You are not currently logged in.
Access JSTOR through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Amyloid Precursor Protein Processing and Aβ 42 Deposition in a Transgenic Mouse Model of Alzheimer Disease
K. Johnson-Wood, M. Lee, R. Motter, K. Hu, G. Gordon, R. Barbour, K. Khan, M. Gordon, H. Tan, D. Games, I. Lieberburg, D. Schenk, P. Seubert and L. McConlogue
Proceedings of the National Academy of Sciences of the United States of America
Vol. 94, No. 4 (Feb. 18, 1997), pp. 1550-1555
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/41369
Page Count: 6
You can always find the topics here!Topics: Software applications, Transgenic animals, Hippocampus, Antibodies, Amyloids, Pathology, Cerebellum, Alzheimers disease, Animals, Amyloidosis
Were these topics helpful?See something inaccurate? Let us know!
Select the topics that are inaccurate.
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
The PDAPP transgenic mouse, which over-expresses human amyloid precursor protein (APP717V→ F), has been shown to develop much of the pathology associated with Alzheimer disease. In this report, levels of APP and its amyloidogenic metabolites were measured in brain regions of transgenic mice between 4 and 18 months of age. While absolute levels of APP expression likely contribute to the rate of amyloid β -peptide (Aβ ) deposition, regionally specific factors also seem important, as homozygotic mice express APP levels in pathologically unaffected regions in excess of that measured in certain amyloid plaque-prone regions of heterozygotic mice. Regional levels of APp and APP-β were nearly constant at all ages, while Aβ levels dramatically and predictably increased in brain regions undergoing histochemically confirmed amyloidosis, most notably in the cortex and hippocampus. In hippocampus, Aβ concentrations increase 17-fold between the ages of 4 and 8 months, and by 18 months of age are over 500-fold that at 4 months, reaching an average level in excess of 20 nmol of Aβ per g of tissue. Aβ 1-42 constitutes the vast majority of the depositing Aβ species. The similarities observed between the PDAPP mouse and human Alzheimer disease with regard to Aβ 42 deposition occurring in a temporally and regionally specific fashion further validate the use of the model in understanding processes related to the disease.
Proceedings of the National Academy of Sciences of the United States of America © 1997 National Academy of Sciences