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Alzheimer's first substantive description of plaques appeared in 1911. [11] In contrast, Oskar Fischer published a series of comprehensive investigations of plaques and dementia in 1907, 1910 and 1912. [11] By 1911, Max Bielschowsky proposed the amyloid-nature of plaque deposits.
The reasons why amyloid cause diseases are unclear. In some cases, the deposits physically disrupt tissue architecture, suggesting disruption of function by some bulk process. An emerging consensus implicates prefibrillar intermediates, rather than mature amyloid fibers, in causing cell death, particularly in neurodegenerative diseases.
Amyloid beta (Aβ, Abeta or beta-amyloid) denotes peptides of 36–43 amino acids that are the main component of the amyloid plaques found in the brains of people with Alzheimer's disease. [2] The peptides derive from the amyloid-beta precursor protein (APP), which is cleaved by beta secretase and gamma secretase to yield Aβ in a cholesterol ...
The researchers also discovered that plaques only form when a specific level of amyloid beta from neurons is present, at which point oligodendrocytes contribute to plaque build-up.
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 ...
Amyloid light chains deposition in shoulder joint causes enlarged shoulders, also known as "shoulder pad sign". [18] Amyloid light chain depositions can also cause bilateral symmetric polyarthritis. [18] The deposition of amyloid proteins in the bone marrow without causing plasma cell dyscrasias is called amyloidoma. It is commonly found in ...
Eventually, the fragments form oligomers, then fibrils, beta-sheets, and finally plaques. The presence of β-amyloid plaques in the brain causes the body to recruit and activate microglial cells and astrocytes. [34] Following cleavage by β-secretase, APP is cleaved by a membrane-bound protein complex called γ-secretase to generate Aβ. [35]
Amyloid plaque Aβ protein species ends in residue 40 or 42, [4] but it is suspected that Aβ42 form is crucial in the pathogenesis of AD. Although Aβ42 makes up less than 10% of total Aβ, it aggregates at much faster rates than Aβ40. [5] Aβ42 is the initial and major component of amyloid plaque deposits.
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