PMID: 8587649Aug 1, 1995Paper

Different specific binding sites of [3H]glycine and [3H]strychnine in synaptosomal membranes isolated from frog retina

Neurochemical Research
J A Pérez-León, R Salceda

Abstract

Synaptosomal fractions were isolated from frog retina: a fraction enriched in photoreceptor terminals (P1) and a second one (P2) containing interneurons terminals. We compared the binding of [3H]glycine and [3H]strychnine to membranes of these synaptosomes. The binding of both radioactive ligands was saturable and Na(+)-independent. [3H]Glycine bound to a single site in P1 and P2 synaptosomal fractions, with KD = 12 and 82 nM and BMax = 3.1 and 3.06 pmol/mg protein respectively. [3H]Strychnine bound to two sites in each one of the synaptosomal fractions. For P1 KD values were 3.9 and 18.7 nM, and BMax values were 1.1 and 7.1 pmol/mg protein, respectively. Membranes from the P2 synaptosomal fraction showed KD's of 0.6 and 48 nM and BMax's of 0.4 and 4.5 pmol/mg. Specific [3H]glycine binding was displaced by beta-alanine, 1-serine, d-serine and HA966, but not by strychnine, 7-chlorokynurenic or 5,7-dichloro-kynurenic acids. Specific [3H]strychnine binding was partially displaced by glycine and related amino acids and totally displaced only by 2-NH2-strychnine. Our results indicate the presence of high affinity binding sites for glycine and strychnine in frog retinal synaptosomal membranes. The pharmacological binding pattern indi...Continue Reading

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Citations

Jan 25, 2007·Amino Acids·M J Scolari, G B Acosta
Jun 10, 2011·Synapse·Miguel Ángel Velázquez-Flores, Rocío Salceda
Nov 26, 1998·International Journal of Developmental Neuroscience : the Official Journal of the International Society for Developmental Neuroscience·A Rodríguez-ContrerasA M López-Colomé
Jul 16, 2005·Neurochemical Research·Rocío Salceda, Marisela Aguirre-Ramirez

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