Diamine oxidase in relation to diamine and polyamine metabolism

Agents Actions. 1994 Nov;43(1-2):69-77. doi: 10.1007/BF02005768.

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.

Publication types

  • Review

MeSH terms

  • Amine Oxidase (Copper-Containing) / drug effects
  • Amine Oxidase (Copper-Containing) / metabolism*
  • Animals
  • Diamines / metabolism*
  • Ethanol / pharmacology
  • Humans
  • Molecular Structure
  • Polyamines / metabolism*
  • Putrescine / metabolism
  • Tissue Distribution

Substances

  • Diamines
  • Polyamines
  • Ethanol
  • Amine Oxidase (Copper-Containing)
  • Putrescine