Proteins that are Toxic to the Heart and Nerves may Help Prevent Alzheimer's Diseas
Researchers’ previous studies have known that a sticky plaque called amyloid beta is a hallmark of Alzheimer’s disease and is toxic to brain cells. In the mid-1990s, researchers discovered other proteins in these plaques. One of these is a protein called thyrotropin (TTR), which seems to have a protective effect on brain cells. When mice with Alzheimer's disease models were genetically modified to produce more TTR, they developed into Alzheimer's-like disease at a slower rate. When their TTR was lowered, they would develop related symptoms faster.
In healthy people and animals, TTR helps transport thyroid hormone and vitamin A derivative retinol to the desired location in the body. To do this, the TTR forms tetramers. But when they're separated into molecules called monomers, these individual fragments can form sticky fibrils like amyloid beta, these fibers combine to form toxic clumps in the heart and nerves, causing rare amyloidosis. In this case, amyloid will accumulate in the organ and interfere with its function.
The researchers wondered if there was a link between the different roles of TTR in preventing and causing amyloid protein-related diseases. To explore this question, the scientists developed nine different variants of TTR, which have different propensity to separate into aggregated monomers to form sticky fibrils. Some variants did this quickly within a few hours, while others were slow. Other variants are very stable and do not break down into monomers at all.
When the researchers mixed these TTR variants with amyloid β and placed them on neuronal cells, they found that the toxicity of amyloid β residues was significantly different. The variant, which separated into monomers and quickly aggregated into fibrils, offered some protection, but was short-lived. Those that took longer to separate into monomers provided longer protection. Those that were never isolated provided no protection from amyloid beta at all.
Therefore, the researchers suspected that a part of TTR binds to amyloid β, thereby preventing amyloid β from forming aggregation by itself. However, when the protein was in tetramer form, this important TTR seemed to be hidden. To be sure, computational studies have shown that part of this protein hidden when the leaflets are joined together may stick to amyloid.
Researchers are currently testing whether this modified TTR peptide can prevent or slow the progression of Alzheimer's disease in a mouse model. If they succeed, this protein fragment can become the basis for new treatments for this intractable disease, bringing hope to patients with Alzheimer's disease.
At present, Wuxi Donglin Sci & Tech Development Co.,Ltd. has developed a variety of ELISA products for testing TTR level. If you want to know about the TTR ELISA kit, you can directly visit the website:
http://www.dldevelop.com/Research-reagent/dl-ttr-b.html
http://www.dldevelop.com/Research-reagent/dl-ttr-hu.html
http://www.dldevelop.com/Research-reagent/dl-ttr-mu.html
http://www.dldevelop.com/Research-reagent/dl-ttr-p.html
http://www.dldevelop.com/Research-reagent/dl-ttr-ra.html
In healthy people and animals, TTR helps transport thyroid hormone and vitamin A derivative retinol to the desired location in the body. To do this, the TTR forms tetramers. But when they're separated into molecules called monomers, these individual fragments can form sticky fibrils like amyloid beta, these fibers combine to form toxic clumps in the heart and nerves, causing rare amyloidosis. In this case, amyloid will accumulate in the organ and interfere with its function.
The researchers wondered if there was a link between the different roles of TTR in preventing and causing amyloid protein-related diseases. To explore this question, the scientists developed nine different variants of TTR, which have different propensity to separate into aggregated monomers to form sticky fibrils. Some variants did this quickly within a few hours, while others were slow. Other variants are very stable and do not break down into monomers at all.
When the researchers mixed these TTR variants with amyloid β and placed them on neuronal cells, they found that the toxicity of amyloid β residues was significantly different. The variant, which separated into monomers and quickly aggregated into fibrils, offered some protection, but was short-lived. Those that took longer to separate into monomers provided longer protection. Those that were never isolated provided no protection from amyloid beta at all.
Therefore, the researchers suspected that a part of TTR binds to amyloid β, thereby preventing amyloid β from forming aggregation by itself. However, when the protein was in tetramer form, this important TTR seemed to be hidden. To be sure, computational studies have shown that part of this protein hidden when the leaflets are joined together may stick to amyloid.
Researchers are currently testing whether this modified TTR peptide can prevent or slow the progression of Alzheimer's disease in a mouse model. If they succeed, this protein fragment can become the basis for new treatments for this intractable disease, bringing hope to patients with Alzheimer's disease.
At present, Wuxi Donglin Sci & Tech Development Co.,Ltd. has developed a variety of ELISA products for testing TTR level. If you want to know about the TTR ELISA kit, you can directly visit the website:
http://www.dldevelop.com/Research-reagent/dl-ttr-b.html
http://www.dldevelop.com/Research-reagent/dl-ttr-hu.html
http://www.dldevelop.com/Research-reagent/dl-ttr-mu.html
http://www.dldevelop.com/Research-reagent/dl-ttr-p.html
http://www.dldevelop.com/Research-reagent/dl-ttr-ra.html
