title: Diamine oxidase in relation to diamine and polyamine metabolism.
abstract: Diamine oxidase catalyzes the oxidative deamination of short chain aliphatic diamines, like putrescine, and histamine. The enzyme is rate-limiting in the terminal catabolism of polyamines, which are endogenous polycations important for cell growth and differentiation. This review examines the behavior of diamine oxidase in mammalian tissues in relation to diamine and polyamine metabolism under physiological and pathological conditions. The role of diamine oxidase in the control of putrescine levels in growing tissues and the known mechanisms responsible for the enzyme expression are also described.
authors.affiliation: Consiglio Nazionale delle Ricerche, Università di Milano, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Sessa
authors.forename: A
authors.initials: A
authors.lastname: Perin
mesh_terms: D006631:Amine Oxidase (Copper-Containing) / Q000187:drug effects / Q000378:metabolism*; D000818:Animals; D003959:Diamines / Q000378:metabolism*; D000431:Ethanol / Q000494:pharmacology; D006801:Humans; D015394:Molecular Structure; D011073:Polyamines / Q000378:metabolism*; D011700:Putrescine / Q000378:metabolism; D014018:Tissue Distribution
chemical_list: D003959:Diamines; D011073:Polyamines; D000431:Ethanol; D006631:Amine Oxidase (Copper-Containing); D011700:Putrescine