Cloning and characterization of multiple human polyamine oxidase splice variants that code for isoenzymes with different biochemical characteristics.
The recently cloned and characterized human polyamine oxidase (PAOh1) potentially represents a new class of catabolic enzymes in the mammalian polyamine metabolic pathway capable of the efficient oxidation of polyamines. Here the discovery of three additional human PAO splice variants is reported, and the data support the fact that the human PAO gene codes for at least four isoenzymes, each of which exhibit distinctive biochemical characteristics, suggesting the existence of additional levels of complexity in polyamine catabolism.
Murray-Stewart
Tracy
T
Sidney Kimmel Comprehensive Cancer Center, Johns Hopkins University, Bunting Blaustein Building, Room 551, 1650 Orleans Street, Baltimore, MD 21231, USA.
Wang
Yanlin
Y
Devereux
Wendy
W
Casero
Robert A
RA
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D015723:Gene Library; D006801:Humans; D007700:Kinetics; D008957:Models, Genetic; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000096:biosynthesis* / Q000235:genetics*; D011073:Polyamines / Q000737:chemistry; D014176:Protein Biosynthesis; D020033:Protein Isoforms; D017386:Sequence Homology, Amino Acid; D013095:Spermidine / Q000737:chemistry; D013096:Spermine / Q000031:analogs & derivatives* / Q000737:chemistry; D013379:Substrate Specificity; D014158:Transcription, Genetic; D014407:Tumor Cells, Cultured; D000097667:Polyamine Oxidase
D018076:DNA, Complementary; D000587:Oxidoreductases Acting on CH-NH Group Donors; D011073:Polyamines; D020033:Protein Isoforms; D013095:Spermidine; D013096:Spermine; D000097667:Polyamine Oxidase; C029452:N'-acetylspermine