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Proteolytic Cleavage of the Alzheimer's Disease Amyloid A4 Precursor Protein
Author(s) -
Ishiura Shoichi
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb08160.x
Subject(s) - amyloid precursor protein , cleavage (geology) , biochemistry of alzheimer's disease , alzheimer's disease , p3 peptide , chemistry , amyloid (mycology) , extracellular , protein precursor , senile plaques , proteolysis , biochemistry , bace1 as , amyloid precursor protein secretase , limiting , microbiology and biotechnology , disease , biology , pathology , medicine , enzyme , inorganic chemistry , paleontology , mechanical engineering , fracture (geology) , engineering
Amyloid A4 protein (ß‐protein) is deposited in the brain of a patient with Alzheimer's disease (AD) as one of the main components of extracellular cerebrovascular amyloid, as well as neurofibrillary tangles. It is derived from a precursor protein, and its formation has been considered to be a rate‐limiting step for brain degeneration in AD. In this article, proteolytic cleavage events that can degrade amyloid precursor protein are reviewed with respect to how the topographical distribution of the proteinase and its substrates disturbs normal processing steps in AD brain.