The main constituents of extracellular amyloid plaque, amyloid β40, 42, is produced by
the cleavage of amyloid precursor protein (APP).»
Aβ results from the normal
cleavage of amyloid precursor protein (APP), but its accumulation and aggregation into plaques represents the quintessential feature of AD.27 Aβ is found in orders of magnitude greater in AD brains than in healthy brains.28 This fact is noteworthy because lower concentrations of Aβ tend to stay soluble; higher concentrations form plaques more readily.29
Amyloid beta (Aβ) is a small peptide molecule generated from
cleavage of amyloid precursor protein (APP).
Specifically, that aggregates of A-beta peptides, which are formed following
cleavage of the Amyloid Precursor Protein (APP), instigate a series of events that leads to neurodegeneration and, eventually, AD.
Exploiting this compartmentalization, the team developed an endosomally - targeted β - secretase inhibitor that specifically blocked
cleavage of amyloid precursor protein but not non-amyloid proteins.
Not exact matches
Other work addresses mechanisms for decreasing
amyloid beta biosynthesis by enhancing
cleavage of its
precursor protein by the alpha - secretase enzyme.
Proteolytic
cleavage of amyloid - β -
protein precursor (AβPP) by β - and γ - secretases results in production
of the
amyloid - β peptide (Aβ) that accumulates in the brains
of sufferers
of Alzheimer's disease (AD).
The
amyloid - β
protein precursor (AβPP) is cleaved by a transmembrane protease termed β - site AβPP
cleavage enzyme (BACE1), which is being explored as a target for therapy and prevention
of Alzheimer's disease (AD).