화학공학소재연구정보센터
Biochemical and Biophysical Research Communications, Vol.327, No.1, 300-305, 2005
Characterization of newly cloned variant of rat glycine receptor alpha 1 subunit
Responses to glycine, a major inhibitory neurotransmitter within the nervous system, are mediated by glycine receptors (GlyRs). Here, we report the cloning and analysis of a novel splicing variant of the GlyRalpha1 subunit. This variant, named GlyRalpha1(del), has a truncated cytoplasmic region between transmembrane domains (TM)3 and TM4, and compared to other variants, the truncation is contributed by a different acceptor site in exon 9. We transfected GlyRalpha1 or GlyRalpha1(del) into HEK293 cells, and then examined the glycine-activated currents using a whole-cell patch-clamp recording technique. Maximal currents and current-voltage relationships showed no clear difference between GlyRalpha1(del) and GlyRalpha1. Moreover, dose-response curves indicated that the EC50 values for glycine differed significantly between the two GlyRalpha1 derivatives, although their Hill coefficients were similar. When present with other isoforms, GlyRalpha1(del) might alter the response to glycine or to other agonists, as this variant expands the potential heterogeneity among glycine receptors. (C) 2004 Elsevier Inc. All rights reserved.