• Corpus ID: 9054023

CPCCOEt, a noncompetitive metabotropic glutamate receptor 1 antagonist, inhibits receptor signaling without affecting glutamate binding.

@article{Litschig1999CPCCOEtAN,
  title={CPCCOEt, a noncompetitive metabotropic glutamate receptor 1 antagonist, inhibits receptor signaling without affecting glutamate binding.},
  author={Stephan Litschig and Fabrizio Gasparini and D Rueegg and Natacha Stoehr and Peter Josef Flor and Ivo Vranesic and Laurent Prézeau and Jean-Philippe Pin and Christian Thomsen and Rainer Kuhn},
  journal={Molecular pharmacology},
  year={1999},
  volume={55 3},
  pages={
          453-61
        }
}
Metabotropic glutamate receptors (mGluRs) are a family of G protein-coupled receptors characterized by a large, extracellular N-terminal domain comprising the glutamate-binding site. In the current study, we examined the pharmacological profile and site of action of the non-amino-acid antagonist 7-hydroxyiminocyclopropan[b]chromen-1a-carboxylic acid ethyl ester (CPCCOEt). CPCCOEt selectively inhibited glutamate-induced increases in intracellular calcium at human mGluR1b (hmGluR1b) with an… 

Figures and Tables from this paper

BAY36-7620: a potent non-competitive mGlu1 receptor antagonist with inverse agonist activity.
TLDR
BAY36-7620 will be useful to further delineate the functional importance of the mGlu1 receptor, including its putative agonist-independent activity, andTransmembrane helices 4 to 7 are shown to play a critical role in the selectivity of BAY36- 7620.
The non-competitive metabotropic glutamate receptor-1 antagonist CPCCOEt inhibits the in vitro growth of human melanoma.
TLDR
A selective, non-competitive metabotropic glutamate receptor-1 antagonist, CPCCOEt (7-hydroxyiminocyclopropan[b]chromen-1a-carboxylic acid ethyl ester), significantly inhibited the proliferation and modified the morphology of two human melanoma cell lines, thus enhancing existing therapies of melanoma and possibly other malignancies.
Supersensitivity of human metabotropic glutamate 1a receptor signaling in L929sA cells.
TLDR
These results suggest that antagonist-evoked mGlu1 receptor supersensitivity is not merely the result of a blockade of agonist-induced desensitization, and are the first lines of evidence that prolonged antagonist treatment can supersensitize the hmGlu 1a receptor.
Construction of a High Affinity Zinc Binding Site in the Metabotropic Glutamate Receptor mGluR1
TLDR
It is proposed that binding of zinc has introduced a structural constraint in the ATD lobe, preventing the formation of a “closed” conformation, and thus stabilizing a more or less inactive “open” form of the AtD.
A Novel Selective Allosteric Modulator Potentiates the Activity of Native Metabotropic Glutamate Receptor Subtype 5 in Rat Forebrain
TLDR
It is found that allosteric potentiation of mGluR5 increases the effect of threshold agonist concentrations in native systems and potentiated NMDA receptor currents in hippocampal slices induced by threshold levels of DHPG, whereas having no effect on these currents by itself.
...
...

References

SHOWING 1-10 OF 54 REFERENCES
Actions of phenylglycine analogs at subtypes of the metabotropic glutamate receptor family.
(R,S)-4-phosphonophenylglycine, a potent and selective group III metabotropic glutamate receptor agonist, is anticonvulsive and neuroprotective in vivo.
TLDR
(R,S)-4-phosphonophenylglycine (PPG) is described as a novel, potent, and selective agonist for group III mGluRs and protected against N-methyl-D-aspartate- and quinolinic acid-induced striatal lesions in rats and was anticonvulsive in the maximal electroshock model in mice.
Pharmacological characterization of 1-aminoindan-1,5-dicarboxylic acid, a potent mGluR1 antagonist.
TLDR
The pharmacological profile of 1-aminoindan-1,5-dicarboxylic acid, a rigid (carboxyphenyl)glycine derivative acting on metabotropic glutamate receptors (mGluRs) is examined to suggest that AIDA is a potent, selective and competitive mGluR1 a antagonist.
The agonist selectivity of a class III metabotropic glutamate receptor, human mGluR4a, is determined by the N-terminal extracellular domain
To test the hypothesis that the determinants for agonist selectivity of class III metabotropic glutamate receptors (mGluRs) are localized in the N-terminal extracellular domain, a chimaeric cDNA was
N‐Acetylaspartylglutamate Selectively Activates mGluR3 Receptors in Transfected Cells
TLDR
Sequence homology and pharmacological data suggest that these two receptors are highly related structurally and functionally and NAAG selectively activated the mGluR3 receptor.
...
...