Changes on the properties of glycine receptors during neuronal development

Glycine receptors (GlyRs) play a major role in the excitability of spinal cord and brain stem neurons. During development, several properties of these receptors undergo significant changes resulting in major modifications of their physiological functions. For example, the receptor structure switches...

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Bibliographic Details
Published inBrain Research Reviews Vol. 47; no. 1; pp. 33 - 45
Main Authors Aguayo, Luis G., van Zundert, Brigitte, Tapia, Juan C., Carrasco, Monica A., Alvarez, Francisco J.
Format Book Review Conference Proceeding Journal Article
LanguageEnglish
Published Amsterdam Elsevier B.V 01.12.2004
Elsevier
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Summary:Glycine receptors (GlyRs) play a major role in the excitability of spinal cord and brain stem neurons. During development, several properties of these receptors undergo significant changes resulting in major modifications of their physiological functions. For example, the receptor structure switches from a monomeric α or heteromeric α2β in immature neurons to an α1β receptor type in mature neurons. Together with these changes in receptor subunits, the postsynaptic cluster size increases with development. Parallel to these modifications, the apparent receptor affinity to glycine and strychnine, as well as that of Zn 2+ and ethanol increases with time. The mature receptor is characterized by a slow desensitizing current and high sensitivity to modulation by protein kinase C. Also, the high level of glycinergic transmission in immature spinal neurons modulates neuronal excitability causing membrane depolarization and changes in intracellular calcium. Due to these properties, chronic inhibition of glycinergic transmission affects neurite outgrowth and produces changes in the level of synaptic transmission induced by GABA A and AMPA receptors. Finally, the high level of plasticity found in immature GlyRs is likely associated to changes in cytoskeleton dynamics.
ISSN:0165-0173
1872-6321
DOI:10.1016/j.brainresrev.2004.06.007