Signal transduction and pharmacological characteristics of a metabotropic glutamate receptor, mGluRl, in transfected CHO cells

  title={Signal transduction and pharmacological characteristics of a metabotropic glutamate receptor, mGluRl, in transfected CHO cells},
  author={Ichiro Aramori and Shigetada Nakanishi},
Pharmacological Properties of Metabotropic Glutamate Receptors
The use of this sensitive technique allowed other investigators to begin characterizing the various receptor systems that were linked to this novel second-messenger system in the CNS (see Fisher and Agranoff, 1987).
Role of the Second and Third Intracellular Loops of Metabotropic Glutamate Receptors in Mediating Dual Signal Transduction Activation*
Two residues are uncovered that are crucial for coupling to both pathways, since their substitution leads to receptor inactivation, and are introduced within the second and third intracellular loops of mGluR1α.
Activation of metabotropic glutamate receptors increases cAMP accumulation in hippocampus by potentiating responses to endogenous adenosine
  • DG Winder, P. Conn
  • Biology
    The Journal of neuroscience : the official journal of the Society for Neuroscience
  • 1993
The hypothesis that 1S,3R- ACPD-stimulated increases in cAMP accumulation in rat hippocampal slices are dependent upon the presence of endogenous adenosine and are mediated by an mGluR that potentiates cAMP responses to other agonists is tested.
Novel functions for subtypes of metabotropic glutamate receptors
  • D. Schoepp
  • Biology, Chemistry
    Neurochemistry International
  • 1994
Group I metabotropic glutamate receptors, mGlu1a and mGlu5a, couple to cyclic AMP response element binding protein (CREB) through a common Ca2+‐ and protein kinase C‐dependent pathway
Although the [Ca2+]i signatures activated by these mGlu receptors differ, they couple to CREB with comparable potency and recruit similar downstream components to execute CREB phosphorylation, indicating that coupling of the group I mGLU receptors to CREBs occurs independently of these pathways.
Regulation of mitogen-activated protein kinases by Group I metabotropic glutamate receptors
Stimulation of mGlula/mGlu5a receptors, did not alter cellular proliferation, or have a marked effect on cytoskeletal organisation, as measured by immunocytochemistry, indicating that the activation of mitogenic signalling by these two mGlu receptors does not result in changes in growth in these cells.


A transfected m1 muscarinic acetylcholine receptor stimulates adenylate cyclase via phosphatidylinositol hydrolysis.
Observations suggest that carbachol-stimulated cAMP accumulation does not occur through direct m1 muscarinic receptor coupling or through the release of arachidonic acid and its metabolites, but is mediated through the activation of phospholipase C.
A new type of glutamate receptor linked to inositol phospholipid metabolism
Evidence is reported for a new type of Glu receptor, which prefers Q A as agonist, and which directly activates inositol phospholipid metabolism through interaction with GTP-binding regulatory proteins, leading to the formation of inositl 1,4,5-trisphosphate (InsP3) and mobilization of intracellular Ca2+.
Transfected D2 dopamine receptors mediate the potentiation of arachidonic acid release in Chinese hamster ovary cells.
Results suggest that the D2 receptor may be increasing the release of arachidonic acid by a mechanism involving protein kinase C but independent of the D 2 receptor's inhibition of adenylyl cyclase.
Arachidonic acid released from striatal neurons by joint stimulation of ionotropic and metabotropic quisqualate receptors
It is reported that in mature striatal neurons in primary cultures, quisqualate can release arachidonic acid by associatively activating both quisQualate metabotropic receptors coupled to phospholipase C (Qp) and Qi receptors21.
Glutamate stimulates inositol phosphate formation in striatal neurones
The results suggest that excitatory amino acids stimulate inositol phosphate formation directly, rather than indirectly by the evoked release and subsequent actions of adenosine4 or acetylcholine5.