Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Science 18 May 1990:
Vol. 248. no. 4957, pp. 854 - 857
DOI: 10.1126/science.2111579

Articles

Science, Vol 248, Issue 4957, 854-857
Copyright © 1990 by American Association for the Advancement of Science


articles

Relation of neuronal APP-751/APP-695 mRNA ratio and neuritic plaque density in Alzheimer's disease

SA Johnson, T McNeill, B Cordell, and CE Finch

Andrus Gerontology Center, University of Southern California, Los Angeles 90089.

An ongoing controversy concerns the cellular distribution of the differentially spliced forms of the amyloid protein precursor (APP) mRNAs and changes in prevalence of these transcripts during Alzheimer's disease. In situ hybridization on serial sections was used to prove that most hippocampal pyramidal neurons contain both APP-751 and APP-695 mRNA species. The APP-751/APP-695 mRNA ratio is generally increased during Alzheimer's disease, as shown by RNA gel blot analysis. Moreover, there was a strong linear relation between the increase in APP-751/APP-695 mRNA ratio in pyramidal neurons and the density of senile plaques within the hippocampus and entorhinal cortex. Thus, the increase in APP-751/APP-695 mRNA provides a molecular marker for regional variations in plaque density between individuals diagnosed with Alzheimer's disease by the commonly used composite criteria.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Copper Depletion Down-regulates Expression of the Alzheimer's Disease Amyloid-{beta} Precursor Protein Gene.
S. A. Bellingham, D. K. Lahiri, B. Maloney, S. La Fontaine, G. Multhaup, and J. Camakaris (2004)
J. Biol. Chem. 279, 20378-20386
   Abstract »    Full Text »    PDF »
Differential effect of zinc finger deletions on the binding of CTCF to the promoter of the amyloid precursor protein gene.
W. W. Quitschke, M. J. Taheny, L. J. Fochtmann, and A. A. Vostrov (2000)
Nucleic Acids Res. 28, 3370-3378
   Abstract »    Full Text »    PDF »
Alzheimer Amyloid Protein Precursor in the Rat Hippocampus: Transport and Processing through the Perforant Path.
J. D. Buxbaum, G. Thinakaran, V. Koliatsos, J. O'Callahan, H. H. Slunt, D. L. Price, and S. S. Sisodia (1998)
J. Neurosci. 18, 9629-9637
   Abstract »    Full Text »    PDF »
Thyroid Hormones Regulate {beta}-Amyloid Gene Splicing and Protein Secretion in Neuroblastoma Cells.
M. J. Latasa, B. Belandia, and A. Pascual (1998)
Endocrinology 139, 2692-2698
   Abstract »    Full Text »    PDF »
Relative Increase in Alzheimer's Disease of Soluble Forms of Cerebral Abeta Amyloid Protein Precursor Containing the Kunitz Protease Inhibitory Domain.
R. D. Moir, T. Lynch, A. I. Bush, S. Whyte, A. Henry, S. Portbury, G. Multhaup, D. H. Small, R. E. Tanzi, K. Beyreuther, et al. (1998)
J. Biol. Chem. 273, 5013-5019
   Abstract »    Full Text »    PDF »
The Zinc Finger Protein CTCF Binds to the APBbeta Domain of the Amyloid beta -Protein Precursor Promoter. EVIDENCE FOR A ROLE IN TRANSCRIPTIONAL ACTIVATION.
A. A. Vostrov and W. W. Quitschke (1997)
J. Biol. Chem. 272, 33353-33359
   Abstract »    Full Text »    PDF »
The Alternatively Spliced Kunitz Protease Inhibitor Domain Alters Amyloid beta Protein Precursor Processing and Amyloid beta Protein Production in Cultured Cells.
L. Ho, K.-i. Fukuchi, and StevenG. Younkin (1996)
J. Biol. Chem. 271, 30929-30934
   Abstract »    Full Text »    PDF »
In situ hybridization analysis of presenilin 1 mRNA in Alzheimer disease and in lesioned rat brain.
K. Page, R. Hollister, R. E. Tanzi, and B. T. Hyman (1996)
PNAS 93, 14020-14024
   Abstract »    Full Text »    PDF »
The Initiator Element and Proximal Upstream Sequences Affect Transcriptional Activity and Start Site Selection in the Amyloid beta -Protein Precursor Promoter.
W. W. Quitschke, J. P. Matthews, R. J. Kraus, and A. A. Vostrov (1996)
J. Biol. Chem. 271, 22231-22239
   Abstract »    Full Text »    PDF »
Interleukin-1beta and Glutamate Activate the NF-kappa B/Rel Binding Site from the Regulatory Region of the Amyloid Precursor Protein Gene in Primary Neuronal Cultures.
M. Grilli, F. Goffi, M. Memo, and P. Spano (1996)
J. Biol. Chem. 271, 15002-15007
   Abstract »    Full Text »    PDF »
Levels and Alternative Splicing of Amyloid beta Protein Precursor (APP) Transcripts in Brains of APP Transgenic Mice and Humans with Alzheimer's Disease.
E. M. Rockenstein, L. McConlogue, H. Tan, M. Power, E. Masliah, and L. Mucke (1995)
J. Biol. Chem. 270, 28257-28267
   Abstract »    Full Text »    PDF »
Identification and Characterization of a kappaB/Rel Binding Site in the Regulatory Region of the Amyloid Precursor Protein Gene.
M. Grilli, M. Ribola, A. Alberici, A. Valerio, M. Memo, and P. Spano (1995)
J. Biol. Chem. 270, 26774-26777
   Abstract »    Full Text »    PDF »
Nucleolin and Heterogeneous Nuclear Ribonucleoprotein C Proteins Specifically Interact with the 3`-Untranslated Region of Amyloid Protein Precursor mRNA.
S. H. E. Zaidi and J. S. Malter (1995)
J. Biol. Chem. 270, 17292-17298
   Abstract »    Full Text »    PDF »
beta-Amyloid Peptide Produced in Vitro Is Degraded by Proteinases Released by Cultured Cells.
A. Naidu, D. Quon, and B. Cordell (1995)
J. Biol. Chem. 270, 1369-1374
   Abstract »    Full Text »    PDF »
Brain Oxidative Energy and Related Metabolism, Neuronal Stress, and Alzheimer's Disease: A Speculative Synthesis.
S. Hoyer (1993)
J Geriatr Psychiatry Neurol 6, 3-13
   Abstract »    PDF »
Alzheimer's disease: the amyloid cascade hypothesis.
J. Hardy and G. Higgins (1992)
Science 256, 184-185
   PDF »
Solution structures of beta peptide and its constituent fragments: relation to amyloid deposition.
C. Barrow and M. Zagorski (1991)
Science 253, 179-182
   Abstract »    PDF »
Deciphering Alzheimer's disease: the amyloid precursor protein yields new clues.
D. Selkoe (1990)
Science 248, 1058-1060
   PDF »
gamma 1- and gamma 2-Syntrophins, Two Novel Dystrophin-binding Proteins Localized in Neuronal Cells.
G. Piluso, M. Mirabella, E. Ricci, A. Belsito, C. Abbondanza, S. Servidei, A. A. Puca, P. Tonali, G. A. Puca, and V. Nigro (2000)
J. Biol. Chem. 275, 15851-15860
   Abstract »    Full Text »    PDF »
A Region to the N-terminal Side of the CTCF Zinc Finger Domain Is Essential for Activating Transcription from the Amyloid Precursor Protein Promoter.
A. A. Vostrov, M. J. Taheny, and W. W. Quitschke (2002)
J. Biol. Chem. 277, 1619-1627
   Abstract »    Full Text »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)