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Amyloid β/A4 Precursor Protein (APP) Processing in Lysosomes a
Author(s) -
TAGAWA KAZUHIKO,
MARUYAMA KEI,
ISHIURA SHOICHI
Publication year - 1992
Publication title -
annals of the new york academy of sciences
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.1992.tb27482.x
Subject(s) - amyloid precursor protein , chemistry , amyloid (mycology) , microbiology and biotechnology , alzheimer's disease , biology , medicine , disease , pathology , inorganic chemistry
Alzheimer's disease (AD) is characterized by the formation of senile plaques, the main component of which is amyloid beta protein. The processing of the amyloid beta/A4 protein has been implicated in the pathogenesis of AD. We have reported cathepsin B as a candidate APP secretase. By using APP-transfected COS-1 cells, we determined that the putative APP secretase, lysosomal cathepsin B, is involved in the constitutive processing of the precursor molecule. Digestion experiments demonstrated that cathepsin B cleaves the APP molecule into two fragments with molecular masses 115 kDa and 9 kDa, representing presumptive proteolytic fragments of constitutive processing.