[3H]R214127: a novel high-affinity radioligand for the mGlu1 receptor reveals a common binding site shared by multiple allosteric antagonists.

@article{Lavreysen20033HR214127AN,
  title={[3H]R214127: a novel high-affinity radioligand for the mGlu1 receptor reveals a common binding site shared by multiple allosteric antagonists.},
  author={Hilde Lavreysen and Cornelus Gerardus Mari Janssen and François Bischoff and Xavier Langlois and Jos{\'e}e E. Leysen and Anne Simone Josephine Lesage},
  journal={Molecular pharmacology},
  year={2003},
  volume={63 5},
  pages={
          1082-93
        }
}
R214127 was shown to be a potent and noncompetitive metabotropic glutamate 1 (mGlu1) receptor-selective antagonist. The kinetics and pharmacology of [(3)H]1-(3,4-dihydro-2H-pyrano[2,3-b]quinolin-7-yl)-2-phenyl-1-ethanone (R214127) binding to rat mGlu1a receptor Chinese hamster ovary (CHO)-dhfr(-) membranes was investigated, as well as the distribution of [(3)H]R214127 binding in rat brain tissue and sections. Specific binding to rat mGlu1a receptor CHO-dhfr(-) membranes was approximately 92% of… 
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