Multiple Signals Participating in GABA Receptor Modulation

摘要: Publisher Summary This chapter focuses on multiple signals participating in γ-aminobutyric acid (GABA) receptor modulation. Benzodiazepine appears to bind a brain site that is contiguous the where GABA binds and occupancy of benzodiazepine recognition by an anxiolytic causes increase Bmax binding high affinity sites. Conversely, stimulation sites agonist increases for this ligand. These interactions are consistent with possibility benzodiazepines occupy co-transmitter might coexist GABAergic axons. Histochemical evidence indicates motilin-like immunoreactivity present axons; however, motilin fails displace 3H-diazepam or modify binding. If peptide endogenous effector, it may not be but, perhaps, anxiogenic. The clear interaction between explained experiments discussed suggests specific mechanism involved. discusses molecular nature mechanism, isolation purification homogeneity protein, GABA-modulin, which modulates these two molecules. GABA-modulin phosphorylated probably process operative allosteric modulation GABA. Benzodiazepines interact modulatory function, changing phosphorylation GABA-modulin.