mGlu<sub>1</sub> receptor | Metabotropic glutamate receptors | IUPHAR/BPS Guide to PHARMACOLOGY

mGlu1 receptor

Target id: 289

Nomenclature: mGlu1 receptor

Family: Metabotropic glutamate receptors

Annotation status:  image of a green circle Annotated and expert reviewed. Please contact us if you can help with updates.  » Email us

   GtoImmuPdb view: OFF :     Currently no data for mGlu1 receptor in GtoImmuPdb

Gene and Protein Information
class C G protein-coupled receptor
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human 7 1194 6q24 GRM1 glutamate metabotropic receptor 1 19,32,100
Mouse 7 1199 10 A2 Grm1 glutamate receptor, metabotropic 1 124
Rat 7 1199 1p13 Grm1 glutamate metabotropic receptor 1 42,76
Previous and Unofficial Names
GPRC1A | wobl | metabotropic glutamate receptor 1 | MGLUR1 | SCAR13 | glutamate receptor, metabotropic 1 | glutamate receptor
Database Links
Specialist databases
GPCRDB grm1_human (Hs), grm1_mouse (Mm), grm1_rat (Rn)
Other databases
ChEMBL Target
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Gene
OMIM
Orphanet
RefSeq Nucleotide
RefSeq Protein
UniProtKB
Wikipedia
Selected 3D Structures
Image of receptor 3D structure from RCSB PDB
Description:  Crystal structure of metabotropic glutamate receptor subtype 1 complexed with glutamate
PDB Id:  1EWK
Resolution:  2.2Å
Species:  Rat
References:  55
Image of receptor 3D structure from RCSB PDB
Description:  Crystal structure of metabotropic glutamate receptor subtype 1 ligand free form II
PDB Id:  1EWV
Resolution:  4.0Å
Species:  Rat
References:  55
Image of receptor 3D structure from RCSB PDB
Description:  Crystal Structure of Metabotropic Glutamate Receptor Subtype 1 Complexed with Glutamate and Gadolinium Ion
PDB Id:  1ISR
Resolution:  4.0Å
Species:  Rat
References:  113
Image of receptor 3D structure from RCSB PDB
Description:  Crystal Structure of Metabotropic Glutamate Receptor Subtype 1 Complexed with an antagonist
PDB Id:  1ISS
Resolution:  3.3Å
Species:  Rat
References:  113
Image of receptor 3D structure from RCSB PDB
Description:  Crystal structure of metabotropic glutamate receptor subtype 1 ligand free form 1
PDB Id:  1EWT
Resolution:  3.7Å
Species:  Rat
References:  55
Image of receptor 3D structure from RCSB PDB
Description:  Metabotropic glutamate receptor mGluR1 complexed with LY341495 antagonist
PDB Id:  3KS9
Ligand:  LY341495
Resolution:  1.9Å
Species:  Human
References: 
Image of receptor 3D structure from RCSB PDB
Description:  Structure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulator.
PDB Id:  4OR2
Ligand:  FITM
Resolution:  2.8Å
Species:  Human
References:  118
Natural/Endogenous Ligands
L-glutamic acid
Comments: Other endogenous ligands include L-aspartic acid, L-serine-O-phosphate, NAAG and L-cysteine sulphinic acid

Download all structure-activity data for this target as a CSV file

Agonists
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Reference
[3H]quisqualate Rn Full agonist 7.5 – 7.7 pKd 57,70
pKd 7.5 – 7.7 [57,70]
quisqualate Rn Full agonist 7.5 – 8.0 pKi 57,82
pKi 7.5 – 8.0 [57,82]
L-glutamic acid Rn Full agonist 6.4 – 6.5 pKi 57,82
pKi 6.4 – 6.5 [57,82]
ibotenic acid Rn Full agonist 5.9 – 6.4 pKi 82,111
pKi 5.9 – 6.4 [82,111]
(1S,3R)-ACPD Rn Full agonist 5.5 – 6.1 pKi 57,82,111
pKi 5.5 – 6.1 [57,82,111]
3,5-DHPG Rn Full agonist 5.8 pKi 57
pKi 5.8 [57]
L-CCG-I Rn Full agonist 5.6 pKi 82
pKi 5.6 [82]
L-glutamic acid Hs Agonist 4.8 – 5.0 pEC50 86
pEC50 4.8 – 5.0 [86]
(S)-3HPG Rn Partial agonist 4.9 pIC50 82
pIC50 4.9 [82]
View species-specific agonist tables
Agonist Comments
Values indicated are those determined from binding studies on recombinant mGlu1a receptors. Further information on agonist pharmacology as based on functional assays can be found in [94].

So far no differences in the agonist pharmacological profile has been reported between the rat and human mGlu1 receptors using functional assays.

The best characterized agonists of the ionotropic glutamate receptors, AMPA, NMDA and kainate are inactive on mGlu1. Although several splice variants of mGlu1 have been identified (see below), all are likely to have an identical agonist pharmacology since they possess an indentical agonist binding site.

The agonist binding site is located in the large extracellular domain of this receptor, that retains its ability to bind ligands when produced as a soluble protein. The structure of this binding domain has been solved [55,113]. This domain is formed of two lobes, and agonists bind in the cleft between the two lobes. Agonists likely stabilize a closed form of this domain, whereas antagonists prevent closure. Functional importance of critical residues involved in agonist action has been confirmed by mutagenesis studies [83,92].

Cations such as Ca2+ have been proposed to directly activate mGlu1 receptors [27,54,108]. However, it is still unclear whether this is a direct agonist effect or if this is due to a potentiation of ambient glutamate produced by the cells expressing the recombinant receptor.
Antagonists
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Reference
AIDA Hs Antagonist 4.2 pA2 81
pA2 4.2 [81]
[11C]JNJ-16567083 Rn Antagonist 9.1 pKi 43
pKi 9.1 (Ki 8.7x10-10 M) [43]
LY341495 Hs Antagonist 7.8 pKi 50
pKi 7.8 [50]
(S)-4C3HPG Hs Antagonist 5.8 – 6.0 pKi 57,82
pKi 5.8 – 6.0 [57,82]
LY367385 Rn Antagonist 5.9 pKi 57
pKi 5.9 (Ki 1.26x10-6 M) [57]
(S)-4CPG Rn Antagonist 5.4 pKi 57
pKi 5.4 [57]
DCG-IV Rn Antagonist 4.1 pKi 82
pKi 4.1 [82]
AIDA Rn Antagonist 4.0 pKi 57
pKi 4.0 [57]
(+)-MCPG Rn Antagonist 3.8 pKi 57
pKi 3.8 [57]
3-MATIDA Rn Antagonist 5.2 pIC50 80
pIC50 5.2 (IC50 6.3x10-6 M) [80]
LY367385 Hs Antagonist 5.1 pIC50 14
pIC50 5.1 (IC50 8.8x10-6 M) [14]
(S)-TBPG Rn Antagonist 4.2 pIC50 18
pIC50 4.2 (IC50 6.89x10-5 M) [18]
(S)-(+)-CBPG Rn Antagonist 4.2 pIC50 71
pIC50 4.2 (IC50 6.7x10-5 M) [71]
View species-specific antagonist tables
Antagonist Comments
Indicated affinities were determined by displacement studies of [3H]quisqualate bound on HEK cell membranes expressing a recombinant rat mGlu1 (except for LY341495 value determined from functional studies). More information on agonist potencies determined from functional studies can be obtained from [94]. So far no differences have been reported for the antagonist affinities between the rat and the human receptor. Although LY367385 and AIDA have been shown to specifically antagonize mGlu1 receptors versus mGlu5, both compounds are able to displace bound [3H]quisqualate to mGlu5 (see [94]).
Allosteric Modulators
Key to terms and symbols View all chemical structures Click column headers to sort
Ligand Sp. Action Affinity Units Reference
[3H]R214127 Hs Negative 9.0 pKd 57
pKd 9.0 [57]
[3H]EM-TBPC Rn Positive 8.2 pKd 70
pKd 8.2 [70]
[3H]YM298198 Rn Negative 7.5 pKd 53
pKd 7.5 (Kd 3.2x10-8 M) [53]
BAY 367620 Rn Negative 9.5 pKi 11
pKi 9.5 (Ki 3.4x10-10 M) [11]
compound 23c [PMID: 17929793] Rn Negative 9.4 pKi 119
pKi 9.4 (Ki 4x10-10 M) [119]
[11C]MMTP Rn Negative 9.2 pKi 89
pKi 9.2 (Ki 6x10-10 M) [89]
[18F]FITM Rn Negative 9.1 pKi 120
pKi 9.1 (Ki 8.7x10-10 M) [120]
compound 11c [PMID: 17929793] Rn Negative 9.0 pKi 119
pKi 9.0 (Ki 1x10-9 M) [119]
NPS2390 Rn Negative 8.9 pKi 57
pKi 8.9 [57]
R214127 Rn Negative 8.9 pKi 57
pKi 8.9 [57]
JNJ-16567083 Rn Negative 8.9 pKi 43
pKi 8.9 (Ki 1.4x10-9 M) [43]
compound 23h [PMID: 17929793] Rn Negative 8.8 pKi 119
pKi 8.8 (Ki 1.5x10-9 M) [119]
compound 23e [PMID: 17929793] Rn Negative 8.8 pKi 119
pKi 8.8 (Ki 1.5x10-9 M) [119]
compound 11q [PMID: 19433355] Rn Negative 8.5 pKi 91
pKi 8.5 (Ki 3.5x10-9 M) [91]
compound 9a [PMID: 22266036] Hs Negative 8.4 pKi 6
pKi 8.4 (Ki 3.6x10-9 M) [6]
compound 22 [PMID: 17276684] Hs Negative 8.4 pKi 20
pKi 8.4 (Ki 3.6x10-9 M) [20]
compound 11s [PMID: 19433355] Rn Negative 8.3 pKi 91
pKi 8.3 (Ki 4.7x10-9 M) [91]
compound 12e [PMID: 22266036] Rn Negative 8.3 pKi 6
pKi 8.3 (Ki 5.2x10-9 M) [6]
A-794278 Rn Negative 8.3 pKi 123
pKi 8.3 (Ki 5.4x10-9 M) [123]
FITM Rn Negative 8.3 pKi 30
pKi 8.3 (Ki 5.4x10-9 M) [30]
Description: Measured using rat brain homogenate in a competition binding assay displacing [18F}-FITM.
compound 27 [PMID: 20346665] Rn Negative 8.1 pKi 90
pKi 8.1 (Ki 7.9x10-9 M) [90]
compound 29 [PMID: 17064898] Rn Negative 8.0 pKi 85
pKi 8.0 (Ki 9.3x10-9 M) [85]
FPTQ Rn Negative 7.9 pKi 29
pKi 7.9 (Ki 1.26x10-8 M) [29]
EM-TBPC Rn Negative 7.8 pKi 70
pKi 7.8 (Ki 1.7x10-8 M) [70]
Ro67-7476 Rn Positive 7.5 – 7.9 pKi 51
pKi 7.5 – 7.9 (Ki 3.16x10-8 – 1.26x10-8 M) [51]
YM-202074 Rn Negative 7.7 pKi 52
pKi 7.7 (Ki 2x10-8 M) [52]
Ro01-6128 Rn Positive 7.5 – 7.7 pKi 51
pKi 7.5 – 7.7 (Ki 3.16x10-8 – 1.99x10-8 M) [51]
compound 24 [PMID: 20346665] Hs Negative 6.9 pKi 90
pKi 6.9 (Ki 1.15x10-7 M) [90]
compound 24 [PMID: 20346665] Rn Negative 6.9 pKi 90
pKi 6.9 (Ki 1.15x10-7 M) [90]
compound 2f [PMID: 17532216] Hs Negative 6.9 pKi 117
pKi 6.9 (Ki 1.27x10-7 M) [117]
LY456066 Rn Negative 6.8 pKi 31
pKi 6.8 (Ki 1.43x10-7 M) [31]
CPCCOEt Rn Negative 5.3 pKi 57
pKi 5.3 [57]
Ro67-4853 Rn Positive 5.1 pKi 51
pKi 5.1 (Ki 7.94x10-6 M) [51]
Ro0711401 Rn Positive 7.3 pEC50 116
pEC50 7.3 (EC50 5.6x10-8 M) [116]
compound 3a [PMID: 16099654] Rn Positive 7.2 pEC50 115
pEC50 7.2 (EC50 6.5x10-8 M) [115]
compound 4b [PMID: 16099654] Rn Positive 7.2 pEC50 115
pEC50 7.2 (EC50 6.5x10-8 M) [115]
VU 0483605 Hs Positive 6.4 pEC50 12
pEC50 6.4 (EC50 3.9x10-7 M) [12]
VU-71 Rn Positive 5.6 pEC50 115
pEC50 5.6 (EC50 2.4x10-6 M) [115]
CPCCOEt Rn Negative 5.3 pEC50 58
pEC50 5.3 (EC50 5x10-6 M) [58]
compound 11q [PMID: 19433355] Hs Negative 9.1 pIC50 91
pIC50 9.1 (IC50 9x10-10 M) [91]
A-841720 Rn Negative 9.0 – 9.0 pIC50 122-123
pIC50 9.0 – 9.0 (IC50 1.05x10-9 – 1x10-9 M) [122-123]
JNJ16259685 Hs Negative 8.9 pIC50 61
pIC50 8.9 (IC50 1.21x10-9 M) [61]
compound 23i [PMID: 17929793] Hs Negative 8.9 pIC50 119
pIC50 8.9 (IC50 1.4x10-9 M) [119]
compound 24 [PMID: 20346665] Hs Negative 8.7 pIC50 90
pIC50 8.7 (IC50 2.1x10-9 M) [90]
compound 11s [PMID: 19433355] Hs Negative 8.7 pIC50 91
pIC50 8.7 (IC50 2.1x10-9 M) [91]
compound 23h [PMID: 17929793] Hs Negative 8.7 pIC50 119
pIC50 8.7 (IC50 2.2x10-9 M) [119]
compound 23c [PMID: 17929793] Hs Negative 8.6 pIC50 119
pIC50 8.6 (IC50 2.5x10-9 M) [119]
CFMTI Hs Negative 8.6 pIC50 93
pIC50 8.6 (IC50 2.6x10-9 M) [93]
compound 23e [PMID: 17929793] Hs Negative 8.5 pIC50 119
pIC50 8.5 (IC50 2.9x10-9 M) [119]
A-794282 Hs Negative 8.5 pIC50 121
pIC50 8.5 (IC50 3x10-9 M) [121]
compound 22 [PMID: 19289283] Rn Negative 8.5 pIC50 72
pIC50 8.5 (IC50 3x10-9 M) [72]
[18F]MK-1312 Hs Negative 8.4 pIC50 41
pIC50 8.4 (IC50 3.6x10-9 M) [41]
MK-5435 Hs Negative 8.4 pIC50 41
pIC50 8.4 (IC50 4.3x10-9 M) [41]
A-794282 Rn Negative 8.3 pIC50 123
pIC50 8.3 (IC50 4.7x10-9 M) [123]
FTIDC Rn Negative 8.3 pIC50 104
pIC50 8.3 (IC50 4.8x10-9 M) [104]
compound 11c [PMID: 17929793] Hs Negative 8.3 pIC50 119
pIC50 8.3 (IC50 4.9x10-9 M) [119]
[18F]FITM Hs Negative 8.3 pIC50 120
pIC50 8.3 (IC50 5.1x10-9 M) [120]
[18F]FPIT Rn Negative 8.3 pIC50 28
pIC50 8.3 (IC50 5.4x10-9 M) [28]
FTIDC Hs Negative 8.2 pIC50 104
pIC50 8.2 (IC50 5.8x10-9 M) [104]
compound 32 [PMID: 19289283] Rn Negative 8.2 pIC50 72
pIC50 8.2 (IC50 6x10-9 M) [72]
compound 10i [PMID: 23084894] Hs Negative 8.2 pIC50 10
pIC50 8.2 (IC50 6x10-9 M) [10]
compound 9a [PMID: 22266036] Hs Negative 8.2 pIC50 6
pIC50 8.2 (IC50 6.3x10-9 M) [6]
compound 9n [PMID: 23084894] Hs Negative 8.1 pIC50 10
pIC50 8.1 (IC50 7x10-9 M) [10]
YM-202074 Rn Negative 8.1 pIC50 52
pIC50 8.1 (IC50 8.6x10-9 M) [52]
compound 29 [PMID: 17064898] Rn Negative 8.1 pIC50 85
pIC50 8.1 (IC50 9x10-9 M) [85]
[11C]MMTP Hs Negative 8.0 pIC50 89
pIC50 8.0 (IC50 9.5x10-9 M) [89]
A-841720 Hs Negative 8.0 pIC50 121
pIC50 8.0 (IC50 1x10-8 M) [121]
A-794278 Hs Negative 8.0 pIC50 121
pIC50 8.0 (IC50 1x10-8 M) [121]
R214127 Hs Negative 8.0 pIC50 57
pIC50 8.0 (IC50 1.04x10-8 M) [57]
compound 12e [PMID: 22266036] Hs Negative 7.9 pIC50 6
pIC50 7.9 (IC50 1.2x10-8 M) [6]
DM-PPP Rn Negative 7.8 pIC50 79
pIC50 7.8 [79]
YM298198 Rn Negative 7.8 pIC50 53
pIC50 7.8 [53]
3,5-dimethyl PPP Rn Negative 7.8 pIC50 79
pIC50 7.8 (IC50 1.58x10-8 M) [79]
compound 3 [PMID: 12470711] Rn Negative 7.8 pIC50 79
pIC50 7.8 (IC50 1.6x10-8 M) [79]
compound 27 [PMID: 20346665] Hs Negative 7.6 pIC50 90
pIC50 7.6 (IC50 2.7x10-8 M) [90]
LY456066 Hs Negative 7.6 pIC50 31
pIC50 7.6 (IC50 2.8x10-8 M) [31]
BAY 367620 Rn Negative 6.8 – 8.0 pIC50 11,57
pIC50 6.8 – 8.0 (IC50 1.58x10-7 – 1x10-8 M) [11,57]
A-850002 Rn Negative 7.4 pIC50 123
pIC50 7.4 (IC50 4.09x10-8 M) [123]
A-850002 Hs Negative 7.4 pIC50 121
pIC50 7.4 (IC50 4.3x10-8 M) [121]
CFMMC Hs Negative 7.3 pIC50 31
pIC50 7.3 (IC50 5x10-8 M) [31]
cis-10 [PMID: 15771457] Hs Negative 7.0 pIC50 68
pIC50 7.0 (IC50 9.4x10-8 M) [68]
VU0469650 Hs Negative 7.0 pIC50 65
pIC50 7.0 (IC50 9.9x10-8 M) [65]
YM298198 Hs Negative 6.9 pIC50 31
pIC50 6.9 (IC50 1.2x10-7 M) [31]
LY456236 Hs Negative 6.9 pIC50 63
pIC50 6.9 (IC50 1.4x10-7 M) [63]
EM-TBPC Rn Negative 6.9 pIC50 70
pIC50 6.9 (IC50 1.28x10-7 M) [70]
compound 22 [PMID: 17276684] Rn Negative 6.8 pIC50 20
pIC50 6.8 (IC50 1.67x10-7 M) [20]
CPCCOEt Hs Negative 5.2 – 5.8 pIC50 64
pIC50 5.2 – 5.8 (IC50 6.3x10-6 – 1.5x10-6 M) [64]
PHCCC Hs Positive - -
View species-specific allosteric modulator tables
Allosteric Modulator Comments
Values for Ro67-4853 and Ro67-7476 were determined by binding studies using [3H]R214127 binding [57] or from functional studies [11,51,64]. Among these allosteric regulators only NPS2390 is not mGlu1 selective, being also active as a negative allosteric modulator of mGlu5. Among the positive modulators, only Ro67-4853 is active on the human receptor [51]. The binding site of all allosteric regulators have been mapped within the 7 transmembrane domain of the receptor [11,51,64,70].
Primary Transduction Mechanisms
Transducer Effector/Response
Gq/G11 family Phospholipase C stimulation
Comments:  The primary action of the mGlu1 is to activate PLC through stimulating Gq/11, resulting in the PIP2 breakdown which can be monitored as the production of inositol phosphate. The PIP2 breakdown causes the increases in the intracellular calcium concentration and the activation of the TRPC channels [38]. The primary transduction is observed both in cell lines and the native tissue expressing the mGlu1.
References:  3,16,24,87
Secondary Transduction Mechanisms
Transducer Effector/Response
Gs family
Gi/Go family
G protein independent mechanism
Adenylate cyclase stimulation
Adenylate cyclase inhibition
Phospholipase A2 stimulation
Phospholipase D stimulation
Other - See Comments
Comments:  Stimulation of adenylyl cyclase via mGlu1 has been reported in transfected cell lines [24] and suggested in neuronal cells [103]. Activation of the mGlu1 triggers the PTX-sensitive Gi/o signaling pathway in transfected cell lines, but its physiological role is unclear. The mGlu1 also induces the phospohrylation of the ERK in the G protein dependent and independent manner. In the latter case, the effects are mediated via beta-arrestin and dependent on the type of the ligands [22]. Activation of PLD has been reported in a cell line and native tissues [24,95]. The mGlu1 has been reported to activate the TRPC1 channels indepedently of G protein [49].
References:  3,16,24,87
Tissue Distribution
Testes.
Species:  Human
Technique:  immunocytochemistry.
References:  102
Peripheral unmyelinated sensory afferent terminals.
Species:  Mouse
Technique:  Immunoelectron microscopy.
References:  8
Thymus, thymocytes, TC-1s thymic epithelial cell line.
Species:  Mouse
Technique:  RT-PCR.
References:  101
Olfactory bulb, stratum oriens of CA1 and polymorph layer of dentate gyrus in hippocampus, globus pallidus, thalamus, substantia nigra, superior colliculus, cerebellum > neocortex, striatum, amygdala, hypothalamus, medulla.
Species:  Rat
Technique:  Immunohistochemistry.
References:  73
GABAergic neurons of the cerebellar cortex, somatostatin/GABA-immunopositive cells in the neocortex and hippocampus.
Species:  Rat
Technique:  Immunohistochemistry.
References:  5
Olfactory bulb, CA3 region of the hippocampus, dentate gyrus, globus pallidus, thalamic nuclei, medial geniculate nucleus, mammillary bodies, Darkshevich's nucleus, deep cerebellar nuclei, lateral vestibular nucleus, facial nucleus, spinal motor nucleus of the trigeminal nerve.
Species:  Rat
Technique:  in situ hybridisation.
References:  26
Olfactory bulb, thalamic nuclei (anterodorsal, anteroventral, ventrolateral posterior, medial geniculate, nucleus gelatinosum) > lateral hypothalamus, island of Calleja, mammillary bodies, nucleus of Darkshevich, brainstem, cranial nuclei, ventral horn of the spinal cord.
Species:  Rat
Technique:  Immunohistochemistry.
References:  26
mGlu1(a): cerebellum, diencephalon, mesencephalon, olfactory bulb, brainstem.
mGlu1(b): cerebral cortex, septum, striatum.
Species:  Rat
Technique:  PCR.
References:  37
In the hippocampus, mGlu1(a) is located in non-principal neurones in all areas, including the oriens-alveus border of the CA1 field, whereas mGlu1(b) is expressed in principal cells of the CA3 field and dentate granule cells, but absent in the CA1 region.
Species:  Rat
Technique:  Immunohistochemistry.
References:  23
Purkinje cell bodies and dendrites, golgi neurones of the granular cell layer, hippocampus (interneurons of the striatum oriens and dentate hilar region).
Species:  Rat
Technique:  immunocytochemistry.
References:  37
mGlu1(b): magnocellular neurons of the neuroendocrine supraoptic, paraventricular and circuate nuclei, neuronal cell bodies of the retrochiasmatic, anterior commissural and paraventricular nuclei.
Species:  Rat
Technique:  immunocytochemistry.
References:  77
mGlu1(b) and mGlu1(c): Hippocampus: CA3 region > granule cells.
Absent in CA1 region.
Species:  Rat
Technique:  Immunohistochemistry.
References:  66
mGlu1(a): heart: nerve terminals, ganglion cells and elements of the conducting system.
Species:  Rat
Technique:  immunocytochemistry.
References:  34
Subpopulation of basal keratinocytes.
Species:  Rat
Technique:  immunocytochemistry.
References:  33
mGlu1(a) and mGlu1(b): circumvallate papillae (taste buds).
Species:  Rat
Technique:  RT-PCR, in situ hybridisation, immunocytochemistry.
References:  112
Testes.
Species:  Rat
Technique:  RT-PCR.
References:  102
When examined at the electron microscopic level in the cerebellar cortex, mGlu(1b) was found at the same perisynaptic location as mGlu(1a).
Species:  Rat
Technique:  immunocytochemistry.
References:  78
Cerebellum, mitral and tufted cells of the olfactory bulb, hippocampus, lateral septum, thalamus, globus pallidus, entopendenuclear nucleus, ventral pallidum, magnocellular preoptic nucleus, substantia nigra, dorsal cochlear nucleus > dentate gyrus, striatum, islands of Calleja, superficial layers of the retrospinal, cingulate and entorhinal cortices, mammillary nuclei, red nucleus, superior colliculus.
Species:  Rat
Technique:  in situ hybridization.
References:  97
Cerebellar cortex.
Species:  Rat
Technique:  immunocytochemistry.
References:  44
Neostriatum, neocortex, hippocampus.
Species:  Rat
Technique:  in situ hybridization.
References:  48
Unipolar brush cells of cerebellum and cochlear nuclear complex.
Species:  Rat
Technique:  immunocytochemistry.
References:  46
Striatal neurons.
Species:  Rat
Technique:  Immunohistochemistry.
References:  106
Cerebellum, thalamus, dentate gyrus, medial central gray > CA3 region of the hippocampus and hypothalamus > basal ganglia, cortex.
Species:  Rat
Technique:  Radioligand binding.
References:  59
Retina.
Species:  Rat
Technique:  in situ hybridisation.
References:  39
Hippocampal dentate gyrus and CA2-3, cerebellar Purkinje cells.
Species:  Rat
Technique:  in situ hybridization.
References:  76
At the subcellular level, mGlu1 proteins were found in post-synaptic elements on the side of the post-synaptic density. Although some reports have suggested the presence of mGlu1 in pre-synaptic elements, this issue remains at present unresolved.
Species:  Rat
Technique:  immunocytochemistry.
References:  26,66-67
Expression Datasets

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Log average relative transcript abundance in mouse tissues measured by qPCR from Regard, J.B., Sato, I.T., and Coughlin, S.R. (2008). Anatomical profiling of G protein-coupled receptor expression. Cell, 135(3): 561-71. [PMID:18984166] [Raw data: website]

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Functional Assays
Measurement of Ca2+ levels in CHO cells transfected with the rat mGlu1 receptor.
Species:  Rat
Tissue:  CHO cells.
Response measured:  Ca2+ mobilisation.
References:  61
Measurement of IP levels in rat cerebellar granule cells expressing the native mGlu1 receptor.
Species:  Rat
Tissue:  Primary cultures of cerebellar granule cells.
Response measured:  IP accumulation.
References:  60
Measurement of intracellular Ca2+ levels and K+ conductance in rat dopamine neurons.
Species:  Rat
Tissue:  Dopamine neurons of the ventral tegmental area.
Response measured:  Mobilisation of Ca2+ and subsequent increase in K+ conductance.
References:  25
Measurement of IP levels in CHO cells transfected with the rat mGlu1.
Species:  Rat
Tissue:  CHO cells.
Response measured:  IP formation.
References:  96
Measurement of IP and Ca2+ levels in L929sA cells transfected with the human mGlu1 receptor.
Species:  Human
Tissue:  L929sA cells.
Response measured:  IP accumulation and Ca2+ mobilisation.
References:  58
mGlu1 induced current and intracellular Ca2+ levels
Species:  Mouse
Tissue:  Cultured cerebellar Purkinje neurons
Response measured:  mGlu1 induced current and Ca2+ mobilization
References:  105
Voltage-sensitivity of the mGlu1
Species:  Rat
Tissue:  Oocyte
Response measured:  Calcium induced Cl- current
References:  84
Measurement of IP levels
Species:  Rat
Tissue:  HEK 293 cells
Response measured:  IP accumulation
References:  74
Measurement of IP, cAMP and arachidonic acid levels in CHO cells transfected with the rat mGlu1 receptor.
Species:  Rat
Tissue:  CHO cells.
Response measured:  IP, cAMP, arachidonic acid formation and calcium mobilisation
References:  4,61,96
Physiological Functions
Slow excitatory effect as well as inhibitory effects, depending on the channel activated or inhibited.
Species:  Rat
Tissue:  Dopamine neurons of the ventral tegmental area.
References:  25
mGlu1 at the periphery is involved in the sensation of inflamatory pain.
Species:  Mouse
Tissue:  Skin.
References:  8
Long-term depression (LTD).
Species:  Rat
Tissue:  Purkinje cells.
References:  96
Motor coordination, spacial learning, cerebellar long-term depression (LTD) and hippocampal mossy fibre long-term potentiation (LTP).
Species:  Mouse
Tissue:  In vivo.
References:  17
Long-term depression (LTD).
Species:  Mouse
Tissue:  In vivo.
References:  2
Excitatory synaptic transmission, long-term depression, short-term potentiation.
Species:  Mouse
Tissue:  Hippocampal slices.
References:  1
Normal synapse formation, synaptic plasticity and motor control.
Species:  Mouse
Tissue:  In vivo.
References:  45
Physiological Consequences of Altering Gene Expression
Cerebellar ataxia.
Species:  Mouse
Tissue: 
Technique:  Gene targeting in embryonic stem cells.
References:  2,17,45
Persistent multiple climbing fiber innervation of cerebellar Purkinje cells.
Species:  Mouse