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lüll Beta-amyloid catabolism: roles for neprilysin (NEP) and other metallopeptidases?Carson JA; Turner AJJ Neurochem 2002[Apr]; 81 (1): 1-8The steady-state level of amyloid beta-peptide (Abeta) represents a balance between its biosynthesis from the amyloid precursor protein (APP) through the action of the beta- and gamma-secretases and its catabolism by a variety of proteolytic enzymes. Recent attention has focused on members of the neprilysin (NEP) family of zinc metalloproteinases in amyloid metabolism. NEP itself degrades both Abeta(1-40) and Abeta(1-42) in vitro and in vivo, and this metabolism is prevented by NEP inhibitors. Other NEP family members, for example endothelin-converting enzyme, may contribute to amyloid catabolism and may also play a role in neuroprotection. Another metalloproteinase, insulysin (insulin-degrading enzyme) has also been advocated as an amyloid-degrading enzyme and may contribute more generally to metabolism of amyloid-forming peptides. Other candidate enzymes proposed include angiotensin-converting enzyme, some matrix metalloproteinases, plasmin and, indirectly, thimet oligopeptidase (endopeptidase-24.15). This review critically evaluates the evidence relating to proteinases implicated in amyloid catabolism. Therapeutic strategies aimed at promoting A,beta degradation may provide a novel approach to the therapy of Alzheimer's disease.|Amino Acid Sequence[MESH]|Amyloid beta-Peptides/*metabolism[MESH]|Amyloid beta-Protein Precursor/metabolism[MESH]|Animals[MESH]|Aspartic Acid Endopeptidases/metabolism[MESH]|Endothelin-Converting Enzymes[MESH]|Humans[MESH]|Insulysin/metabolism[MESH]|Metalloendopeptidases/*metabolism[MESH]|Models, Molecular[MESH]|Molecular Sequence Data[MESH]|Neprilysin/metabolism[MESH]|Nervous System/metabolism[MESH]|Peptide Fragments/metabolism[MESH] |