{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["You H"],"funding":["NICHD NIH HHS","NIEHS NIH HHS"],"pagination":["1737-42"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3277185"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["109(5)"],"pubmed_abstract":["N-methyl-d-aspartate receptors (NMDARs) mediate critical CNS functions, whereas excessive activity contributes to neuronal damage. At physiological glycine concentrations, NMDAR currents recorded from cultured rodent hippocampal neurons exhibited strong desensitization in the continued presence of NMDA, thus protecting neurons from calcium overload. Reducing copper availability by specific chelators (bathocuproine disulfonate, cuprizone) induced nondesensitizing NMDAR currents even at physiologically low glycine concentrations. This effect was mimicked by, and was not additive with, genetic ablation of cellular prion protein (PrP(C)), a key copper-binding protein in the CNS. Acute ablation of PrP(C) by enzymatically cleaving its cell-surface GPI anchor yielded similar effects. Biochemical "],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Aβ neurotoxicity depends on interactions between copper ions, prion protein, and N-methyl-D-aspartate receptors."],"pmcid":["PMC3277185"],"funding_grant_id":["P01HD29587","P01 ES016738","P01 HD029587"],"pubmed_authors":["Zamponi GW","Stys PK","Kannanayakal TJ","Chen L","Xia P","Lipton SA","Engbers JD","Hameed S","You H","Tsutsui S"],"additional_accession":[]},"is_claimable":false,"name":"Aβ neurotoxicity depends on interactions between copper ions, prion protein, and N-methyl-D-aspartate receptors.","description":"N-methyl-d-aspartate receptors (NMDARs) mediate critical CNS functions, whereas excessive activity contributes to neuronal damage. At physiological glycine concentrations, NMDAR currents recorded from cultured rodent hippocampal neurons exhibited strong desensitization in the continued presence of NMDA, thus protecting neurons from calcium overload. Reducing copper availability by specific chelators (bathocuproine disulfonate, cuprizone) induced nondesensitizing NMDAR currents even at physiologically low glycine concentrations. This effect was mimicked by, and was not additive with, genetic ablation of cellular prion protein (PrP(C)), a key copper-binding protein in the CNS. Acute ablation of PrP(C) by enzymatically cleaving its cell-surface GPI anchor yielded similar effects. Biochemical ","dates":{"release":"2012-01-01T00:00:00Z","publication":"2012 Jan","modification":"2025-04-22T07:05:13.913Z","creation":"2019-03-27T00:49:01Z"},"accession":"S-EPMC3277185","cross_references":{"pubmed":["22307640"],"doi":["10.1073/pnas.1110789109"]}}