Premium
Secretory cleavage site of Alzheimer amyloid precursor protein is heterogeneous in Down's syndrome brain
Author(s) -
Kametania Fuyuki,
Tanaka Kikuko,
Tokuda Takahiko,
Ikeda Shu-ichi
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)00851-5
Subject(s) - proteolysis , amyloid precursor protein , chemistry , alzheimer's disease , polyacrylamide gel electrophoresis , biochemistry , p3 peptide , gel electrophoresis , blot , cleavage (geology) , amyloid (mycology) , microbiology and biotechnology , biology , enzyme , medicine , disease , gene , inorganic chemistry , paleontology , fracture (geology)
Aβ (β/A4) is the major constituent of brain amyloid in Alzheimer's disease (AD), Down's syndrome (DS) and normal aged persons. This protein is presumably derived by normal proteolysis from a precursor protein (APP). In this study, C‐terminal fragments of APP in a Tris/Triton soluble fraction were partially purified from DS brain by heparin‐affinity and reverse phase chromatography, and analyzed by N‐terminal amino acid sequencing after SDS polyacrylamide gel electrophoresis and Western blotting. We found at least six different C‐terminal fragments including those with the entire Aβ region. These results suggest that secretory processing of APP is heterogeneous and generates amyloidogenic C‐terminal fragments.