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  • 1
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    Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease (1997)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1997-07-18
    Description: Most cases of early-onset familial Alzheimer's disease (FAD) are caused by mutations in the genes encoding the presenilin 1 (PS1) and PS2 proteins, both of which undergo regulated endoproteolytic processing. During apoptosis, PS1 and PS2 were shown to be cleaved at sites distal to their normal cleavage sites by a caspase-3 family protease. In cells expressing PS2 containing the asparagine-141 FAD mutant, the ratio of alternative to normal PS2 cleavage fragments was increased relative to wild-type PS2-expressing cells, suggesting a potential role for apoptosis-associated cleavage of presenilins in the pathogenesis of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, T W -- Pettingell, W H -- Jung, Y K -- Kovacs, D M -- Tanzi, R E -- New York, N.Y. -- Science. 1997 Jul 18;277(5324):373-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genetics and Aging Unit, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Charlestown, MA 02129, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9219695" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/metabolism/pathology ; Amino Acid Chloromethyl Ketones/pharmacology ; Amino Acid Substitution ; Animals ; *Apoptosis ; Caspase 3 ; *Caspases ; Cysteine Endopeptidases/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Enzyme Activation ; Etoposide/pharmacology ; Membrane Proteins/chemistry/genetics/*metabolism ; Mutation ; Oligopeptides/pharmacology ; Phosphorylation ; Presenilin-1 ; Presenilin-2 ; Rats ; Staurosporine/pharmacology ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 2
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    Candidate gene for the chromosome 1 familial Alzheimer's disease locus (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-08-18
    Description: A candidate gene for the chromosome 1 Alzheimer's disease (AD) locus was identified (STM2). The predicted amino acid sequence for STM2 is homologous to that of the recently cloned chromosome 14 AD gene (S182). A point mutation in STM2, resulting in the substitution of an isoleucine for an asparagine (N141l), was identified in affected people from Volga German AD kindreds. This N141l mutation occurs at an amino acid residue that is conserved in human S182 and in the mouse S182 homolog. The presence of missense mutations in AD subjects in two highly similar genes strongly supports the hypothesis that mutations in both are pathogenic.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levy-Lahad, E -- Wasco, W -- Poorkaj, P -- Romano, D M -- Oshima, J -- Pettingell, W H -- Yu, C E -- Jondro, P D -- Schmidt, S D -- Wang, K -- AG0513C/AG/NIA NIH HHS/ -- R01-AG11762/AG/NIA NIH HHS/ -- R01-AG11899/AG/NIA NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1995 Aug 18;269(5226):973-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Geriatric Research Education, and Clinical Center (182B), Veterans Affairs Medical Center, Seattle, WA 98108, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7638622" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Aged ; Alzheimer Disease/ethnology/*genetics ; Amino Acid Sequence ; Base Sequence ; Chromosome Mapping ; Chromosomes, Human, Pair 1/*genetics ; Cloning, Molecular ; DNA, Complementary/genetics ; Female ; Gene Expression ; Germany/ethnology ; Humans ; Lod Score ; Male ; Membrane Proteins/chemistry/*genetics ; Middle Aged ; Molecular Sequence Data ; Mutation ; Pedigree ; Point Mutation ; Presenilin-2
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 3
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    Rapid induction of Alzheimer A beta amyloid formation by zinc (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-09-02
    Description: A beta 1-40, a major component of Alzheimer's disease cerebral amyloid, is present in the cerebrospinal fluid and remains relatively soluble at high concentrations (less than or equal to 3.7 mM). Thus, physiological factors which induce A beta amyloid formation could provide clues to the pathogenesis of the disease. It has been shown that human A beta specifically and saturably binds zinc. Here, concentrations of zinc above 300 nM rapidly destabilized human A beta 1-40 solutions, inducing tinctorial amyloid formation. However, rat A beta 1-40 binds zinc less avidly and is immune to these effects, perhaps explaining the scarcity with which these animals form cerebral A beta amyloid. These data suggest a role for cerebral zinc metabolism in the neuropathogenesis of Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bush, A I -- Pettingell, W H -- Multhaup, G -- d Paradis, M -- Vonsattel, J P -- Gusella, J F -- Beyreuther, K -- Masters, C L -- Tanzi, R E -- R01 AG11899-01/AG/NIA NIH HHS/ -- R01 NS30428-03/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1994 Sep 2;265(5177):1464-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics and Aging, Massachusetts General Hospital, Boston.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8073293" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/etiology/*metabolism ; Amyloid beta-Peptides/chemistry/*metabolism ; Animals ; Brain/metabolism ; Edetic Acid/pharmacology ; Humans ; Kinetics ; Mice ; Peptide Fragments/chemistry/*metabolism ; Rats ; Solubility ; Zinc/*metabolism/pharmacology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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