ZFIN ID: ZDB-PUB-010404-4
Isolation and characterization of an alpha 2-type zebrafish glycine receptor subunit
Imboden, M., De Saint Jan, D., Leulier, F., Korn, H., Goblet, C., and Bregestovski, P.
Date: 2001
Source: Neuroscience   103(3): 799-810 (Journal)
Registered Authors: Bregestovski, Piotz, Goblet, Christiane, Imboden, Medea, Korn, Henri
Keywords: phylogenetic relationships; ionic currents; oocyte expression; developmental expression
MeSH Terms:
  • Aging/metabolism
  • Amino Acid Sequence/genetics
  • Animals
  • Base Sequence/genetics
  • Blotting, Northern
  • Brain/growth & development
  • Brain/physiology
  • Embryo, Nonmammalian/metabolism
  • Molecular Sequence Data
  • Oocytes/metabolism
  • Receptors, Glycine/genetics
  • Receptors, Glycine/isolation & purification*
  • Receptors, Glycine/physiology
  • Reverse Transcriptase Polymerase Chain Reaction
  • Xenopus
  • Zebrafish/embryology
  • Zebrafish/genetics*
  • Zebrafish/metabolism*
PubMed: 11274795 Full text @ Neuroscience
The complementary DNA for a novel alpha subunit of the glycine receptor, alphaZ2, was isolated from a zebrafish adult brain library. The molecular characteristics, phylogenetic relationships and messenger RNA length of this alphaZ2 subunit show it to be an alpha2-type glycine receptor subunit isoform. The leader peptide however, diverges from those of known glycine receptor alpha isoforms. Recombinantly expressed in Xenopus oocytes, alphaZ2 formed functional glycine receptor channels. These homomeric channels were activated by glycine and taurine, with apparent affinities similar to those reported for zebrafish alphaZ1 glycine receptor, and were also effectively antagonized by nanomolar concentrations of strychnine. However, during prolonged applications of agonists, ionic currents of alphaZ2 receptor channels declined to a much lower steady-state level than those of alphaZ1, indicating different desensitization properties. Analysis of messenger RNA revealed that alphaZ2 is specifically expressed in adult brain tissue and present in both adult and embryonic zebrafish.This report contributes to the characterization of the diversity of glycine receptor isoforms in vertebrates.