2010 Volume 27 Pages 43-46
Prooxidant effects of polyamines were analyzed by using permeabilized yeast cells and purified yeast glutathione reductase.
1. Polyamine stimulated NADH-dependent inactivation of aconitase in the presence of cyanide, implying that the superoxide-generating enzyme with NADH was activated by polyamines. Polyamines further stimulated NADPH-dependent inactivation of aconitase in the presence of menadione and cyanide, suggesting the activation of NADPH/naphthoquinone-dependent production of superoxide. The order of effectiveness of polyamines as activators was spermine > spermidine. Putrescine showed little effect.
2. Glutathione reductase, the principal enzyme scavenging reactive oxygen species, was inhibited by polyamines. Polyamine-dependent production of reactive oxygen and the inhibition of the activity scavenging reactive oxygen may explain the cytotoxic effects of these compounds.