Gene and Protein Information
class C G protein-coupled receptor
Species	TM	AA	Chromosomal Location	Gene Symbol	Gene Name	Reference
Human	7	1194	6q24.3	GRM1	glutamate metabotropic receptor 1	20,33,101
Mouse	7	1199	10 A1	Grm1	glutamate receptor, metabotropic 1	125
Rat	7	1199	1p13	Grm1	glutamate metabotropic receptor 1	44,77

Previous and Unofficial Names

GPRC1A | metabotropic glutamate receptor 1 | wobl | MGLUR1 | SCAR13 | glutamate receptor, metabotropic 1 | glutamate receptor

Database Links
Specialist databases
GPCRdb	grm1_human (Hs), grm1_mouse (Mm), grm1_rat (Rn)
Other databases
Alphafold	Q13255 (Hs), P97772 (Mm), P23385 (Rn)
ChEMBL Target	CHEMBL3772 (Hs), CHEMBL2892 (Mm), CHEMBL4477 (Rn)
Ensembl Gene	ENSG00000152822 (Hs), ENSMUSG00000019828 (Mm), ENSRNOG00000068415 (Rn), ENSRNOG00000014290 (Rn)
Entrez Gene	2911 (Hs), 14816 (Mm), 24414 (Rn)
Human Protein Atlas	ENSG00000152822 (Hs)
KEGG Gene	hsa:2911 (Hs), mmu:14816 (Mm), rno:24414 (Rn)
OMIM	604473 (Hs)
Orphanet	ORPHA327283 (Hs)
Pharos	Q13255 (Hs)
RefSeq Nucleotide	NM_001278067 (Hs), NM_001278066 (Hs), NM_001278064 (Hs), NM_001278065 (Hs), NM_016976 (Mm), NM_001114333 (Mm), NM_017011 (Rn), NM_001114330 (Rn)
RefSeq Protein	NP_001264995 (Hs), NP_001264994 (Hs), NP_001264996 (Hs), NP_001264993 (Hs), NP_001107805 (Mm), NP_058672 (Mm), NP_001107802 (Rn), NP_058707 (Rn)
UniProtKB	Q13255 (Hs), P97772 (Mm), P23385 (Rn)
Wikipedia	GRM1 (Hs)

Selected 3D Structures
	Description:  Crystal structure of metabotropic glutamate receptor subtype 1 complexed with glutamate PDB Id:  1EWK Resolution:  2.2Å Species:  Rat References:  57
	Description:  Crystal structure of metabotropic glutamate receptor subtype 1 ligand free form II PDB Id:  1EWV Resolution:  4.0Å Species:  Rat References:  57
	Description:  Crystal Structure of Metabotropic Glutamate Receptor Subtype 1 Complexed with Glutamate and Gadolinium Ion PDB Id:  1ISR Resolution:  4.0Å Species:  Rat References:  114
	Description:  Crystal Structure of Metabotropic Glutamate Receptor Subtype 1 Complexed with an antagonist PDB Id:  1ISS Resolution:  3.3Å Species:  Rat References:  114
	Description:  Crystal structure of metabotropic glutamate receptor subtype 1 ligand free form 1 PDB Id:  1EWT Resolution:  3.7Å Species:  Rat References:  57
	Description:  Metabotropic glutamate receptor mGluR1 complexed with LY341495 antagonist PDB Id:  3KS9 Ligand:  LY341495 Resolution:  1.9Å Species:  Human References:
	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:  119

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 Value Parameter Reference [3H]quisqualate Rn Full agonist 7.5 – 7.7 pKd 59,71 ⤷ pKd 7.5 – 7.7 [59,71] quisqualate Rn Full agonist 7.5 – 8.0 pKi 59,83 ⤷ pKi 7.5 – 8.0 [59,83] L-glutamic acid Rn Full agonist 6.4 – 6.5 pKi 59,83 ⤷ pKi 6.4 – 6.5 [59,83] ibotenic acid Rn Full agonist 5.9 – 6.4 pKi 83,112 ⤷ pKi 5.9 – 6.4 [83,112] (1S,3R)-ACPD Rn Full agonist 5.5 – 6.1 pKi 59,83,112 ⤷ pKi 5.5 – 6.1 [59,83,112] 3,5-DHPG Rn Full agonist 5.8 pKi 59 ⤷ pKi 5.8 [59] L-CCG-I Rn Full agonist 5.6 pKi 83 ⤷ pKi 5.6 [83] L-glutamic acid Hs Agonist 4.8 – 5.0 pEC50 87 ⤷ pEC50 4.8 – 5.0 [87] (S)-3HPG Rn Partial agonist 4.9 pIC50 83 ⤷ pIC50 4.9 [83]
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 [95]. 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 [57,114]. 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 [84,93]. Cations such as Ca2+ have been proposed to directly activate mGlu1 receptors [28,56,109]. 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 Value Parameter Reference AIDA Hs Antagonist 4.2 pA2 82 ⤷ pA2 4.2 [82] [11C]JNJ-16567083 Rn Antagonist 9.1 pKi 45 ⤷ pKi 9.1 (Ki 8.7x10-10 M) [45] LY341495 Hs Antagonist 7.8 pKi 52 ⤷ pKi 7.8 [52] (S)-4C3HPG Hs Antagonist 5.8 – 6.0 pKi 59,83 ⤷ pKi 5.8 – 6.0 [59,83] LY367385 Rn Antagonist 5.9 pKi 59 ⤷ pKi 5.9 (Ki 1.26x10-6 M) [59] (S)-4CPG Rn Antagonist 5.4 pKi 59 ⤷ pKi 5.4 [59] DCG-IV Rn Antagonist 4.1 pKi 83 ⤷ pKi 4.1 [83] AIDA Rn Antagonist 4.0 pKi 59 ⤷ pKi 4.0 [59] (+)-MCPG Rn Antagonist 3.8 pKi 59 ⤷ pKi 3.8 [59] 3-MATIDA Rn Antagonist 5.2 pIC50 81 ⤷ pIC50 5.2 (IC50 6.3x10-6 M) [81] LY367385 Hs Antagonist 5.1 pIC50 15 ⤷ pIC50 5.1 (IC50 8.8x10-6 M) [15] (S)-TBPG Rn Antagonist 4.2 pIC50 19 ⤷ pIC50 4.2 (IC50 6.89x10-5 M) [19] (S)-(+)-CBPG Rn Antagonist 4.2 pIC50 72 ⤷ pIC50 4.2 (IC50 6.7x10-5 M) [72]
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 [95]. 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 [95]).

Allosteric Modulators
Key to terms and symbols	View all chemical structures	Click column headers to sort
Ligand Sp. Action Value Parameter Reference VU0483605 N/A Positive 6.0 pKB 41 ⤷ pKB 6.0 [41] [3H]R214127 Hs Negative 9.0 pKd 59 ⤷ pKd 9.0 [59] [3H]EM-TBPC Rn Positive 8.2 pKd 71 ⤷ pKd 8.2 [71] [3H]YM298198 Rn Negative 7.5 pKd 55 ⤷ pKd 7.5 (Kd 3.2x10-8 M) [55] 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 120 ⤷ pKi 9.4 (Ki 4x10-10 M) [120] [11C]MMTP Rn Negative 9.2 pKi 90 ⤷ pKi 9.2 (Ki 6x10-10 M) [90] [18F]FITM Rn Negative 9.1 pKi 121 ⤷ pKi 9.1 (Ki 8.7x10-10 M) [121] compound 11c [PMID: 17929793] Rn Negative 9.0 pKi 120 ⤷ pKi 9.0 (Ki 1x10-9 M) [120] NPS2390 Rn Negative 8.9 pKi 59 ⤷ pKi 8.9 [59] R214127 Rn Negative 8.9 pKi 59 ⤷ pKi 8.9 [59] JNJ-16567083 Rn Negative 8.9 pKi 45 ⤷ pKi 8.9 (Ki 1.4x10-9 M) [45] compound 23h [PMID: 17929793] Rn Negative 8.8 pKi 120 ⤷ pKi 8.8 (Ki 1.5x10-9 M) [120] compound 23e [PMID: 17929793] Rn Negative 8.8 pKi 120 ⤷ pKi 8.8 (Ki 1.5x10-9 M) [120] compound 11q [PMID: 19433355] Rn Negative 8.5 pKi 92 ⤷ pKi 8.5 (Ki 3.5x10-9 M) [92] 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 21 ⤷ pKi 8.4 (Ki 3.6x10-9 M) [21] compound 11s [PMID: 19433355] Rn Negative 8.3 pKi 92 ⤷ pKi 8.3 (Ki 4.7x10-9 M) [92] 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 124 ⤷ pKi 8.3 (Ki 5.4x10-9 M) [124] FITM Rn Negative 8.3 pKi 31 ⤷ pKi 8.3 (Ki 5.4x10-9 M) [31] Description: Measured using rat brain homogenate in a competition binding assay displacing [18F}-FITM. compound 27 [PMID: 20346665] Rn Negative 8.1 pKi 91 ⤷ pKi 8.1 (Ki 7.9x10-9 M) [91] compound 29 [PMID: 17064898] Rn Negative 8.0 pKi 86 ⤷ pKi 8.0 (Ki 9.3x10-9 M) [86] FPTQ Rn Negative 7.9 pKi 30 ⤷ pKi 7.9 (Ki 1.26x10-8 M) [30] EM-TBPC Rn Negative 7.8 pKi 71 ⤷ pKi 7.8 (Ki 1.7x10-8 M) [71] Ro67-7476 Rn Positive 7.5 – 7.9 pKi 53 ⤷ pKi 7.5 – 7.9 (Ki 3.16x10-8 – 1.26x10-8 M) [53] YM-202074 Rn Negative 7.7 pKi 54 ⤷ pKi 7.7 (Ki 2x10-8 M) [54] Ro01-6128 Rn Positive 7.5 – 7.7 pKi 53 ⤷ pKi 7.5 – 7.7 (Ki 3.16x10-8 – 1.99x10-8 M) [53] compound 24 [PMID: 20346665] Hs Negative 6.9 pKi 91 ⤷ pKi 6.9 (Ki 1.15x10-7 M) [91] compound 24 [PMID: 20346665] Rn Negative 6.9 pKi 91 ⤷ pKi 6.9 (Ki 1.15x10-7 M) [91] compound 2f [PMID: 17532216] Hs Negative 6.9 pKi 118 ⤷ pKi 6.9 (Ki 1.27x10-7 M) [118] LY456066 Rn Negative 6.8 pKi 32 ⤷ pKi 6.8 (Ki 1.43x10-7 M) [32] CPCCOEt Rn Negative 5.3 pKi 59 ⤷ pKi 5.3 [59] Ro67-4853 Rn Positive 5.1 pKi 53 ⤷ pKi 5.1 (Ki 7.94x10-6 M) [53] Ro0711401 Rn Positive 7.3 pEC50 117 ⤷ pEC50 7.3 (EC50 5.6x10-8 M) [117] compound 3a [PMID: 16099654] Rn Positive 7.2 pEC50 116 ⤷ pEC50 7.2 (EC50 6.5x10-8 M) [116] compound 4b [PMID: 16099654] Rn Positive 7.2 pEC50 116 ⤷ pEC50 7.2 (EC50 6.5x10-8 M) [116] VU0483605 Hs Positive 6.4 pEC50 13 ⤷ pEC50 6.4 (EC50 3.9x10-7 M) [13] VU-71 Rn Positive 5.6 pEC50 116 ⤷ pEC50 5.6 (EC50 2.4x10-6 M) [116] CPCCOEt Rn Negative 5.3 pEC50 60 ⤷ pEC50 5.3 (EC50 5x10-6 M) [60] compound 11q [PMID: 19433355] Hs Negative 9.1 pIC50 92 ⤷ pIC50 9.1 (IC50 9x10-10 M) [92] A-841720 Rn Negative 9.0 – 9.0 pIC50 123-124 ⤷ pIC50 9.0 – 9.0 (IC50 1.05x10-9 – 1x10-9 M) [123-124] JNJ16259685 Hs Negative 8.9 pIC50 63 ⤷ pIC50 8.9 (IC50 1.21x10-9 M) [63] compound 23i [PMID: 17929793] Hs Negative 8.9 pIC50 120 ⤷ pIC50 8.9 (IC50 1.4x10-9 M) [120] compound 24 [PMID: 20346665] Hs Negative 8.7 pIC50 91 ⤷ pIC50 8.7 (IC50 2.1x10-9 M) [91] compound 11s [PMID: 19433355] Hs Negative 8.7 pIC50 92 ⤷ pIC50 8.7 (IC50 2.1x10-9 M) [92] compound 23h [PMID: 17929793] Hs Negative 8.7 pIC50 120 ⤷ pIC50 8.7 (IC50 2.2x10-9 M) [120] compound 23c [PMID: 17929793] Hs Negative 8.6 pIC50 120 ⤷ pIC50 8.6 (IC50 2.5x10-9 M) [120] CFMTI Hs Negative 8.6 pIC50 94 ⤷ pIC50 8.6 (IC50 2.6x10-9 M) [94] compound 23e [PMID: 17929793] Hs Negative 8.5 pIC50 120 ⤷ pIC50 8.5 (IC50 2.9x10-9 M) [120] A-794282 Hs Negative 8.5 pIC50 122 ⤷ pIC50 8.5 (IC50 3x10-9 M) [122] compound 22 [PMID: 19289283] Rn Negative 8.5 pIC50 73 ⤷ pIC50 8.5 (IC50 3x10-9 M) [73] [18F]MK-1312 Hs Negative 8.4 pIC50 43 ⤷ pIC50 8.4 (IC50 3.6x10-9 M) [43] MK-5435 Hs Negative 8.4 pIC50 43 ⤷ pIC50 8.4 (IC50 4.3x10-9 M) [43] A-794282 Rn Negative 8.3 pIC50 124 ⤷ pIC50 8.3 (IC50 4.7x10-9 M) [124] FTIDC Rn Negative 8.3 pIC50 105 ⤷ pIC50 8.3 (IC50 4.8x10-9 M) [105] compound 11c [PMID: 17929793] Hs Negative 8.3 pIC50 120 ⤷ pIC50 8.3 (IC50 4.9x10-9 M) [120] [18F]FITM Hs Negative 8.3 pIC50 121 ⤷ pIC50 8.3 (IC50 5.1x10-9 M) [121] [18F]FPIT Rn Negative 8.3 pIC50 29 ⤷ pIC50 8.3 (IC50 5.4x10-9 M) [29] FTIDC Hs Negative 8.2 pIC50 105 ⤷ pIC50 8.2 (IC50 5.8x10-9 M) [105] compound 32 [PMID: 19289283] Rn Negative 8.2 pIC50 73 ⤷ pIC50 8.2 (IC50 6x10-9 M) [73] 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 54 ⤷ pIC50 8.1 (IC50 8.6x10-9 M) [54] compound 29 [PMID: 17064898] Rn Negative 8.1 pIC50 86 ⤷ pIC50 8.1 (IC50 9x10-9 M) [86] [11C]MMTP Hs Negative 8.0 pIC50 90 ⤷ pIC50 8.0 (IC50 9.5x10-9 M) [90] A-841720 Hs Negative 8.0 pIC50 122 ⤷ pIC50 8.0 (IC50 1x10-8 M) [122] A-794278 Hs Negative 8.0 pIC50 122 ⤷ pIC50 8.0 (IC50 1x10-8 M) [122] R214127 Hs Negative 8.0 pIC50 59 ⤷ pIC50 8.0 (IC50 1.04x10-8 M) [59] 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 80 ⤷ pIC50 7.8 [80] YM298198 Rn Negative 7.8 pIC50 55 ⤷ pIC50 7.8 [55] 3,5-dimethyl PPP Rn Negative 7.8 pIC50 80 ⤷ pIC50 7.8 (IC50 1.58x10-8 M) [80] compound 3 [PMID: 12470711] Rn Negative 7.8 pIC50 80 ⤷ pIC50 7.8 (IC50 1.6x10-8 M) [80] compound 27 [PMID: 20346665] Hs Negative 7.6 pIC50 91 ⤷ pIC50 7.6 (IC50 2.7x10-8 M) [91] LY456066 Hs Negative 7.6 pIC50 32 ⤷ pIC50 7.6 (IC50 2.8x10-8 M) [32] BAY 367620 Rn Negative 6.8 – 8.0 pIC50 11,59 ⤷ pIC50 6.8 – 8.0 (IC50 1.58x10-7 – 1x10-8 M) [11,59] A-850002 Rn Negative 7.4 pIC50 124 ⤷ pIC50 7.4 (IC50 4.09x10-8 M) [124] A-850002 Hs Negative 7.4 pIC50 122 ⤷ pIC50 7.4 (IC50 4.3x10-8 M) [122] CFMMC Hs Negative 7.3 pIC50 32 ⤷ pIC50 7.3 (IC50 5x10-8 M) [32] cis-10 [PMID: 15771457] Hs Negative 7.0 pIC50 69 ⤷ pIC50 7.0 (IC50 9.4x10-8 M) [69] VU0469650 Hs Negative 7.0 pIC50 66 ⤷ pIC50 7.0 (IC50 9.9x10-8 M) [66] YM298198 Hs Negative 6.9 pIC50 32 ⤷ pIC50 6.9 (IC50 1.2x10-7 M) [32] LY456236 Hs Negative 6.9 pIC50 12 ⤷ pIC50 6.9 (IC50 1.4x10-7 M) [12] EM-TBPC Rn Negative 6.9 pIC50 71 ⤷ pIC50 6.9 (IC50 1.28x10-7 M) [71] compound 22 [PMID: 17276684] Rn Negative 6.8 pIC50 21 ⤷ pIC50 6.8 (IC50 1.67x10-7 M) [21] CPCCOEt Hs Negative 5.2 – 5.8 pIC50 65 ⤷ pIC50 5.2 – 5.8 (IC50 6.3x10-6 – 1.5x10-6 M) [65] 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 [59] or from functional studies [11,53,65]. 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 [53]. The binding site of all allosteric regulators have been mapped within the 7 transmembrane domain of the receptor [11,53,65,71].

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 [39]. The primary transduction is observed both in cell lines and the native tissue expressing the mGlu1.
References:  3,17,25,88

Secondary Transduction Mechanisms
Transducer	Effector/Response
Gs family Gi/Go family G protein independent mechanism	Adenylyl cyclase stimulation Adenylyl 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 [25] and suggested in neuronal cells [104]. 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 [23]. Activation of PLD has been reported in a cell line and native tissues [25,96]. The mGlu1 has been reported to activate the TRPC1 channels indepedently of G protein [51].
References:  3,17,25,88

Tissue Distribution
Testes. Species:  Human Technique:  immunocytochemistry. References:  103
Thymus, thymocytes, TC-1s thymic epithelial cell line. Species:  Mouse Technique:  RT-PCR. References:  102
Peripheral unmyelinated sensory afferent terminals. Species:  Mouse Technique:  Immunoelectron microscopy. References:  8
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:  27,67-68
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:  74
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:  27
mGlu1(a): cerebellum, diencephalon, mesencephalon, olfactory bulb, brainstem. mGlu1(b): cerebral cortex, septum, striatum. Species:  Rat Technique:  PCR. References:  38
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:  24
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:  38
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:  78
mGlu1(b) and mGlu1(c): Hippocampus: CA3 region > granule cells. Absent in CA1 region. Species:  Rat Technique:  Immunohistochemistry. References:  67
mGlu1(a): heart: nerve terminals, ganglion cells and elements of the conducting system. Species:  Rat Technique:  immunocytochemistry. References:  35
Subpopulation of basal keratinocytes. Species:  Rat Technique:  immunocytochemistry. References:  34
mGlu1(a) and mGlu1(b): circumvallate papillae (taste buds). Species:  Rat Technique:  RT-PCR, in situ hybridisation, immunocytochemistry. References:  113
Testes. Species:  Rat Technique:  RT-PCR. References:  103
Hippocampal dentate gyrus and CA2-3, cerebellar Purkinje cells. Species:  Rat Technique:  in situ hybridization. References:  77
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:  79
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:  98
Cerebellar cortex. Species:  Rat Technique:  immunocytochemistry. References: