BrainStorm Live Episode 5: Meet the Prions
Amprion’s CEO Dr. Russ Lebovitz discusses the role Prions (misfolded proteins) play in neurodegenerative diseases, including Alzheimer’s and Parkinson’s. What’s causing the diseases? It’s the misfolding of normal brain proteins into unusual shapes that stick to one another forming aggregates of various sizes. These aggregated forms of Prions are toxic to nerve cells and ultimately cause irreversible damage and cell death. Prions are rogue proteins.
Amprion’s breakthrough Prion Early Detection Science℠ can detect tiny amounts of Prions before any irreversible damage occurs. Early Detection is the keystone in finding successful treatments for Alzheimer’s and Parkinson’s.
Prions are Rogue Proteins
And it is now clear from many scientific and clinical studies that these diseases are very closely associated with misfolding of proteins that are normally present in the brain. But when they misfold, they form into new structures that appear to be toxic. And so, we’ve identified, predominantly, three misfolded proteins, and that is what Amprion is initially focused on, that seems to be the basis for Alzheimer’s and Parkinson’s, and a number of other diseases.
So, these proteins are Abeta, Tau and Synuclein, and I’ll take a second to describe what we believe happens with each of them, and what Amprion does uniquely. So, Abeta is a prevalent protein in the brain in its normal function, it helps maintain normal brain function. It can misfold in two different ways. If it misfolds in one way, it leads to very large clumps of protein, of misfolded Abeta in the brain that have been recognized for almost a hundred years now, and those are referred to as plaques.
So we’ve always known that plaque was an early sign of Alzheimer’s, but it took a while to understand that that is just a very large clump of misfolded Abeta Amyloid. Abeta can also misfold into a slightly different shape in which it forms much smaller, soluble clumps, or aggregates, of Abeta, and it’s these soluble, small aggregates of Abeta that spread easily throughout the brain and start to make the disease widespread.
There’s a second protein involved in Alzheimer’s called Tau, and it goes through something very similar to what I’ve described for Abeta. So, a normal function of Tau, which has a critical function in nerve cells, but it can misfold also in two different ways just like Abeta. It can misfold into a form that forms very large clumps. In the case of Tau, the large clumps are referred to as neurofibrillary tangles, or tangles, and they’re very easily visible under the microscope.
In fact, some of the earliest signs for Alzheimer’s that one could see under the microscope were the presence of plaques and tangles, because these are very large, insoluble aggregates. But again, Tau also misfolds into a slightly different shape that forms a soluble aggregate of Tau, and again, just like in the case of the soluble aggregates of Abeta, it’s the soluble form that moves between cells and is the basis for this being a progressive disease. The large clumps are immobile and can’t move within the brain. They are a sign, but probably not the direct cause. Whereas the soluble aggregates of Abeta and Tau are what we fear the most. It’s what spreads throughout the brain, it’s what causes these diseases to progress over time and affect large regions of the brain.
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