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The biochemistry of Alzheimer's disease, the most common cause of dementia, is not yet very well understood. Alzheimer's disease (AD) has been identified as a proteopathy : a protein misfolding disease due to the accumulation of abnormally folded amyloid beta (Aβ) protein in the brain . [ 1 ]
Subtle changes in brain activity in the presence of both amyloid-beta and tau proteins may point to Alzheimer's disease, long before symptoms appear, a new study indicates.
An advance in 1984 and 1985 was the identification of Aβ as the protein that forms the cores of plaques. [20] This discovery led to the generation of new tools to study plaques, particularly antibodies to Aβ, and presented a molecular target for the development of potential therapies for Alzheimer's disease. [4] [21] [22] [23]
The other protein implicated in Alzheimer's disease, tau protein, also forms such prion-like misfolded oligomers, and there is some evidence that misfolded Aβ can induce tau to misfold. [6] [7] A study has suggested that APP and its amyloid potential is of ancient origins, dating as far back as early deuterostomes. [8]
A main theory behind the cause of Alzheimer’s disease is the build-up of the protein amyloid-beta in the brain. Researchers from the University of Cincinnati provide evidence suggesting it’s ...
A different perspective on Alzheimer's is revealed by a mouse study that has found that APP possesses ferroxidase activity similar to ceruloplasmin, facilitating iron export through interaction with ferroportin; it seems that this activity is blocked by zinc trapped by accumulated Aβ in Alzheimer's. [9]
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