Monoamine oxidase B (MAOB)-containing structures in MAOA-deficient transgenic mice

Brain Res. 1997 Oct 10;771(1):121-32. doi: 10.1016/s0006-8993(97)00832-9.

Abstract

Monoamine oxidase (MAO)-containing structures were studied for the first time in type A MAO (MAOA)-deficient transgenic mice (Tg8) derived from C3H strain, using MAO enzyme histochemistry. In this mutant line, MAOA activity was not detected in neurons of the locus coeruleus. In contrast, in their dorsal raphe neurons, we noted an intense activity of type B MAO (MAOB). Based on pharmacological MAOA suppression experiments employing a specific inhibitor (clorgyline), we confirmed that the localization of MAOB-positive structures are not different between Tg8 mutant and normal C3H line. Many of MAOB-positive structures which have not been described previously in the rat, cat and primates were described in this study. In the forebrain, MAOB-containing neurons were discriminated in the striatum, septal nuclei, major island of Calleja, diagonal band, medial forebrain bundle, ventral pallidum and amygdaloid nucleus. Stained neurons in the thalamus and hypothalamus were much more extensively distributed in the mouse than the rat. Pontine laterodorsal tegmental neurons showed MAOB activity. The present data suggest that serotonin, a preferential substrate for MAOA, can be oxidized by MAOB in MAOA-deficient Tg8 mice.

Publication types

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

MeSH terms

  • Animals
  • Brain / enzymology*
  • Cats
  • Cerebral Cortex / enzymology
  • Clorgyline / pharmacology
  • Female
  • Isoenzymes / deficiency*
  • Isoenzymes / genetics
  • Isoenzymes / metabolism*
  • Locus Coeruleus / enzymology
  • Male
  • Mice
  • Mice, Inbred C3H
  • Mice, Transgenic
  • Monoamine Oxidase / deficiency*
  • Monoamine Oxidase / genetics
  • Monoamine Oxidase / metabolism*
  • Nerve Fibers / enzymology
  • Neurons / enzymology*
  • Organ Specificity
  • Primates
  • Raphe Nuclei / enzymology
  • Rats
  • Tegmentum Mesencephali / enzymology

Substances

  • Isoenzymes
  • Monoamine Oxidase
  • Clorgyline