title: Disulfonic stilbenes prevent beta-amyloid (25-35) neuronal toxicity in rat cortical cultures.
abstract: Anion exchange proteins were recently identified among some of the proteins found clustered together in the hallmark plaques and tangles of Alzheimer's patient's brains. Anion exchange proteins underlie chloride/bicarbonate exchange, cell shape regulation and participate in removal of aged cells by the immune system. In this study we compared the neuroprotective efficacy of an anion exchanger inhibitor, 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS), against beta-amyloid((25-35)) neurotoxicity, staurosporine-induced apoptosis and glutamate-induced necrosis in primary cortical cultures. We demonstrate potent neuroprotective efficacy with DIDS against beta-amyloid((25-35)) and staurosporine, but not against glutamate. Our results suggest that anion exchange proteins may play an important role in beta-amyloid toxicity and that DIDS may represent a viable therapeutic agent for Alzheimer's disease.
authors.affiliation: Institute for Biological Sciences, National Research Council, Ottawa, Canada.
authors.forename: Zhenlei
authors.initials: Z
authors.lastname: Xia
authors.forename: Joseph
authors.initials: J
authors.lastname: Tauskela
authors.forename: Daniel L
authors.initials: DL
authors.lastname: Small
mesh_terms: D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid / Q000494:pharmacology*; D016229:Amyloid beta-Peptides / Q000633:toxicity*; D000818:Animals; D016923:Cell Death / Q000187:drug effects / Q000502:physiology; D002478:Cells, Cultured; D002540:Cerebral Cortex / Q000166:cytology / Q000187:drug effects* / Q000502:physiology; D009474:Neurons / Q000166:cytology / Q000187:drug effects* / Q000502:physiology; D010446:Peptide Fragments / Q000633:toxicity*; D051381:Rats
chemical_list: D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C074636:amyloid beta-protein (25-35); D017878:4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid