein in the microchip and sent it to the Space Station. After 6 months of "traveling" in the microchip will get the ideal crystal type and transfer to analysis in Russia and Japan.

This thermal shock protein drug is expected to go into production in 3-4 years.

While Western media is cautious about this information (almost no British, American or other developed countries report on this achievement), and we have to wait a few more years to be able to to testify the claims of Russian scientists, but we can hope that with the advancement of science and technology, all the difficult problems of life, such as cancerous disease will be gradually solved.

1. Russia claims to find a cure for all cancers