Agonist binding to purified glycine receptor reconstituted into giant liposomes elicits two types of chloride currents

FEBS Letters

Riquelme, Gloria¹  López, Elena¹  González Ros, José M.¹  Ferragut, José A.¹  Mayor, Frederico²  Morato, Esperanza²  Ruiz-Gómez, Ana² 

[1] Department of Neurochemistry and Institute of Neurosciences, University of Alicante, San Juan, 03550 Alicante, Spain;Departamento de Biologia Molecular, Centra de Biologia Molecular (CSIC-UAM), Universidad Autónoma de Madrid, Canto Blanco, 28049 Madrid, Spain

关键词: Ion channel-coupled receptor;    Reconstitution;    Patch-damp method;    Receptor heterogeneity;    GlyR;    glycine receptor;   

DOI  :  10.1016/0014-5793(90)80505-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Using ‘inside-out’ membrane patches obtained from reconstituted giant liposomes containing purified glycine receptor from rat spinal cord, we have detected chloride currents elicited in response to the presence of the agonists glycine or β-alanine. Regardless of the agonist employed, two different patterns of single channel currents could be detected, which differ in their main conductance, complexity of substates and opening frequency. In agreement with the expectations of glycine receptor heterogeneity suggested recently at the mRNA and cDNA level, our results indicate the existence of functionally different glycine receptors in the adult rat spinal cord.

【 授权许可】

Unknown