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Two‐way cleavage of β‐amyloid protein precursor by multicatalytic proteinase
Author(s) -
Kojima Shin-ichi,
Omori Motoko
Publication year - 1992
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(92)80588-8
Subject(s) - amyloid precursor protein , extracellular , enzyme , p3 peptide , cleavage (geology) , biochemistry , amyloid precursor protein secretase , alpha secretase , chemistry , proteinase k , amyloid (mycology) , protein precursor , amyloid β , microbiology and biotechnology , biology , alzheimer's disease , medicine , disease , inorganic chemistry , paleontology , fracture (geology)
The β‐amyloid protein (β‐AP) derived from a β‐amyloid protein precursor (APP) is a hallmark of Alzheimer's disease. The abundant generation of β‐AP suggests the abnormal processing of APP, but the molecular mechanism remains unclear. The main APP‐processing enzyme was purified from the rat brain and identified to be a macropain‐like multicatalytic proteinase. The purified enzyme cleaved the Gln 15 ‐Lys 16 bond of β‐AP, but altered to cleave at the N‐terminus of β‐AP to release the extracellular domain of β‐AP in the presence of Ca 2+ . These findings suggest that the functional change in this multicatalytic proteinase may result in abnormal processing of APP.