| Autor: |
Pullan LM; Department of Pharmacology, ICI Pharmaceuticals, ICI Americas Inc., Wilmington, DE 19897., Verticelli AM, Paschetto KA |
| Jazyk: |
angličtina |
| Zdroj: |
European journal of pharmacology [Eur J Pharmacol] 1991 Sep 12; Vol. 208 (1), pp. 25-9. |
| DOI: |
10.1016/0922-4106(91)90047-l |
| Abstrakt: |
HA-966 (1-hydroxy-3-amino-pyrrolid-2-one), an antagonist at the strychnine-insensitive glycine site on the N-methyl-D-aspartate (NMDA) receptor complex, only partially inhibits the binding of noncompetitive antagonists to the NMDA receptor but enhances the binding of the NMDA competitive antagonist CPP (3-(2-carboxypiperazin-4-yl)propyl-1-phosphonic acid). Here we report that the IC50 of the active (R)-enantiomer of HA-966 for displacement of [3H]glycine binding is decreased in the presence of spermine, suggesting that spermine increases the affinity of (R)-HA-966 at the [3H]glycine binding site. The IC50 values of the agonist glycine and the partial agonist 1-aminocyclopropane-1-carboxylate are also decreased. The IC50 values of glycine antagonists 6,7-dinitroquinoxalin-2,3-dione and 7-chlorokynurenic acid are not significantly altered. The spermine shift represents the first demonstration of the agonist-like character of the (R)-enantiomer of HA-966 at the glycine site. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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