Lee Shekter - Molecular structure and pharmacological characterization of humEAA2, a novel human kainate receptor subunit.

Document created by Lee Shekter on Aug 22, 2014
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  Publication Details (including relevant citation   information): Kamboj,R.K., Schoepp,D.D., Nutt,S.,   Shekter,L., Korczak,B., True,R.A., Zimmerman,D.M., Wosnick,M.A.,   Mol Pharmacol, 1992, 42 (1),   pp 10-15

  Abstract: A cDNA encoding a novel human   glutamate receptor subunit protein was isolated from a human   hippocampal library. This cDNA, termed humEAA2, is most closely   related to rat cDNAs for kainate receptor proteins and, when   expressed in COS cells, is associated with high affinity kainate   receptor binding. The relative potency of compounds in displacing   [3H]kainate binding was kainate greater than quisqualate greater   than domoate greater than L-glutamate much greater than   6,7-dinitroquinoxaline-2,3-dione greater than dihydrokainate   greater than 6-cyano-7-nitroquinoxaline-2,3-dione greater than   (RS)-alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid.   Homomeric expression of humEAA2 does not appear to elicit   ligand-gated channel activity. Nevertheless, the molecular   structure and pharmacology of high affinity kainate binding   suggest that humEAA2 is a novel subunit protein of a human   kainate receptor complex.

  Address (URL): http://www.hubmed.org/display.cgi?uids=1321949