Biogenic amines and polyamines: similar biochemistry for different physiological missions and biomedical applications

Crit Rev Biochem Mol Biol. 2003;38(1):23-59. doi: 10.1080/713609209.


Biogenic amines are organic polycations derived from aromatic or cationic amino acids. All of them have one or more positive charges and a hydrophobic skeleton. Nature has evolved these molecules to play different physiological roles in mammals, but maintains similar patterns for their metabolic and intracellular handling. As deduced from this review, many questions still remain to be solved around their biochemistry and molecular biology, blocking our aims to control the relevant pathologies in which they are involved (cancer and immunological, neurological, and gastrointestinal diseases). Advances in this knowledge are dispersed among groups working on different biomedical areas. In these pages, we put together the most relevant information to remark how fruitful it can be to learn from Nature and to take advantage of the biochemical similarities (key protein structures and their regulation data on metabolic interplays and binding properties) to generate new hypothesis and develop different biomedical strategies based on biochemistry and molecular biology of these compounds.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amine Oxidase (Copper-Containing) / metabolism
  • Animals
  • Aromatic-L-Amino-Acid Decarboxylases / genetics
  • Aromatic-L-Amino-Acid Decarboxylases / metabolism
  • Biogenic Amines / chemistry
  • Biogenic Amines / metabolism*
  • Histamine / metabolism
  • Humans
  • Membrane Transport Proteins / metabolism
  • Metabolic Diseases / metabolism
  • Molecular Structure
  • Nucleic Acids / metabolism
  • Polyamines / chemistry
  • Polyamines / metabolism*
  • Transferases / metabolism


  • Biogenic Amines
  • Membrane Transport Proteins
  • Nucleic Acids
  • Polyamines
  • Histamine
  • Amine Oxidase (Copper-Containing)
  • Transferases
  • Aromatic-L-Amino-Acid Decarboxylases