Does beta-alanine activate more than one chloride channel associated receptor?
In order to define which receptor-channel complexes are activated by beta-alanine, we performed cross-desensitization experiments between this amino acid and the classical inhibitory neurotransmitters, glycine and gamma-aminobutyric acid (GABA), all of which increase chloride conductances. Using the whole-cell patch-clamp technique and cultured chick spinal neurons, we found that beta-alanine completely desensitizes the glycine response, and only partially reduces GABA evoked currents. No interaction occurred between GABA and glycine at the level of their respective receptors. Conversely, both GABA and glycine reduced the beta-alanine response. These results indicate that beta-alanine activates the glycine receptor, and also suggest that it could be a partial agonist of GABAA receptor(s).
D000409:Alanine / Q000494:pharmacology*; D000818:Animals; D002478:Cells, Cultured; D002645:Chickens; D018118:Chloride Channels; D002712:Chlorides / Q000378:metabolism*; D004553:Electric Conductivity; D005998:Glycine / Q000494:pharmacology; D007473:Ion Channels / Q000187:drug effects / Q000502:physiology; D008565:Membrane Proteins / Q000378:metabolism*; D009474:Neurons / Q000187:drug effects / Q000502:physiology*; D013116:Spinal Cord / Q000502:physiology*; D015091:beta-Alanine / Q000494:pharmacology*; D005680:gamma-Aminobutyric Acid / Q000494:pharmacology
D018118:Chloride Channels; D002712:Chlorides; D007473:Ion Channels; D008565:Membrane Proteins; D015091:beta-Alanine; D005680:gamma-Aminobutyric Acid; D000409:Alanine; D005998:Glycine