Chaperone Works to Lessen Alzheimer’s Symptoms and Toxic Protein Buildup, Mouse Study Says

Chaperone Works to Lessen Alzheimer’s Symptoms and Toxic Protein Buildup, Mouse Study Says
A molecular chaperone called TPT-172 was able to prevent proteins linked to Alzheimer’s — including amyloid-beta and tau — from building up in the brain, improve memory and ease brain inflammation when tested in a mouse model of the disease. The study, “A pharmacological chaperone improves memory by reducing Aβ and tau neuropathology in a mouse model with plaques and tangles,” was published in Molecular Neurodegeneration. Several studies have identified genes linked to cellular structures known as endosomes as susceptibility risk factors for Alzheimer's onset. Endosomes are small membrane-bound compartments that act like vehicles, moving proteins and molecules from one part of a cell to another. These structures are important for the transport of amyloid precursor protein (APP) when it gets broken down into amyloid-beta, the molecule responsible for the buildup of toxic plaques in the brains of Alzheimer’s patients. If endosomes don’t work as intended, amyloid-beta levels rise, forming plaques that damage and kill neurons. One protein that enables the correct functioning of the endosome is the vacuolar protein sorting 35 (VPS35). VPS35 is part of a group of proteins called the retromer complex system, which is responsible for moving proteins out of endosomes. Compared to healthy individuals, Alzheimer’s patients are known to have lower levels of VPS35 in the brain, and in vitro (lab) studies have shown that these lower levels can increase the formation of amyloid-beta aggregates. Researchers at Temple University in Philadelphia used a pharmacological chaperone, a small molecule that can enter cells and act as ‘scaffolding’ to support the structure of a particular protein, to stabilize VPS35. This chaperone, called TPT-172, p
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