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Agonist binding to purified glycine receptor reconstituted into giant liposomes elicits two types of chloride currents
Author(s) -
Riquelme Gloria,
Morato Esperanza,
López Elena,
Ruiz-Gómez Ana,
Ferragut José A.,
González Ros José M.,
Mayor Frederico
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80505-d
Subject(s) - glycine , agonist , liposome , chemistry , glycine receptor , receptor , chloride , biophysics , biochemistry , amino acid , biology , organic chemistry
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.