Background: Malondialdehyde (MDA) released during oxidative stress modifies proteins covalently. Results: The C terminus of complement regulator factor H binds negative patches on MDA-modified proteins, and aHUSrelated mutations affect the interaction. Conclusion: Defects in factor H binding to MDA-modified surfaces might allow deleterious complement activation on them. Significance: MDA-modifications are potentially a new factor in aHUS pathogenesis.
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