Thiocyanate stabilizes AMPA binding to the quisqualate receptor

Citations of this article
Mendeley users who have this article in their library.
Get full text


Calcium and chloride ions stimulated [3H]glutamate binding to quisqualate-sensitive [3H]glutamate binding sites 4-fold, as measured by quantitative autoradiography, whereas 100 mM potassium thiocyanate had no additional effect. In contrast, calcium and chloride had little effect on the binding of [3H](RS)-α-amino-3-hydroxy-5-methylisoxazole-4-proprion ic acid ([3H]AMPA), but 100 mM thiocyanate stimulated binding 4-fold. AMPA displace little [3H]glutamate binding from quisqualate-sensitive binding sites in the molecular layer of the cerebellum in the absence of thiocyanate. However, in the presence of thiocyanate AMPA became a more effective displacer, but still displaced only 44% of the quisqualate-sensitive [3H]glutamate binding. The distribution of [3H]glutamate binding to quisqualate-sensitive sites was similar to but not identical with that of [3H]AMPA binding. However, the distribution of AMPA-displaceable [3H]glutamate binding correlated highly (r = 0.97, P<0.0005) with that of [3H]AMPA binding. The results suggest that AMPA binds to a subclass of quisqualate-sensitive [3H]glutamate binding sites that are highly influenced by ionic environment and that quisqualate-sensitive binding sites exist in several states. © 1988.




Nielsen, E., Cha, J. H. J., Honoré, T., Penney, J. B., & Young, A. B. (1988). Thiocyanate stabilizes AMPA binding to the quisqualate receptor. European Journal of Pharmacology, 157(2–3), 197–203.

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free