The mammalian glycine receptor: biology and structure of a neuronal chloride channel protein |
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| Affiliation: | 1. School of Veterinary Medicine, University College Dublin, Belfield, Dublin 4, Ireland;2. School of Agriculture and Food Science, University College Dublin, Belfield, Dublin 4, Ireland;3. School of Food Science & Env. Health, Dublin Institute of Technology, Ireland;4. Faculty of Veterinary Medicine, University of Kufa, Iraq;1. Institute of Tropical Agriculture and Forestry, Hainan University, Haikou 570228, China;2. Department of Entomology, Nanjing Agricultural University, Nanjing 210095, China;3. Institute of Insect Science, Zhejiang University, Hangzhou 310058, China |
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| Abstract: | Glycine is a major inhibitory neurotransmitter in the central nervous system (CNS) of vertebrates and invertebrates. The postsynaptic receptor for this amino acid is an oligomeric glycoprotein which, upon binding of glycine, transiently forms an anion-selective transmembrane channel. Agonist-mediated receptor activation is antagonized by strychnine, a high-affinity ligand of the glycine receptor (GlyR). Biochemical and immunological data show that affinity-purified preparations of the mammalian GlyR contain three polypeptides of Mr 48,000, 58,000 and 93,000. These polypeptides have different functional properties and/or topologies in the postsynaptic membrane of the glycinergic synapse. The primary sequence of the Mr 48,000 subunit deduced by cDNA cloning exhibits structural and amino-acid homology to nicotinic acetylcholine and GABAa receptor proteins, indicating a common evolutionary relationship between the different neurotransmitter-gated ion channels of excitable membranes. Monoclonal antibodies against the GlyR allow its histochemical localization in different regions of the CNS. GlyR deficiencies have been implicated in the pathogenesis of spasticity and spinal cord degeneration in mouse and man. |
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