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Sites of anaesthetic action on ligand-gated ion channels

  • R. A. Harris
  • M. P. Mascia
  • I. A. Lobo
Conference paper

Abstract

In searching for the molecular targets of anaesthetic action, the ligand-gated ion channel family has emerged as a group of proteins particularly sensitive to general anaesthetics [1]. One member of this family is the strychnine-sensitive glycine receptor, a protein that mediates inhibition mainly in the brainstem and spinal cord. Activation of this receptor by glycine induces opening of the functional part of the receptor, an integral chloride channel. The glycine receptor is composed of α (α 1–4) and β subunits organized in a pentameric structure of 3 α and 2 β surrounding the central channel [2]. However, during pre-natal development and until 2–3 weeks after birth the glycine receptor is mainly homomeric, consisting of α2 subunits. Glycine α subunits can therefore be expressed homomerically in heterologous systems, such as Xenopus laevis oocytes, to produce functional homomeric receptors with similar pharmacological properties to native receptors [3].

Keywords

Volatile Anaesthetic Glycine Receptor Xenopus Laevis Oocyte Anaesthetic Action Glycine Response 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Italia 2003

Authors and Affiliations

  • R. A. Harris
  • M. P. Mascia
  • I. A. Lobo

There are no affiliations available

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