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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]
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 ...
Subtle changes in brain activity in the presence of both amyloid-beta and tau proteins may point to Alzheimer's disease, ... not clear as to how these two proteins might cause Alzheimer’s disease.
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]
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]
Human growth hormone derived from cadavers was linked to Alzheimer's disease in five patients ... amyloid-beta protein. ... of plaques and tangles in the brain that cause Alzheimer’s disease.
Neurofibrillary tangles (NFTs) are intracellular aggregates of hyperphosphorylated tau protein that are most commonly known as a primary biomarker of Alzheimer's disease. Their presence is also found in numerous other diseases known as tauopathies. Little is known about their exact relationship to the different pathologies.
Now, research has found that a protein that regulates cell repair could be a promising new target for treating several of these conditions, including the most common, Alzheimer’s disease.
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