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Transgenic Animal Models for Alzheimer's Disease a
Author(s) -
FUKUCHI KENICHIRO,
OGBURN CHARLES E.,
SMITH ANNETTE C.,
KUNKEL DENNIS D.,
FURLONG CLEMENT E.,
DEEB SAMIR S.,
NOCHLIN DAVID,
SUMI S. MARK,
MARTIN GEORGE M.
Publication year - 1993
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.1749-6632.1993.tb23055.x
Subject(s) - neurotoxicity , amyloid precursor protein , in vivo , neuropathology , genetically modified mouse , transgene , in vitro , biochemistry of alzheimer's disease , alzheimer's disease , bace1 as , chemistry , p3 peptide , biology , microbiology and biotechnology , disease , gene , biochemistry , pathology , toxicity , medicine , genetics , organic chemistry
The neuropathology of Alzheimer's disease is characterized by the deposition of abnormal protein aggregates. The main constituent of the deposition is β‐amyloid protein. A seminal role of this protein is supported by the discovery of point mutations in the gene of its precursor protein in certain forms of familial Alzheimer's disease. In vitro (cultured neuronal cells), overexpression of the precursor protein or a part of the precursor leads to degeneration of neurons, suggesting neurotoxicity of its derivatives. At this tune, all of the reported transgenic mice bearing DNA construct for the precursor or a part of the precursor, however, have not developed convincing pathological changes similar to what is observed in patients with Alzheimer's disease. This interesting discrepancy between in vitro and in vivo suggests suppressors in vivo which ameliorate β‐amyloid precursor protein derivative‐mediated neurotoxicity.