The complementary DNA for a novel or subunit of the glycine receptor, alpha
Z2, was isolated from a zebrafish adult brain library. The molecular chara
cteristics, phylogenetic relationships and messenger RNA length of this alp
ha Z2 subunit show it to be an alpha2-type glycine receptor subunit isoform
. The leader peptide however, diverges from those of known glycine receptor
oc isoforms. Recombinantly expressed in Xenopus oocytes, alpha Z2 formed f
unctional glycine receptor channels. These homomeric channels were activate
d by glycine and taurine, with apparent affinities similar to those reporte
d for zebrafish alpha Z1 glycine receptor, and were also effectively antago
nized by nanomolar concentrations of strychnine. However, during prolonged
applications of agonists, ionic currents of alpha Z2 receptor channels decl
ined to a much lower steady-state level than those of alpha Z1, indicating
different desensitization properties. Analysis of messenger RNA revealed th
at alpha Z2 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. (C) 2001 IBRO. Published by Elsevier Sci
ence Ltd. All rights reserved.