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Cu/Zn superoxide dismutase can form pore-like structures.

Jinhyuk Chung·Hoichang Yang·Mitchel D de Beus·Chang Y Ryu·Kilwon Cho·Wilfredo Colón
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Abstract

Mutations in Cu/Zn superoxide dismutase (SOD) are associated with familial amyotrophic lateral sclerosis (FALS), a neurodegenerative disease that is characterized by the selective death of motor neurons. Despite the genetic association made between the protein and the disease, the mechanism by which the mutant SOD proteins become toxic is still a mystery. Using wild-type SOD and three pathogenic mutants (A4V, G37R, and G85R), we show that the copper-induced oxidation of metal-depleted SOD causes its in vitro aggregation into pore-like structures, as determined by atomic force microscopy. Because toxic pores have been recently implicated in the pathogenic mechanism of other neurodegenerative diseases, these results raise the possibility that the aberrant self-assembly of oxidatively damaged SOD mutants into toxic oligomers or pores may have a pathological role in FALS.

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CopperDimerizationEnzyme ActivationEnzyme StabilityMacromolecular SubstancesMicroscopy, Atomic ForceMutationOxidation-ReductionPorosityProtein ConformationRecombinant ProteinsStructure-Activity RelationshipSuperoxide DismutaseWaterComparative StudyJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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Jinhyuk Chung, Hoichang Yang, Mitchel D de Beus, Chang Y Ryu, Kilwon Cho, Wilfredo Colón. 2003-12-26. Cu/Zn superoxide dismutase can form pore-like structures.. https://doi.org/10.1016/j.bbrc.2003.11.008

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