%0 Journal Article %1 wang2001cloning %A Wang, Yanlin %A Devereux, Wendy %A Woster, Patrick M. %A Murray-Stewart, Tracy %A Hacker, Amy %A Casero, Robert A., Jr %D 2001 %J Cancer Research %K 7 background cancer %N 14 %P 5370-5373 %T Cloning and Characterization of a Human Polyamine Oxidase That Is Inducible by Polyamine Analogue Exposure %U http://cancerres.aacrjournals.org/content/61/14/5370.long %V 61 %X 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 M(r) 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 microM of N1,N"-bis(ethyl)norspermine results in approximately 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.

@article{wang2001cloning, abstract = {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 M(r) 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 microM of N1,N"-bis(ethyl)norspermine results in approximately 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.}, added-at = {2017-10-19T19:48:27.000+0200}, author = {Wang, Yanlin and Devereux, Wendy and Woster, Patrick M. and Murray-Stewart, Tracy and Hacker, Amy and {Casero, Robert A.}, Jr}, biburl = {https://www.bibsonomy.org/bibtex/23a514b778aea7fed97dfbbc994716ef3/artheibault}, description = {This article describes the first cloning of a polyamine oxidase. Later research would expand upon the study of polyamine oxidases and their role in cancer.}, interhash = {9e1bc3b69114462c8033cb44a274e1d4}, intrahash = {3a514b778aea7fed97dfbbc994716ef3}, issn = {1538-7445}, journal = {Cancer Research}, keywords = {7 background cancer}, month = jul, number = 14, pages = {5370-5373}, timestamp = {2017-10-25T21:39:39.000+0200}, title = {Cloning and Characterization of a Human Polyamine Oxidase That Is Inducible by Polyamine Analogue Exposure}, url = {http://cancerres.aacrjournals.org/content/61/14/5370.long}, volume = 61, year = 2001 }