Cloning and characterization of a human polyamine oxidase that is inducible by polyamine analogue exposure

Yanlin Wang, Wendy Devereux, Patrick M. Woster, Tracy Murray Stewart, Amy Hacker, Robert A. Casero

Research output: Contribution to journalArticlepeer-review


Mammalian polyamine catabolism is under the control of two enzymes, spermidine/spermine N1-acetyltransferase and the flavin adenine dinucleotide-dependent polyamine oxidase (PAO). In this study, the cloning and initial characterization of human PAO is reported. A 1894-bp cDNA with an open reading frame of 1668-bp codes for a protein of 555 amino acids. In vitro transcription/translation of this cDNA clone produces the expected Mr 61, 900 protein with PAO activity. The PAO activity of this clone is inhibited by MDL 72, 527, a specific inhibitor of mammalian PAO. However, neither pargyline, a specific monoamine oxidase inhibitor, nor semicarbazide, a specific diamine oxidase inhibitor, inhibits the PAO activity of this clone. PAO has been referred to as being constitutively expressed. However, 24-h exposure of a non-small cell lung carcinoma cell line, NCI H157, to 10 μM of N1, N″-bis(ethyl)norspermine results in ∼5-fold induction of PAO mRNA and a > 3-fold induction of PAO activity. These results demonstrate that in at least one cell type, PAO is up-regulated in response to polyamine analogue exposure. The PAO clone described here should provide a useful tool, which will facilitate the dissection of the role of polyamine catabolism in normal growth and in response to the antitumor polyamine analogues.

Original languageEnglish (US)
Pages (from-to)5370-5373
Number of pages4
JournalCancer Research
Issue number14
StatePublished - Jul 15 2001

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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