G Protein-Mediated Neuronal DNA Fragmentation Induced by Familial Alzheimer's Disease-Associated Mutants of APP

Missense mutations in the 695-amino acid form of the amyloid precursor protein (APP$_{695}$) cosegregate with disease phenotype in families with dominantly inherited Alzheimer's disease. These mutations convert valine at position 642 to isoleucine, phenylalanine, or glycine. Expression of these...

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Published in:Science (American Association for the Advancement of Science) 1996-05, Vol.272 (5266), p.1349-1352
Main Authors: Yamatsuji, Tomoki, Matsui, Takashi, Okamoto, Takashi, Komatsuzaki, Katsumi, Takeda, Shizu, Fukumoto, Hiroaki, Iwatsubo, Takeshi, Suzuki, Nobuhiro, Asami-Odaka, Asano, Ireland, Scott, Kinane, T. Bernard, Giambarella, Ugo, Nishimoto, Ikuo
Format: Article
Language:English
Subjects:
Alzheimer Disease - genetics
Alzheimer Disease - metabolism
Alzheimer's disease
Amino acids
Amyloid beta-Peptides - metabolism
Amyloid beta-Protein Precursor - chemistry
Amyloid beta-Protein Precursor - genetics
Amyloid beta-Protein Precursor - physiology
Amyloidosis
Animals
Antibodies
Apoptosis
Base Sequence
Biological and medical sciences
Cell lines
Cellular immunity
Complementary DNA
Culture Media, Conditioned
Cultured cells
Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases
Dementia
Deoxyribonucleic acid
DNA
DNA - metabolism
DNA fragmentation
Genetic aspects
Genetic mutation
GTP-Binding Proteins - physiology
Humans
Hybrid Cells
Medical sciences
Mice
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Neurology
Neurons
Neurons - cytology
Neurons - metabolism
Nucleosomes - metabolism
Observation
Peptide Fragments - metabolism
Proteins
Rats
Transfection
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cited_by cdi_FETCH-LOGICAL-c817t-a401aa1975c65ea2a370e42814b522940086679a5e122a0d758d126892699b333
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container_issue 5266
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container_title Science (American Association for the Advancement of Science)
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creator Yamatsuji, Tomoki
Matsui, Takashi
Okamoto, Takashi
Komatsuzaki, Katsumi
Takeda, Shizu
Fukumoto, Hiroaki
Iwatsubo, Takeshi
Suzuki, Nobuhiro
Asami-Odaka, Asano
Ireland, Scott
Kinane, T. Bernard
Giambarella, Ugo
Nishimoto, Ikuo
description Missense mutations in the 695-amino acid form of the amyloid precursor protein (APP$_{695}$) cosegregate with disease phenotype in families with dominantly inherited Alzheimer's disease. These mutations convert valine at position 642 to isoleucine, phenylalanine, or glycine. Expression of these mutant proteins, but not of normal APP$_{695}$, was shown to induce nucleosomal DNA fragmentation in neuronal cells. Induction of DNA fragmentation required the cytoplasmic domain of the mutants and appeared to be mediated by heterotrimeric guanosine triphosphate-binding proteins (G proteins).
doi_str_mv 10.1126/science.272.5266.1349
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Bernard</au><au>Giambarella, Ugo</au><au>Nishimoto, Ikuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>G Protein-Mediated Neuronal DNA Fragmentation Induced by Familial Alzheimer's Disease-Associated Mutants of APP</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1996-05-31</date><risdate>1996</risdate><volume>272</volume><issue>5266</issue><spage>1349</spage><epage>1352</epage><pages>1349-1352</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><coden>SCIEAS</coden><abstract>Missense mutations in the 695-amino acid form of the amyloid precursor protein (APP$_{695}$) cosegregate with disease phenotype in families with dominantly inherited Alzheimer's disease. These mutations convert valine at position 642 to isoleucine, phenylalanine, or glycine. Expression of these mutant proteins, but not of normal APP$_{695}$, was shown to induce nucleosomal DNA fragmentation in neuronal cells. Induction of DNA fragmentation required the cytoplasmic domain of the mutants and appeared to be mediated by heterotrimeric guanosine triphosphate-binding proteins (G proteins).</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>8650548</pmid><doi>10.1126/science.272.5266.1349</doi><tpages>4</tpages></addata></record>
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identifier ISSN: 0036-8075
ispartof Science (American Association for the Advancement of Science), 1996-05, Vol.272 (5266), p.1349-1352
issn 0036-8075
1095-9203
language eng
recordid cdi_proquest_miscellaneous_35190121
source American Association for the Advancement of Science; Social Science Premium Collection; Education Collection
subjects Alzheimer Disease - genetics
Alzheimer Disease - metabolism
Alzheimer's disease
Amino acids
Amyloid beta-Peptides - metabolism
Amyloid beta-Protein Precursor - chemistry
Amyloid beta-Protein Precursor - genetics
Amyloid beta-Protein Precursor - physiology
Amyloidosis
Animals
Antibodies
Apoptosis
Base Sequence
Biological and medical sciences
Cell lines
Cellular immunity
Complementary DNA
Culture Media, Conditioned
Cultured cells
Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases
Dementia
Deoxyribonucleic acid
DNA
DNA - metabolism
DNA fragmentation
Genetic aspects
Genetic mutation
GTP-Binding Proteins - physiology
Humans
Hybrid Cells
Medical sciences
Mice
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Neurology
Neurons
Neurons - cytology
Neurons - metabolism
Nucleosomes - metabolism
Observation
Peptide Fragments - metabolism
Proteins
Rats
Transfection
title G Protein-Mediated Neuronal DNA Fragmentation Induced by Familial Alzheimer's Disease-Associated Mutants of APP
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