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Title: Amyloidogenic processing of human amyloid precursor protein in hippocampal neurons devoid of cathepsin D
Authors: Saftig, P ×
Peters, C
von Figura, K
Craessaerts, Kathleen
Van Leuven, Freddy
De Strooper, Bart #
Issue Date: Dec-1996
Series Title: Journal of Biological Chemistry vol:271 issue:44 pages:27241-4
Abstract: betaA4-Amyloid peptide, the main component of the amyloid plaques in the brain of Alzheimer's disease patients is produced from amyloid precursor protein (APP) by proteolytical processing. Several lines of evidence suggest a direct role for cathepsin D, the major endosomal/lysosomal aspartic endopeptidase, in betaA4-amyloid peptide generation. Here we tested this hypothesis using primary cultures of hippocampal neurons derived from cathepsin D-deficient (knock out) mice and expressing wild-type human APP and two clinical APP variants via recombinant Semliki Forest virus. We demonstrate APP secretory processing, production of carboxyl-terminal amyloid fragments, and secretion of the betaA4-amyloid peptide in the complete absence of cathepsin D. The results rule out cathepsin D as a critical component of alpha-, beta-, or gamma-secretase and therefore as a primary target for drugs aimed at decreasing the betaA4-amyloid peptide burden in Alzheimer's disease.
URI: 
ISSN: 0021-9258
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Associated Laboratories - miscellaneous (-)
Molecular Genetics Section (-)
Department of Human Genetics - miscellaneous
× corresponding author
# (joint) last author

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