Copper complexes with superoxide dismutase activity enhance oxygen-mediated toxicity in human erythroleukemia cells

C. Steinkuhler, I. Mavelli, G. Melino, L. Rossi, U. Weser, G. Rotilio

Research output: Contribution to journalArticlepeer-review

Abstract

Many human tumor cells have low activity of H2O2-detoxifying glutathione peroxidase (GSH-Px) and catalase, though some cell lines still maintain normal levels of superoxide dismutase (SOD), which scavenges O2- by dismutating it to H2O2 and O2. Such an alteration of the balance of the antioxygenic enzymes should result in a higher H2O2 steady-state concentration, thus increasing the cell sensitivity to oxidative insults. This hypothesis is supported by the finding that lipophilic low molecular weight copper complexes with SOD activity display antitumor action in vivo, probably by further increasing H2O2 content of the cells and producing oxidative killing of the tumor. In this context we investigated the effects of two low molecular weight active-center analogues of copper- and zinc-containing SOD, N,N'-bis(2-pyridylmethylene)-1,4- butanediamine (N,N',N'',N''')-Cu(II)-diperchlorate (PUPY), and 1,8-di(2-imidazoyl)-2,7-diazoctadiene-1,7-(N,N',N'',N''')-Cu(II)-dipe chlorate (CuIm) on the human erythroleukemia cell line K562.

Original languageEnglish
Pages (from-to)133-136
Number of pages4
JournalAnnals of the New York Academy of Sciences
Volume551
Publication statusPublished - 1988

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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