Carnosine and related dipeptides protect human ceruloplasmin against peroxyl radical-mediated modification.
Ceruloplasmin (CP) is the major plasma antioxidant and copper transport protein. In a previous study, we showed that the aggregation of human ceruloplasmin was induced by peroxyl radicals. We investigated the effects of antioxidant dipeptides carnosine, homocarnosine and anserine on peroxyl radical-mediated ceruloplasmin modification. Carnosine, homocarnosine and anserine significantly inhibited the aggregation of CP induced by peroxyl radicals. When CP was incubated with peroxyl radicals in the presence of three compounds, ferroxidase activity, as measured by the activity staining method, was protected. All three compounds also inhibited the formation of dityrosine in peroxyl radicals-treated CP. The results suggest that carnosine and related compounds act as peroxyl radical scavenger to protect the protein modification. It is proposed that carnosine and related peptides might be explored as potential therapeutic agents for pathologies that involve CP modification mediated by peroxyl radicals generated in the lipid peroxidation.[1]References
- Carnosine and related dipeptides protect human ceruloplasmin against peroxyl radical-mediated modification. Kang, J.H., Kim, K.S., Choi, S.Y., Kwon, H.Y., Won, M.H., Kang, T.C. Mol. Cells (2002) [Pubmed]
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