http://purl.uniprot.org/citations/27325698 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/27325698 | http://www.w3.org/2000/01/rdf-schema#comment | "The dysfunction and loss of synapses in Alzheimer disease are central to dementia symptoms. We have recently demonstrated that pathological Amyloid β oligomer (Aβo) regulates the association between intracellular protein mediators and the synaptic receptor complex composed of cellular prion protein (PrP(C)) and metabotropic glutamate receptor 5 (mGluR5). Here we sought to determine whether Aβo alters the physiological signaling of the PrP(C)-mGluR5 complex upon glutamate activation. We provide evidence that acute exposure to Aβo as well as chronic expression of familial Alzheimer disease mutant transgenes in model mice prevents protein-protein interaction changes of the complex induced by the glutamate analog 3,5-dihydroxyphenylglycine. We further show that 3,5-dihydroxyphenylglycine triggers the phosphorylation and activation of protein-tyrosine kinase 2-β (PTK2B, also referred to as Pyk2) and of calcium/calmodulin-dependent protein kinase II in wild-type brain slices but not in Alzheimer disease transgenic brain slices or wild-type slices incubated with Aβo. This study further distinguishes two separate Aβo-dependent signaling cascades, one dependent on extracellular Ca(2+) and Fyn kinase activation and the other dependent on the release of Ca(2+) from intracellular stores. Thus, Aβo triggers multiple distinct PrP(C)-mGluR5-dependent events implicated in neurodegeneration and dementia. We propose that targeting the PrP(C)-mGluR5 complex will reverse aberrant Aβo-triggered states of the complex to allow physiological fluctuations of glutamate signaling."xsd:string |
http://purl.uniprot.org/citations/27325698 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m116.720664"xsd:string |
http://purl.uniprot.org/citations/27325698 | http://purl.uniprot.org/core/author | "Strittmatter S.M."xsd:string |
http://purl.uniprot.org/citations/27325698 | http://purl.uniprot.org/core/author | "Haas L.T."xsd:string |
http://purl.uniprot.org/citations/27325698 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
http://purl.uniprot.org/citations/27325698 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/27325698 | http://purl.uniprot.org/core/pages | "17112-17121"xsd:string |
http://purl.uniprot.org/citations/27325698 | http://purl.uniprot.org/core/title | "Oligomers of Amyloid beta Prevent Physiological Activation of the Cellular Prion Protein-Metabotropic Glutamate Receptor 5 Complex by Glutamate in Alzheimer Disease."xsd:string |
http://purl.uniprot.org/citations/27325698 | http://purl.uniprot.org/core/volume | "291"xsd:string |
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