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An Endosomal‐Lysosomal Pathway for Degradation of Amyloid Precursor Protein a
Author(s) -
COLE GREG M.,
BELL LLORAINE,
TRUONG QUANG B.,
SAITOH TSUNAO
Publication year - 1992
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1992.tb27480.x
Subject(s) - endosome , immunoprecipitation , lysosome , amyloid precursor protein , microbiology and biotechnology , chemistry , protein degradation , biochemistry , enzyme , biology , alzheimer's disease , cell , medicine , disease , gene
We previously reported evidence for a lysosomal degradative pathway for APP and C-terminal fragments thereof, based on Western and immunocytochemical analysis of drug-treated cells. Here, we verify the existence of a lysosomal degradative pathway for APP using pulse chase immunoprecipitation analysis of drug-treated cells and fibroblasts with and without a known lysosomal hydrolase targeting defect. The results are consistent with the hypothesis that part or all of the beta-protein domain of APP is normally degraded by lysosomes. A mechanism for beta-protein deposition based on this data is hypothesized.