BrainStorm Live Episode 6: What Is The Molecular Basis For Alzheimer’s?
Amprion CEO Dr. Russ Lebovitz explains the molecular basis and specific Prions structure underlying Alzheimer’s disease. The bad players are: Abeta and Tau. Both of these Prions or misfolded proteins are proteins gone rogue. Amprion’s breakthrough Prion Early Detection Testing℠ detects these rogue proteins in people who are at-risk with Alzheimer’s prior to any clinical symptoms.
Prions Structure in Alzheimer’s Disease
And while there are, and have been, many theories over time, the ones that keep coming up again in scientific and clinical studies are that the major neurodegenerative diseases, which would be Alzheimer’s, Parkinson’s, things we now refer to as Tau, or Tau-driven or Tauopathies, are all linked to misfolded proteins that accumulate in the brain. And over time, we have come to learn that there are three predominant proteins that misfold in the brain, and that seem to be associated close to 100% with the major neurodegenerative diseases.
For Alzheimer’s, there are two proteins. The first is Abeta, and Abeta was discovered, largely, because patients who die of Alzheimer’s have large plaques in their brain which appear to be made up of Abeta Amyloid. In the case of Alzheimer’s, and I don’t know how well you can read this, but there are two proteins that appear to be involved: Abeta and Tau. And Abeta misfolds and appears in plaques. Tau, when it misfolds on a very large scale, ends up in something called “tangles”.
For Parkinson’s, we find that in almost all cases, there is a misfolded protein called Alpha Synuclein, and it ends up in the brain in visible intracellular particles called Lewy Bodies. And so what we have learned is, again, Synuclein for Parkinson’s, Abeta and Tau are very prevalent and clearly part of the disease process for Alzheimer’s.
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