Abstract: In synaptic plasma membranes from rat forebrain, the potencies of glycine recognition site agonists and antagonists for modulating (3H)1‐(1‐(2‐thienyl)cyclohexyl)piperidine ((3H)TCP) binding and for displacing strychnine‐insensitive (3H)glycine binding are altered in the presence of N‐methyl‐D‐aspartate (NMDA) recognition site ligands. The NMDA competitive antagonist, cis‐4‐phosphonomethyl‐2‐piperidine carboxylate (CGS 19755), reduces (3H)glycine binding, and the reduction can be fully reversed by the NMDA recognition site agonist, L‐glutamate. Scatchard analysis of (3H)glycine binding shows that in the presence of CGS 19755 there is no change in Bmax (8.81 vs. 8.79 pmol/mg of protein), but rather a decrease in the affinity of glycine (KD of 0.202 γM vs. 0.129 γM). Similar decreases in affinity are observed for the glycine site agonists, D‐serine and 1‐aminocyclopropane‐1‐carboxylate, in the presence of CGS 19755. In contrast, the affinity of glycine antagonists, 1‐hydroxy‐3‐amino‐2‐pyrrolidone and 1‐aminocyclobutane‐1‐carboxylate, at this (3H)glycine recognition site increases in the presence of CGS 19755. The functional consequence of this change in affinity was addressed using the modulation of (3H)TCP binding. In the presence of L‐glutamate, the potency of glycine agonists for the stimulation of (3H)TCP binding increases, whereas the potency of glycine antagonists decreases. These data are consistent with NMDA recognition site ligands, through their interactions at the NMDA recognition site, modulating activity at the associated glycine recognition site.
Journal of Neurochemistry – Wiley
Published: Mar 1, 1990
It’s your single place to instantly
discover and read the research
that matters to you.
Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.
All for just $49/month
Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly
Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.
Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.
Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.
All the latest content is available, no embargo periods.
“Hi guys, I cannot tell you how much I love this resource. Incredible. I really believe you've hit the nail on the head with this site in regards to solving the research-purchase issue.”Daniel C.
“Whoa! It’s like Spotify but for academic articles.”@Phil_Robichaud
“I must say, @deepdyve is a fabulous solution to the independent researcher's problem of #access to #information.”@deepthiw
“My last article couldn't be possible without the platform @deepdyve that makes journal papers cheaper.”@JoseServera