AUTHOR=Keskitalo Salla , Farkas Melinda , Hanenberg Michael , Szodorai Anita , Kulic Luka , Semmler Alexander , Weller Michael , Nitsch Roger M. , Linnebank Michael TITLE=Reciprocal modulation of Aβ42 aggregation by copper and homocysteine JOURNAL=Frontiers in Aging Neuroscience VOLUME=6 YEAR=2014 URL=https://www.frontiersin.org/journals/aging-neuroscience/articles/10.3389/fnagi.2014.00237 DOI=10.3389/fnagi.2014.00237 ISSN=1663-4365 ABSTRACT=
Hyperhomocysteinemia is a risk factor for Alzheimer’s disease (AD). Both homocysteine (Hcy) and amyloid β (Aβ), which accumulates in the brain of AD patients, bind copper. Aim of this study was to test the hypothesis that the association of Hcy and AD results from a molecular interaction between Hcy and Aβ that is mediated by copper. We established a microtiter plate format thioflavin T aggregation assay to monitor Aβ42 fibrillization. Copper (5 μM) completely prevented Aβ42 (5 μM) fibrillization. Homocysteine in the absence of copper did not impact Aβ42 fibrillization, but physiological concentrations of Hcy (10–100 μM) attenuated the inhibitory effect of copper on Aβ42 fibril formation. These results were qualitatively confirmed by electron microscopy, which did not reveal morphological differences. To compare the toxicity of fibrillar and non-fibrillar Aβ42 exposed to copper or Hcy, rat primary cortical neurons were treated