Postnatal maintenance of the 5-Ht1a-Pet1 autoregulatory loop by serotonin in the raphe nuclei of the brainstem

Mol Brain. 2014 Jun 28:7:48. doi: 10.1186/1756-6606-7-48.

Abstract

Background: Despite the importance of 5-HT1A as a major target for the action of several anxiolytics/antidepressant drugs, little is known about its regulation in central serotonin (5-hydroxytryptamine, 5-HT) neurons.

Results: We report that expression of 5-HT1A and the transcription factor Pet1 was impaired in the rostral raphe nuclei of mice lacking tryptophan hydroxylase 2 (Tph2) after birth. The downregulation of Pet1 was recapitulated in 5-Ht1a-/- mice. Using an explant culture system, we show that reduction of Pet1 and 5-HT1A was rescued in Tph2-/- brainstem by exogenous 5-HT. In contrast, 5-HT failed to rescue reduced expression of Pet1 in 5-Ht1a-/- brainstem explant culture.

Conclusions: These results suggest a causal relationship between 5-HT1A and Pet1, and reveal a potential mechanism by which 5-HT1A-Pet1 autoregulatory loop is maintained by 5-HT in a spatiotemporal-specific manner during postnatal development. Our results are relevant to understanding the pathophysiology of certain psychiatric and developmental disorders.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Animals, Newborn
  • Cell Movement / drug effects
  • Down-Regulation / drug effects
  • Feedback, Physiological / drug effects*
  • GATA3 Transcription Factor / metabolism
  • Mice
  • Mice, Knockout
  • Raphe Nuclei / drug effects
  • Raphe Nuclei / metabolism*
  • Receptor, Serotonin, 5-HT1A / deficiency
  • Receptor, Serotonin, 5-HT1A / metabolism*
  • Serotonergic Neurons / metabolism
  • Serotonin / pharmacology*
  • Transcription Factors / metabolism*
  • Tryptophan Hydroxylase / deficiency
  • Tryptophan Hydroxylase / metabolism

Substances

  • Fev protein, mouse
  • GATA3 Transcription Factor
  • Transcription Factors
  • Receptor, Serotonin, 5-HT1A
  • Serotonin
  • Tph2 protein, mouse
  • Tryptophan Hydroxylase