5-HT2A receptors are expressed by catecholaminergic neurons in the rat nucleus tractus solitarii

Neuroreport. 2002 Dec 3;13(17):2365-9. doi: 10.1097/00001756-200212030-00039.

Abstract

Within the nucleus tractus solitarii (NTS), serotonin (5-HT) exerts modulatory effects on central mechanisms controlling autonomic functions, notably through the stimulation of 5-HT2 receptors. Using double immunocytochemical labeling with specific anti-5-HT2A receptor antibodies and antibodies directed against the catecholamine (CA) synthesizing enzymes, i.e. tyrosine hydroxylase, dopamine beta-hydroxylase (DBH) and phenylethanolamine N-methyltransferase, we investigated whether 5-HT effects could be mediated by 5-HT2A receptors located on CA perikarya and/or processes within the NTS. A relatively high density of 5-HT2A immunoreactive processes was observed throughout the NTS. 5-HT2A neuronal perikarya were also found within the NTS except in its rostrolateral part. Double immunolabeling experiments revealed many 5-HT2A receptors on CA processes but only few 5-HT2A/TH and 5-HT2A/DBH perikarya. These data support the idea that, within the NTS, 5-HT2A-mediated control of autonomic functions involves CA neurons.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Axons / metabolism
  • Axons / ultrastructure
  • Catecholamines / metabolism*
  • Dendrites / metabolism
  • Dendrites / ultrastructure
  • Dopamine beta-Hydroxylase / metabolism
  • Fluorescent Antibody Technique
  • Male
  • Neurons / cytology
  • Neurons / metabolism*
  • Phenylethanolamine N-Methyltransferase / metabolism
  • Rats
  • Rats, Sprague-Dawley
  • Receptor, Serotonin, 5-HT2A
  • Receptors, Serotonin / metabolism*
  • Serotonin / metabolism
  • Solitary Nucleus / cytology
  • Solitary Nucleus / metabolism*
  • Synaptic Transmission / physiology
  • Tyrosine 3-Monooxygenase / metabolism

Substances

  • Catecholamines
  • Receptor, Serotonin, 5-HT2A
  • Receptors, Serotonin
  • Serotonin
  • Tyrosine 3-Monooxygenase
  • Dopamine beta-Hydroxylase
  • Phenylethanolamine N-Methyltransferase