Nuclear localization of human spermine oxidase isoforms - possible implications in drug response and disease etiology.

ABSTRACT: The recent discovery of the direct oxidation of spermine via spermine oxidase (SMO) as a mechanism through which specific antitumor polyamine analogues exert their cytotoxic effects has fueled interest in the study of the polyamine catabolic pathway. A major byproduct of spermine oxidation is H2O2, a source of toxic reactive oxygen species. Recent targeted small interfering RNA studies have confirmed that SMO-produced reactive oxygen species are directly responsible for oxidative stress capable of inducing apoptosis and potentially mutagenic DNA damage. In the present study, we describe a second catalytically active splice variant protein of the human spermine oxidase gene, designated SMO5, which exhibits substrate specificities and affinities comparable to those of the originally identifi

SUBMITTER: Murray-Stewart T 

PROVIDER: S-EPMC3631774 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature