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The GluD2 receptor is a fundamental component of postsynaptic sites in Purkinje neurons, and is required for normal cerebellar function. GluD2 and the closely related GluD1 are classified as members of the ionotropic glutamate receptor iGluR superfamily on the basis of sequence similarity, but do not bind l -glutamate.
Here, we investigate the pharmacology of the orthosteric binding site in GluD2 by examining the activity of analogs of D-Ser and GluN1 glycine site competitive antagonists at GluD2 receptors containing the lurcher mutation GluD2 LC , which promotes spontaneous channel activation.
We identify several compounds that modulate GluD2 LC , including a halogenated alanine analog as well as the kynurenic acid analog 7-chlorooxo-1 H -quinolinecarboxylic acid 7-chlorokynurenic acid; 7-CKA. The GluD2 ligands identified here can potentially serve as a starting point for development of GluD2-selective ligands useful as tools in studies of the signaling role of the GluD2 receptor in the brain.
Similar to the other iGluR subtypes [i. D-Ser and glycine have now been identified as ligands for GluD2 Naur et al. Thus, by its lack of ionotropic activity, the function of the GluD2 receptor in excitatory transmission appears to be fundamentally different from other iGluRs.
A key role for GluD2 in postsynaptic functions in cerebellar Purkinje neurons, including induction of cerebellar long-term depression LTD , a form of synaptic plasticity that underlies motor learning, has been demonstrated Hirai et al. Considerable experimental evidence exists that argues against an ionotropic synaptic signaling function of GluD2. For example, it has been demonstrated that transgenic mice carrying GluD2 mutations in the putative ion channel that abolish ion permeation have a normal phenotype and show intact cerebellar LTD Kakegawa et al.