Glycinergic and GABAergic synaptic transmission are differentially affected by gephyrin in spinal neurons

Brain Res. 2005 Jul 19;1050(1-2):40-7. doi: 10.1016/j.brainres.2005.05.014.

Abstract

In the present study, we have examined the physiological properties of synaptic currents mediated by GlyRs and GABAARs after culturing spinal neurons with a gephyrin antisense oligonucleotide. Application of gephyrin antisense, but not the sense, reduced the glycinergic mIPSC amplitude ( approximately 50%) and frequency ( approximately 85%), indicating the importance of gephyrin for GlyR anchoring at postsynaptic sites. On the other hand, the glycine-evoked current amplitude was unchanged indicating that functional GlyRs were still located in the extrasynaptic membrane. The analysis of the GABAergic transmission in the same neurons revealed approximately 70% reduction in the frequency of the GABAergic mIPSCs, without changes in the amplitude. Interestingly, the modulation of remaining GABAAR-mediated synaptic events by zinc and diazepam was significantly altered by the antisense. These results indicate that gephyrin is required for the membrane insertion/stabilization of the GABAAR gamma2 subunit as well as for its subsequent localization in the postsynaptic membrane.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / genetics
  • Carrier Proteins / physiology*
  • Cells, Cultured
  • Fetus / cytology
  • Glycine / physiology*
  • Membrane Proteins / genetics
  • Membrane Proteins / physiology*
  • Mice
  • Mice, Inbred C57BL
  • Oligonucleotides, Antisense / pharmacology
  • Patch-Clamp Techniques
  • Protein Subunits / physiology*
  • Receptors, GABA-A / physiology*
  • Receptors, Glycine / physiology
  • Spinal Cord / cytology
  • Spinal Cord / embryology
  • Spinal Cord / physiology*
  • Synaptic Transmission / physiology*
  • gamma-Aminobutyric Acid / physiology

Substances

  • Carrier Proteins
  • Gabrg2 protein, mouse
  • Membrane Proteins
  • Oligonucleotides, Antisense
  • Protein Subunits
  • Receptors, GABA-A
  • Receptors, Glycine
  • gephyrin
  • gamma-Aminobutyric Acid
  • Glycine