Journal
BIOCHEMICAL SOCIETY TRANSACTIONS
Volume 33, Issue -, Pages 335-338Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BST0330335
Keywords
Alzheimer's disease; amyloid precursor protein; Creutzfeldt-Jakob disease; GPI anchor; lipid raft; pnon protein
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In the amyloidogenic pathway, the APP (amyloid precursor protein) is proteolytically processed by the beta- and y-secretases to release the A beta (amyloid-beta) peptide that is neurotoxic and aggregates in the brains of patients suffering from Alzheimer's disease. in the non-amyloidogenic pathway, APP is cleaved by a-secretase within the A beta domain, precluding deposition of intact A beta peptide. The cellular form of the PrPc (prion protein) undergoes reactive oxygen Species-mediated beta-cleavage within the copper-binding octapeptide repeats or, alternatively, a-cleavage within the central hydrophobic neurotoxic domain. In addition, PrPc is shed from the membrane by the action of a zinc metalloprotease. Members of the ADAM (a disintegrin and metalloproteinase) family of zinc metalloproteases, notably ADAM10 and TACE (ADAM17) display a-secretase activity towards APP and appear to be responsible for the a-cleavage of PrPc. The amyloidogenic cleavage of APP by the beta- and y-secretases appears to occur preferentially in cholesterol-rich lipid rafts, while the conversion of PrPc into the infectious form PrPSc also appears to occur in these membrane domains.
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