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Molecular Pharmacology

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Abstract

Spermine enhances binding to the glycine site associated with the N-methyl-D-aspartate receptor complex.

A I Sacaan and K M Johnson
Molecular Pharmacology December 1989, 36 (6) 836-839;
A I Sacaan
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K M Johnson
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Abstract

Spermine enhanced strychnine-insensitive [3H]glycine binding 3-fold with an EC50 of 27 +/- 3.1 microM. Spermidine and putrescine were without effect, whereas the ethylenediamine analog of spermine had an intermediate effect. Eadie-Hofstee analysis revealed that spermine increased the affinity of glycine for its receptor without a significant change in receptor density. This effect persisted in the presence of glycine or N-methyl-D-aspartate receptor antagonists. Furthermore, spermine produced a leftward shift in the IC50 of glycine agonists in displacing [3H]glycine binding, without altering the IC50 for glycine antagonists. These data indicate that spermine interacts with the glycine receptor through a novel binding site and, further, that spermine can be used to discriminate glycine agonist and antagonist binding.

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Molecular Pharmacology
Vol. 36, Issue 6
1 Dec 1989
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Abstract

Spermine enhances binding to the glycine site associated with the N-methyl-D-aspartate receptor complex.

A I Sacaan and K M Johnson
Molecular Pharmacology December 1, 1989, 36 (6) 836-839;

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Abstract

Spermine enhances binding to the glycine site associated with the N-methyl-D-aspartate receptor complex.

A I Sacaan and K M Johnson
Molecular Pharmacology December 1, 1989, 36 (6) 836-839;
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