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Carboxy‐terminal truncation of long‐tailed amyloid β‐peptide is inhibited by serine protease inhibitor and peptide aldehyde
Author(s) -
Hamazaki Hideaki
Publication year - 1998
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/s0014-5793(98)00157-4
Subject(s) - phenylmethylsulfonyl fluoride , carboxypeptidase , serine protease , peptide , serine , antipain , biochemistry , exopeptidase , glutamate carboxypeptidase ii , carboxypeptidase a , chemistry , subtilisin , protease , enzyme , biology , leupeptin , genetics , prostate , cancer
The 42/43‐residue amyloid β‐peptide (Aβ) is widely believed to play a major role in Alzheimer's disease. The present study shows that the rat brain contains a carboxypeptidase that efficiently deletes three amino acids from Aβ1–43. The carboxypeptidase activity in the brain was completely inhibited by 1 mM phenylmethylsulfonyl fluoride, suggesting the protease is a serine carboxypeptidase. The carboxy‐terminal truncation of Aβ1–43 was moderately inhibited by carbobenzoxy‐Leu‐leucinal, carbobenzoxy‐Leu‐Leu‐leucinal, and carbobenzoxy‐Leu‐Leu‐norvalinal, and weakly by antipain. The present data suggest that the serine carboxypeptidase contributes to the generation of short‐tailed Aβ peptides and is important in the intracellular clearance of Aβ1–42/43 in brains.