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Review : Glycine Receptors: Molecular Heterogeneity and Implications for Disease

Neurologische Klinik and Zentrum für Molekulare Biologie Universität Heidelberg Heidelberg, Germany

The inhibitory glycine receptor is a ligand-gated chloride channel that exists in developmentally regulated isoforms. These oligomeric transmembrane proteins are composed of variants of the ligand binding subunit and structural ß polypeptides. The agonist and antagonist sites of the subunits are formed by discontinuous sequence motifs. In the murine genome, the genes encoding the 1 ( Glra1), 3 (Glra3), and ß (Glyrb) subunit are autosomally located, whereas the 2 (Glra2) and 4 (Glra4) genes reside on the X-chromosome. Mutations of glycine receptor genes have been found to underly hypertonic motor disorders in mice and humans. The mouse mutants spasmodic (spd) and oscillator (spd^ot) carry recessive mutations of the Glra 1 gene. In the phenotypically similar mouse mutant spastic (spa), the intronic insertion of a LINE-1 transposable element into the Gyrb gene results in the aberrant splicing and a consecutive loss of glycine receptors. The human neurological disorder hyperekplexia (startle disease, stiff baby syndrome) is caused by point mutations within the 1 subunit gene (GLRA1) localized in the human chromosomal region 5q31.3. The Neuroscientist 1:130- 141,1995

Key Words: KEY WORDS Glycine • Hyperekplexia • Inhibition • Mouse mutant • Neurotransmitter receptor • Oscillator mouse • Spasmodic mouse • Spas tic mouse • Strychnine

The Neuroscientist, Vol. 1, No. 3, 130-141 (1995)
DOI: 10.1177/107385849500100304


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