VGluT1- and GAD-immunoreactive terminals in synaptic contact with PAG-immunopositive neurons in principal sensory trigeminal nucleus of rat

Acta Pharmacol Sin. 2007 Feb;28(2):180-4. doi: 10.1111/j.1745-7254.2007.00463.x.

Abstract

Aim: To trace the origin of abundant vesicular glutamate transporter 1-like immunoreactive (VGluT1-LI) axon terminals in the dorsal division of the principal sensory trigeminal nucleus (Vpd) and the relationships between VGluT1-LI, as well as the glutamic acid decarboxylase (GAD)-LI axon terminals, and phosphate- activated glutaminase (PAG)-LI thalamic projecting neurons in the Vpd.

Methods: Following unilateral trigeminal rhizotomy, triple-immunofluorescence histochemistry for VGluT1, GAD and PAG and the immunogold-silver method for VGluT1 or GAD, combined with the immunoperoxidase method for PAG were performed, respectively.

Results: After unilateral trigeminal rhizotomy, the density of VGluT1-like immunoreactivity (IR) in the Vpd on the lesion side was reduced compared to its contralateral counterpart. Under the confocal laser-scanning microscope, the VGluT1-LI or GAD-LI axon terminals were observed to be in close apposition to the PAG-LI thalamic projecting neuronal profiles, and further electron microscope immunocytochemistry confirmed that VGluT1- and GAD-LI axon terminals made asymmetrical and symmetrical synapses upon the PAG-LI neuronal structures.

Conclusion: The present results suggest that the VGluT1-LI axon terminals, which mainly arise from the primary afferents of the trigeminal ganglion, along with the PAG-LI neuronal profiles, form the key synaptic connection involved in sensory signaling.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Glutamate Decarboxylase / analysis*
  • Glutaminase / analysis*
  • Male
  • Presynaptic Terminals / chemistry*
  • Rats
  • Rats, Sprague-Dawley
  • Synapses / physiology*
  • Trigeminal Nuclei / chemistry
  • Trigeminal Nuclei / cytology*
  • Vesicular Glutamate Transport Protein 1 / analysis*
  • gamma-Aminobutyric Acid / physiology

Substances

  • Vesicular Glutamate Transport Protein 1
  • gamma-Aminobutyric Acid
  • Glutaminase
  • Glutamate Decarboxylase