Ultraviolet light triggers the conversion of Cu2+-bound Aβ42 aggregates into cytotoxic species in a copper chelation-independent manner.

ABSTRACT: Increasing evidence indicates that abnormal Cu2+ binding to Aβ peptides are responsible for the formation of soluble Aβ oligomers and ROS that play essential roles in AD pathogenesis. During studying the Cu2+-chelating treatment of Cu2+-bound Aβ42 aggregates, we found that UV light exposure pronouncedly enhances cytotoxicity of the chelator-treated and -untreated Cu2+-bound Aβ42 aggregates. This stimulated us to thoroughly investigate (1) either the chelation treatment or UV light exposure leads to the increased cytotoxicity of the aggregates, and (2) why the chelator-treated and -untreated Cu2+-bound Aβ42 aggregates exhibit the increased cytotoxicity following UV light exposure if the latter is the case. The data indicated that the controlled UV exposure induced the dissociation of Cu2+-f

SUBMITTER: Dong X 

PROVIDER: S-EPMC4563556 | biostudies-literature | 2015 Sep

REPOSITORIES: biostudies-literature