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: Zhenlei Xia, Joseph Tauskela, Daniel L Small
• Journal: Neuroscience letters (Neurosci Lett) Vol. 340 Issue 1 Pg. 53-6 (Apr 03 2003) ISSN: 0304-3940 [Print] Ireland
• PMID: 12648757 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amyloid beta-Peptides
• Peptide Fragments
• amyloid beta-protein (25-35)
• 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid

Topics

• 4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid (pharmacology)
• Amyloid beta-Peptides (toxicity)
• Animals
• Cell Death (drug effects, physiology)
• Cells, Cultured
• Cerebral Cortex (cytology, drug effects, physiology)
• Neurons (cytology, drug effects, physiology)
• Peptide Fragments (toxicity)
• Rats