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  • 1
    Electronic Resource
    Electronic Resource
    Metabotropic Glutamate Receptor Subtype mGluR1α Stimulates the Secretion of the Amyloid β-Protein Precursor Ectodomain (1997)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 69 (1997), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: To examine the effects of glutamatergic neurotransmission on amyloid processing, we stably expressed the metabotropic glutamate receptor subtype 1α (mGluR1α) in HEK 293 cells. Both glutamate and the selective metabotropic agonist 1-amino-1,3-cyclopentanedicarboxylic acid (ACPD) rapidly increased phosphatidylinositol (PI) turnover four- to fivefold compared with control cells that were transfected with the expression vector alone. Increased PI turnover was effectively blocked by the metabotropic antagonist α-methyl-4-carbophenylglycine (MCPG), indicating that heterologous expression of mGluR1α resulted in efficient coupling of the receptors to G protein and phospholipase C activation. Stimulation of mGluR1α with glutamate, quisqualate, or ACPD rapidly increased secretion of the APP ectodomain (APPs); these effects were blocked by MCPG. The metabotropic receptors were coupled to APP processing by protein kinases and by phospholipase A2 (PLA2), and melittin, a peptide that stimulates PLA2, potently increased APPs secretion. These data indicate that mGluR1α can be involved in the regulation of APP processing. Together with previous findings that muscarinic and serotonergic receptor subtypes can increase the secretion of the APP ectodomain, these observations support the concept that proteolytic processing of APP is under the control of several major neurotransmitters.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1997.69020704.x
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  • 2
    Electronic Resource
    Electronic Resource
    Preface (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 695 (1993), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Notes: This volume contains the papers and poster abstracts compiled for the seventh meeting of the International Study Group on the Pharmacology of Memory Disorders Associated with Aging (ISG), that took place in Zürich, Switzerland, on February 12–14, 1993. The ISG was founded 14 years ago in the belief that the development of effective treatments for Alzheimer's disease (AD) and other dementias would be accelerated by periodic meetings of scientists and physicians from around the world who are actively working on issues related to dementia. There have been six previous “Zurich Meetings”—in 1979, 1981, 1984, 1987, 1989, and 1991. The proceedings of the second ISB meeting were published by Raven Press in 1982 (Alzheimer's Disease: A Report of Progress in Research; Corkin, Davis, Growdon, Usdin, and Wurtman, editors); the proceedings of the fourth ISG meeting were published by Springer-Verlag in 1988 as Supplement 24 of the Journal of Neural Transmission (Topics in the Basic and Clinical Science of Dementia; Wurtman, Corkin, and Growdon, editors); the proceedings of the fifth ISB meeting were published by Raven Press in 1990 (Alzheimer's Disease, Advances in Neurology, Volume 51; Wurtman, Corkin, Growdon, and fitter-Walker, editors); and the proceedings of the sixth ISG meeting were published by the New York Academy of Sciences in 1992 (Aging and Alzheimer's Disease, Volume 640; Growdon, Corkin, fitter-Walker, and Wurtman, editors).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1993.tb23017.x
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  • 3
    Electronic Resource
    Electronic Resource
    Receptor-coupled Amyloid Precursor Protein Processing (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 695 (1993), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Notes: The family of β-amyloid protein precursors (APP) can be processed via several alternative proteolytic pathways. Some generate potentially amyloidogenic AFP derivatives, whereas others preclude the formation of such fragments. The cellular mechanisms regulating the relative activities of these pathways are thus important in determining the factors contributing to the formation of amyloidogenic APP derivatives. In order to investigate whether cell-surface receptor activity can regulate APP processing, HEK 293 cell lines stably expressing human muscarinic acetylcholine receptors (mAChR; subtypes m1, m2, m3, m4) were stimulated with the muscarinic agonist carbachol, and the release of APP derivatives was measured. Carbachol increased the release of large amino-terminal APP-fragments 4-to 6-fold in cell lines expressing the m1 or m3 receptors but not in those expressing m2 or m4 subtypes. This increase was blocked by various protein kinase inhibitors and mimicked by phorbol esters, indicating that it is mediated by protein kinase activation, presumably by protein kinase C (PKC). To determine whether additional cell-surface receptor types linked to this signal transduction pathway could also regulate APP processing, we stimulated differentiated PC-12 cells with bradykinin and found that this neuropeptide also increased the secretion of amino-terminal APP derivatives. We next investigated the possibility that neuronal depolarization might affect APP processing in mammalian brain. Electrically stimulated rat hippocampal slices released two times more amino-terminal APP derivatives than unstimulated control slices. This release increased with increasing stimulation frequencies in the physiological firing range of hippocampal pyramidal cells, and was blocked by tetrodotoxin. These results suggest that, in brain, APP processing is regulated by neuronal activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1993.tb23039.x
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  • 4
    Electronic Resource
    Electronic Resource
    Epidemiological, Clinical, and Neuropathological Study of Apolipoprotein E Genotype in Alzheimer's Disease (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 802 (1996), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1996.tb32592.x
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  • 5
    Electronic Resource
    Electronic Resource
    No Association between α1-Antichymotrypsin and Familial Alzheimer's Diseases (1996)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 802 (1996), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1996.tb32596.x
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  • 6
    Electronic Resource
    Electronic Resource
    Can the immune system fight Alzheimer disease? (2006)
    [s.l.] : Nature Publishing Group
    Nature medicine 12 (2006), S. 755-756 
    Details
    ISSN: 1546-170X
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Alzheimer disease is a progressive dementia that primarily impairs memory, language and reasoning. Current treatments provide modest symptomatic benefit to some individuals with Alzheimer disease but do little to slow disease progression. Brains of individuals with Alzheimer disease shrink over ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/nm0706-755
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  • 7
    Electronic Resource
    Electronic Resource
    CHANGES IN MOTOR BEHAVIOR FOLLOWING THE ADMINISTRATION OF SEROTONIN NEUROTOXINS (1978)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 305 (1978), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1978.tb31545.x
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  • 8
    Electronic Resource
    Electronic Resource
    Vasopressin and Bradykinin Regulate Secretory Processing of the Amyloid Protein Precursor of Alzheimer's Disease (1998)
    Springer
    Neurochemical research 23 (1998), S. 807-814 
    Details
    ISSN: 1573-6903
    Keywords: Amyloid ; Alzheimer's Disease ; vasopressin ; bradykinin ; neuropeptides ; receptors ; α-secretase processing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The amyloid protein precursor (APP) can be processed via several alternative processing pathways, α-secretase processing by cleavage within the amyloid β-peptide domain of APP is highly regulated by several external and internal signals including G protein-coupled receptors, protein kinase C and phospholipase A2. In order to demonstrate that G protein-coupled neuropeptide receptors for bradykinin and vasopressin can increase α-secretase processing of APP, we stimulated endogenously expressed bradykinin or vasopressin receptors in cell culture with the neuropeptides and measured the secreted ectodomain (APPs) in the conditioned media. Both bradykinin and vasopressin rapidly increased phosphatidylinositol (PI) turnover in PC-12 and in NRK-49F cells, indicating that these cell lines constitutively expressed functional PI-linked receptors for these neuropeptides. Both bradykinin and vasopressin readily stimulated APPs secretion. Increased APPs secretion was concentration-dependent and saturable, and it was blocked by receptor antagonists indicating specific receptor interaction of the peptides. The bradykinin-induced increase in APPs secretion in PC-12 cells was mediated by protein kinase C (PKC), whereas vasopressin receptors in NRK-49F cells were coupled to APP processing by PKC-independent signalling pathways. Our data show that neuropeptides can modulate APP processing in cell culture. In as much as increased α-secretase processing is associated with decreased formation of Aβ1–40, a major constituent of amyloid plaques, our findings suggest a possible role for modulating neuropeptide receptors as a strategy for altering amyloid metabolism in Alzheimer's disease brain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1022423813362
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