Characterization of an ACPD-insensitive mGluR coupled to phosphoinositide hydrolysis

Chung, Dorothy S.; Jeffrey, Peter L.

doi:10.1016/0028-3908(96)84677-6

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Phosphoinositide Hydrolysis As a Transduction1

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1997

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“…Evidence suggests, however, that novel mGluRs may also exist that couple to phosphoinositide hydrolysis. For instance, Chung et al (97,98) reported evidence for a phosphoinositide hydrolysis-coupled mGluR in cortical slices that does not correspond to any of the previously cloned mGluR subtypes. This receptor is insensitive to 1S, 3R-ACPD but is selectively activated by BrHIBO or (R, S)4-methylhomoibotenic acid.…”

Section: Phosphoinositide Hydrolysis As a Transductionmentioning

confidence: 99%

Pharmacology and Functions of Metabotropic Glutamate Receptors

1997

Annu. Rev. Pharmacol. Toxicol.

2,859

2,457

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In the mid to late 1980s, studies were published that provided the first evidence for the existence of glutamate receptors that are not ligand-gated cation channels but are coupled to effector systems through GTP-binding proteins. Since those initial reports, tremendous progress has been made in characterizing these metabotropic glutamate receptors (mGluRs), including cloning and characterization of cDNA that encodes a family of eight mGluR subtypes, several of which have multiple splice variants. Also, tremendous progress has been made in developing new highly selective mGluR agonists and antagonists and toward determining the physiologic roles of the mGluRs in mammalian brain. These findings have exciting implications for drug development and suggest that the mGluRs provide a novel target for development of therepeutic agents that could have a significant impact on neuropharmacology.

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Section: Phosphoinositide Hydrolysis As a Transductionmentioning

confidence: 99%