Glycine receptors: What gets in and why?

Citation
Ph. Barry et al., Glycine receptors: What gets in and why?, CLIN EXP PH, 26(11), 1999, pp. 935-936
Citations number
12
Categorie Soggetti
Pharmacology & Toxicology
Journal title
CLINICAL AND EXPERIMENTAL PHARMACOLOGY AND PHYSIOLOGY
ISSN journal
03051870 → ACNP
Volume
26
Issue
11
Year of publication
1999
Pages
935 - 936
Database
ISI
SICI code
0305-1870(199911)26:11<935:GRWGIA>2.0.ZU;2-Y
Abstract
1, The glycine receptor channel (GlyR), a member of the ligand-gated ion ch annel superfamily; shares many similar permeation properties with the GABAA receptor channel. 2, The GlyR is anion permeable, with P-K/P-Cl < 0,05, has a 5-6 Angstrom mi nimum pore diameter and a permeation selectivity sequence dominated by hydr ation energies. 3, The channels, which display multiple subconductance states, can be multi ply occupied, 4 Two positive arginine rings at the ends of the pore region may contribute to the anion selectivity of the GlyR, 5, Mutation of the extracellular charged arginine ring can impair channel f unction by decreasing the sensitivity of glycine activation, reducing chann el conductance, shifting the normal multi-subconductance states to lower va lues and by decoupling the link between ligand binding and channel gating, 6, These and other site-directed mutagenesis studies of recombinant GlyR;RI together with studies of native GlyR, are providing further insights into what controls gating and ion permeation and selectivity through this channe l.