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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 ]
Alpha secretases are a family of proteolytic enzymes that cleave amyloid precursor protein (APP) in its transmembrane region.Specifically, alpha secretases cleave within the fragment that gives rise to the Alzheimer's disease-associated peptide amyloid beta when APP is instead processed by beta secretase and gamma secretase.
From the age of 60 years (10%) to the age of 80 years (60%), the proportion of people with senile plaques increases linearly. Women are slightly more likely to have plaques than are men. [45] [44] Both plaques and Alzheimer's disease also are more common in aging persons with trisomy-21 (Down syndrome).
To date, 37 human proteins have been found to form amyloid in pathology and be associated with well-defined diseases. [2] The International Society of Amyloidosis classifies amyloid fibrils and their associated diseases based upon associated proteins (for example ATTR is the group of diseases and associated fibrils formed by TTR). [3]
Brain Aβ is elevated in people with sporadic Alzheimer's disease. Aβ is the main constituent of brain parenchymal and vascular amyloid; it contributes to cerebrovascular lesions and is neurotoxic. [33] [34] [35] It is unresolved how Aβ accumulates in the central nervous system and subsequently initiates the disease of cells. Significant ...
Neurons typically remain in G0, a nondividing, nonreplicating phase of the cell cycle. Neurons subject to loss of synaptic connections, chronic exposure to oxidative stress or stress hormones like glucocorticoids will exit G0 and reenter into a cell cycle that is abortive and leads to cell death through apoptosis.
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