Molecular and cellular pharmacological properties of 5-methoxycarbonylamino-N-acetyltryptamine (MCA-NAT): a nonspecific MT3 ligand

J Pineal Res. 2010 Apr;48(3):222-229. doi: 10.1111/j.1600-079X.2010.00746.x. Epub 2010 Feb 23.

Abstract

5-Methoxycarbonylamino-N-acetyltryptamine (MCA-NAT) has been initially described as a ligand at non MT(1), non MT(2) melatonin binding site (MT3) selective versus MT(1) and MT(2), two membrane melatonin receptors. MCA-NAT activity has been reported by others in different models, in vivo, particularly in the intra-ocular pressure (IOP) models in rabbits and monkeys. Its activity was systematically linked to either MT3 or to a new, yet unknown, melatonin receptor. In this article, the melatonin receptor pharmacology of MCA-NAT is described. MCA-NAT has micromolar range affinities at the melatonin receptors MT(1) and MT(2), while in functional studies, MCA-NAT proved to be a powerful MT(1)/MT(2) partial agonist in the sub-micromolar range. These data strongly suggest that MCA-NAT actions might be mediated by these receptors in vivo. Finally, as described by others, we show that MCA-NAT is unable to elicit any type of receptor-like functional responses from Chinese hamster ovary cells over-expressing quinone reductase 2, the MT3.

MeSH terms

  • Animals
  • Binding, Competitive
  • Cell Line
  • Circular Dichroism
  • Colforsin / antagonists & inhibitors
  • Colforsin / pharmacology
  • Cricetinae
  • Cyclic AMP / metabolism
  • Drug Interactions
  • Haplorhini
  • Humans
  • Inositol Phosphates / metabolism
  • Metallothionein 3
  • Mice
  • Rabbits
  • Rats
  • Receptors, Melatonin / metabolism*
  • Tryptamines / metabolism*
  • Tryptamines / pharmacology*

Substances

  • 5-methoxycarbonylamino-N-acetyltryptamine
  • Inositol Phosphates
  • Metallothionein 3
  • Mt3 protein, mouse
  • Receptors, Melatonin
  • Tryptamines
  • Colforsin
  • Cyclic AMP