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Subunit composition of strychnine‐sensitive glycine receptors expressed by adult rat basolateral amygdala neurons
Author(s) -
McCool Brian A.,
Farroni Jeffery S.
Publication year - 2001
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1046/j.0953-816x.2001.01730.x
Subject(s) - strychnine , forebrain , glycine receptor , receptor , neuroscience , basolateral amygdala , glycine , biology , amygdala , endocrinology , microbiology and biotechnology , medicine , central nervous system , biochemistry , amino acid
In neonatal rats, strychnine‐sensitive glycine receptors are widely expressed in the spinal cord, brainstem and forebrain. During development, these ‘neonatal’ receptors are replaced by an adult isoform, the expression of which becomes restricted primarily to brain stem and spinal cord. Unlike most forebrain regions, functional strychnine‐sensitive glycine receptors appear to persist within adult rat amygdala. However, the subunit composition of glycine receptors expressed by amygdala neurons and its relationship to the adult isoform in brain stem/spinal cord has not been defined precisely. In this report, we have utilized RT‐PCR and single‐cell RT‐PCR to demonstrate that the ‘neonatal’α 2 ‐subunit mRNA persists in adult rat amygdala neurons and is the predominant α‐subunit. We further demonstrate that native amygdala glycine receptors are relatively insensitive to the receptor antagonist picrotoxin, suggesting that α 2 ‐ and β‐subunits may be present together in the same multisubunit complex. We further demonstrate that α 2 ‐ and β‐subunits cloned from adult rat amygdala can form functional channels when expressed in a heterologous system. Together, these studies highlight both the unique characteristics of strychnine‐sensitive glycine receptors in the adult rat amygdala as well as the possibility that α 2 /β channels may represent the adult forebrain isoform of the strychnine‐sensitive glycine receptor.