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Alzheimer's β‐amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
Author(s) -
Kurochkin Igor V.,
Goto Sataro
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00387-4
Subject(s) - insulin degrading enzyme , proteases , peptide , biochemistry , enzyme , cytosol , monoclonal antibody , chemistry , amyloid (mycology) , insulin , p3 peptide , amyloid precursor protein , alzheimer's disease , antibody , biology , disease , endocrinology , medicine , immunology , inorganic chemistry
Cerebral deposition of β‐amyloid peptide (βA) is a hallmark of Alzheimer's disease. Concentration of βA could play a critical role in the rate of amyloid deposition. It is therefore of considerable importance to identify proteases involved in processing of βA. 125 I‐labeled synthetic βA specifically cross‐linked to a single protein with M r = 110,000 in cytosol fractions from rat brain and liver. This protein was identified as insulin degrading enzyme (IDE) since the labeling of the 110 kDa protein was completely blocked by an excess of insulin, and anti‐IDE monoclonal antibodies precipitated the labeled protein. Purified rat IDE effectively degraded βA.