Permeation and gating of alpha1 glycine-gated channels expressed at low and high density in Xenopus oocyte.
When a high density of alpha1-subunit glycine receptor (GlyR) is expressed in Xenopus oocytes, two populations of channels can be distinguished according to their apparent affinity for glycine which differs 5- to 6-fold. To compare the open pore diameter of these channels, the relative permeability of formate with respect to chloride (P(formate)/P(Cl)) was determined in bionic conditions. For the low-affinity GlyR P(formate)/P(Cl) was comparable to that reported for glycine-gated channels in cultured spinal cord and hippocampal neurons. In contrast, the high-affinity GlyR had a 56% larger P(formate)/P(Cl). In addition, the open probability of the channels was differentially sensitive to voltage. These results show that the high expression of alpha1 GlyR resulted in two populations of GlyR which differed not only in the affinity to agonists but also in permeation and gating mechanisms.
Maammar
M
M
Laboratoire de Neurobiologie Cellulaire, UPR CNRS 9009, Strasbourg, France.
Rodeau
J L
JL
Taleb
O
O
D000818:Animals; D002463:Cell Membrane Permeability / Q000502:physiology*; D002712:Chlorides / Q000378:metabolism; D018076:DNA, Complementary; D004594:Electrophysiology; D005561:Formates / Q000378:metabolism; D005998:Glycine / Q000378:metabolism*; D015640:Ion Channel Gating / Q000502:physiology*; D008845:Microinjections; D009865:Oocytes; D018408:Patch-Clamp Techniques; D018009:Receptors, Glycine / Q000737:chemistry / Q000378:metabolism*; D014162:Transfection; D014981:Xenopus
D002712:Chlorides; D018076:DNA, Complementary; D005561:Formates; D018009:Receptors, Glycine; C030544:formic acid; D005998:Glycine