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Alomone Labs
metabotropic glutamate receptors  Metabotropic Glutamate Receptors, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/AGC-006/Anti-mGluR1+(extracellular)+Antibody/pmc03181343-253-14-24 Average 93 stars, based on 1 article reviews
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Alomone Labs
mglur1  Mglur1, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more https://www.bioz.com/product/AGC-006/Anti-mGluR1+(extracellular)+Antibody+-+Carrier+Free/10__1523_slash_jneurosci__3542___13__2014-78-25-55 Average 93 stars, based on 1 article reviews
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Journal: PLoS ONE
Article Title: Dopamine-Induced Plasticity, Phospholipase D (PLD) Activity and Cocaine-Cue Behavior Depend on PLD-Linked Metabotropic Glutamate Receptors in Amygdala
doi: 10.1371/journal.pone.0025639
Figure Lengend Snippet: Responses are plotted as percent change from the baseline fEPSPs as a function of time. Numbers on the representative traces show the time on the graph at which they were recorded. A) SKF81297-induced LTP in the cocaine CPP group (clear triangles, 151.4±8.8%, * p <0.05, n = 6) is completely blocked by the PLD-linked mGluR antagonist (PCCG-13, filled triangles, 95.0±9.2%, n = 6). B) mGluR1 receptor antagonist (LY367385, filled triangles, 106.0±6.7%, n = 6) blocks the SKF81297-induced LTP (clear triangles, * p <0.05, n = 6). C) The mGluR5 antagonist (MPEP, filled triangles, 122.7±5.6%, n = 6) significantly reduces but does not abolish the SKF81297-induced LTP (clear triangles, * p <0.05, n = 6). D) PLC antagonist (U-73122, filled triangles, 128.2±6.1%, n = 6), reduces but does not eliminate the SKF81297-induced LTP (clear triangles, * p <0.05, n = 6). For comparison, panels A and B use same data graphs and fEPSP traces for the slices from cocaine CPP group superfused with SKF81297 as shown in , and .
Article Snippet: Primary antibodies (with the references provided where the antibodies were tested for specificity) included:
Techniques: Comparison
Journal: PLoS ONE
Article Title: Dopamine-Induced Plasticity, Phospholipase D (PLD) Activity and Cocaine-Cue Behavior Depend on PLD-Linked Metabotropic Glutamate Receptors in Amygdala
doi: 10.1371/journal.pone.0025639
Figure Lengend Snippet: The dotted line indicates PLD activity associated with control slices (no EtOH added) which was determined for each animal and used to calculate the change in PLD activity levels with EtOH and/or drug application. Basal levels represent the increase in PLD activity observed in the EtOH-treated slices compared to the no EtOH controls; * p <0.05 compared to the corresponding saline control and # p <0.05 compared to the cocaine CPP group basal PLD activity. Basal PLD activity was significantly increased (*** p <0.001, n = 50) in the cocaine CPP group (dark bars, 527.3±94.3) compared to the saline-treated group (white bars, 142.6±36.9). SKF81297, the D1/5R agonist, application increased the basal levels in the cocaine CPP group significantly (1722.0±176.9, n = 12, # p <0.05) compared to the basal PLD activity observed with EtOH treatment alone in the same experimental group. The D1/5R antagonist, SCH23390, completely blocked basal PLD activity (91.2±21.9, n = 12, ## p <0.01) in the cocaine CPP group. A similar reduction in PEtOH levels was observed with application of either the PLD-linked mGluR antagonist, PCCG-13 (62.9±10.6, n = 7, ## p <0.01) or the mGluR1 antagonist, LY367385 (75.0±13.9, n = 12, ## p <0.01), while the mGluR5 antagonist, MPEP, did not decrease basal PLD activity (305.7±31.5, n = 7, ns) within the cocaine CPP group but were significantly increased compared to (* p <0.05) the saline treated group. Applications of SKF81297 (184.9±30.5, n = 12), SCH23390 (84.9±38.9, n = 12), MPEP (74.2±16.3, n = 7), LY367385 (94.7±18.9, n = 12) and PCCG-13 (132.5±18.4, n = 7) did not significantly alter the PEtOH levels in the saline-treated group compared to the basal activity levels. Inset is a depiction of the triangular excision performed to isolate amygdala (bilaterally for each animal, each slice) containing the basolateral (BLA), the central (CeA) and the lateral (LA) subregions from three serial coronal slices (350 µm) beginning −2.30 mm to −2.80 mm from Bregma .
Article Snippet: Primary antibodies (with the references provided where the antibodies were tested for specificity) included:
Techniques: Activity Assay, Control, Saline
Journal: Journal of Neuroscience
Article Title: The Synaptic Targeting of mGluR1 by Its Carboxyl-Terminal Domain Is Crucial for Cerebellar Function
doi: 10.1523/jneurosci.3542-13.2014
Figure Lengend Snippet: Figure 1. Generation of mGluR1b-rescue mice. A, Strategy for generation of mGluR1a- rescue and mGluR1b-rescue mice. mGluR1a possesses a large intracellular C-terminal region consistingof359aminoacidsfollowingaseven-transmembranedomain.InmGluR1b,thelast 312 amino acids of mGluR1a (red) are replaced by 20 amino acids (blue). mGluR1a-rescue (Ichiseetal.,2000)andmGluR1b-rescuemiceweregeneratedbyintroductionofmGluR1trans- genes under the control of a PC-specific L7 promoter into the mGluR1-KO mice. B, Schematic structure of the transgene constructs. Rat mGluR1b (1) cDNA was inserted into the L7 pro- moter vector. Open white boxes represent exons of the L7 gene (E1–E4). The first 886 amino acid residues in mGluR1b containing extracellular domain (Ex) and seven-transmembrane do- main(7TM)areidenticaltothoseofmGluR1a,althoughinmGluR1bthelast313aminoacidsof mGluR1a (red box) are replaced by 20 amino acids (blue box). The L7-mGluR1b transgene is flankedbyaninsulatorsequence(yellowbox)fromchicken-globingenetoavoidtheposition effect. C, In situ hybridization analysis of the mGluR1 mRNAs in the brain of WT, mGluR1-KO (KO),mGluR1a-rescue(1arescue),andmGluR1b-rescue(1brescue)mice.Parasagittalsections were hybridized with 33P-labeled oligonucleotide probes, which recognize mGluR1a and/or mGluR1b mRNAs. Cb, Cerebellum; Cx, cerebral cortex; Hi, hippocampus; Mb, midbrain; MO, medullaoblongata;OB,olfactorybulb;Th,thalamus.Scalebars,1mm.D,Immunohistochem- ical analysis for mGluR1 proteins. Parasagittal sections from WT (top), mGluR1a-rescue (mid- dle),andmGluR1b-rescuemice(bottom)stainedwithhematoxylin,antibodytomGluR1a,and antibody to mGluR1b. Scale bars, 1 mm.
Article Snippet: Subsequently, the Sepharose was washed three times with 1 ml of lysis buffer, and bound proteins were immunoblotted using antibodies against the extracellular domain of
Techniques: Control, Construct, Plasmid Preparation, In Situ Hybridization, Labeling
Journal: Journal of Neuroscience
Article Title: The Synaptic Targeting of mGluR1 by Its Carboxyl-Terminal Domain Is Crucial for Cerebellar Function
doi: 10.1523/jneurosci.3542-13.2014
Figure Lengend Snippet: Figure 3. Subcellular localizations of mGluR1 are disturbed in PC dendrites of mGluR1b- rescuemice.A,Left,Postembeddingimmunogoldelectronmicrographsshowinglocalizationof mGluR1ainPCspinesinWTandmGluR1a-rescue(1arescue)mice.mGluR1alabelingwaspreferential forperisynapticregionsofPCspines(Sp)contactingPFterminalsinbothmice.Right,Electronmicro- graphs showing immunogold localization of mGluR1b in PC spines in WT and mGluR1b-rescue (1b rescue)mice.mGluR1blabelingwasoftenobservedinintracellular(cytoplasmic)compartments(ar- row)inmGluR1b-rescuemice.Scalebars,100nm.B,Percentageofimmunogoldparticlesshowing plasma membrane-associated labeling for mGluR1a in PC spines of WT and mGluR1a-rescue (1a rescue)andformGluR1binspinesofWTandmGluR1b-rescue(1brescue)mice.Immunogoldparticles were defined to be plasma membrane-associated when the distance from the center of the gold particle to the cell membrane was 35 nm. C, Histograms showing tangential distribution of cell membrane-associatedimmunogoldparticlesformGluR1aonPCspinesofWTandmGluR1a-rescue (1a rescue) and for mGluR1b on PC spines of WT and mGluR1b-rescue (1b rescue) mice. Bold bars representboundariesofthePSD.
Article Snippet: Subsequently, the Sepharose was washed three times with 1 ml of lysis buffer, and bound proteins were immunoblotted using antibodies against the extracellular domain of
Techniques: Clinical Proteomics, Membrane, Labeling
Journal: Journal of Neuroscience
Article Title: The Synaptic Targeting of mGluR1 by Its Carboxyl-Terminal Domain Is Crucial for Cerebellar Function
doi: 10.1523/jneurosci.3542-13.2014
Figure Lengend Snippet: Figure2. mGluR1-signalingproteincomplexesfrommGluR1a-rescueandmGluR1b-rescue cerebella. A, Expression levels of mGluR1 proteins in the cerebella of WT, mGluR1-KO (KO), mGluR1a-rescue (1a rescue), and mGluR1b-rescue (1b rescue) mice. Synaptosomal fractions werepreparedfrommousecerebellaatP15andinadulthoodandwereimmunoblottedwithan antibody specific to the extracellular domain of mGluR1 proteins. Arrowheads indicate bands for mGluR1a (1a) and mGluR1b (1b). B, Composition of mGluR1-signaling protein complex. Synaptosomalfractionfromthecerebellumofeachgenotypewasincubatedwithratmonoclo- nalantibodyagainsttheextracellulardomainofmGluR1orratIgG.Subsequently,theinput(in) and the proteins bound to mGluR1 antibody (mG) and IgG (Ig) were immunoblotted using antibodies against the N-terminal domain of mGluR1, Homer, GluR2, GABABR2, and Cav2.1.
Article Snippet: Subsequently, the Sepharose was washed three times with 1 ml of lysis buffer, and bound proteins were immunoblotted using antibodies against the extracellular domain of
Techniques: Expressing
Journal: Journal of Neuroscience
Article Title: The Synaptic Targeting of mGluR1 by Its Carboxyl-Terminal Domain Is Crucial for Cerebellar Function
doi: 10.1523/jneurosci.3542-13.2014
Figure Lengend Snippet: Figure 4. Regression of multiple climbing fiber innervation is impaired in PCs of mGluR1b- rescue mice. Summary graphs show frequency distributions of PCs in terms of the number of discretestepsofCF-EPSCsfromWTmice(A,n58from4mice),mGluR1-KOmice(B,KO;n 63from5mice),mGluR1a-rescuemice(C,1arescue;n71from5mice),andmGluR1b-rescue mice (D, 1b rescue; n 96 from 7 mice). Insets, Sample traces of CF-EPSCs from PCs.
Article Snippet: Subsequently, the Sepharose was washed three times with 1 ml of lysis buffer, and bound proteins were immunoblotted using antibodies against the extracellular domain of
Techniques:
Journal: Journal of Neuroscience
Article Title: The Synaptic Targeting of mGluR1 by Its Carboxyl-Terminal Domain Is Crucial for Cerebellar Function
doi: 10.1523/jneurosci.3542-13.2014
Figure Lengend Snippet: Figure5. mGluR1-mediatedCa 2mobilizationandLTDareimpairedinmGluR1b-rescuemice.A,DHPG-evokedCa 2mobi- lization in PCs dissociated from mGluR1a-rescue (n 16) and mGluR1b-rescue (n 12) mice. Traces and error bars indicate mean SEM. B, The sustained level (level at 45 s) of DHPG-evoked calcium transient was reduced in mGluR1b-rescue PCs. C, Representative traces of Ca 2 transient elicited by repetitive PF train of 5 stimuli (left and middle columns) or 20 stimuli (right column) at 100 Hz in mGluR1a-rescue and mGluR1b-rescue mice. ESCT was blocked in the presence of NBQX (5 M, middle and right columns). D, Summary graph for the dependence of Ca 2 signals on the number of stimuli. Peak amplitudes of DSCTs recordedinthepresenceofNBQXwerenormalizedbythoseofESCTsevokedby5stimuliat100Hz.Thenumberofcellsforeachdata point is 5–13. *p 0.05 (t test). E–J, Conjunctive PF and CF stimulation (conj) did not induce LTD of PF-EPSP initial slopes in mGluR1b-rescuemice(H,n12),whereasLTDwassuccessfullyinducedinmGluR1a-rescuemice(E,n12).TestPFstimulation was applied at 0.2 Hz. E, H, Time course of averaged PF-EPSP initial slopes in mGluR1a-rescue (E) and mGluR1b-rescue mice (H). Data from each PC were normalized to the mean value of initial slope during the control period for 10 min. F, I, Sample traces of PF-EPSPsbeforeand30minaftertheconjunctivestimulation.EachtraceistheaverageoffiveconsecutiveresponsesinmGluR1a- rescue (F) and mGluR1b-rescue mice (I). G, J, Sample traces of CF-EPSPs in mGluR1a- rescue (G) and mGluR1b-rescue mice (J).
Article Snippet: Subsequently, the Sepharose was washed three times with 1 ml of lysis buffer, and bound proteins were immunoblotted using antibodies against the extracellular domain of
Techniques: Control
Journal: Journal of Neuroscience
Article Title: The Synaptic Targeting of mGluR1 by Its Carboxyl-Terminal Domain Is Crucial for Cerebellar Function
doi: 10.1523/jneurosci.3542-13.2014
Figure Lengend Snippet: Figure6. mGluR1-mediatedslowEPSCsarenormallyevokedinmGluR1b-rescuemice.A,PFevokedfastEPSCsinmGluR1a-and mGluR1b-rescue mice. Paired PF evoked fast EPSCs (black line, interval of 50 ms) in an mGluR1a- (left) and an mGluR1b- (right) rescuemousebeforeinductionofmGluR1-mediatedslowEPSCs.PF-evokedfastEPSCswereblockedinbothkindsofmiceby50M CNQX(grayline).B,mGluR1-mediatedslowEPSCs(arrowhead)evokedbyrepetitivePFstimulation(400A,10pulses)at200Hz inmGluR1a-rescue(left)andmGluR1b-rescue(right)mice.Insets,Completetraces.C,BathapplicationofanmGluR1antagonist, CPCCOEt (100 M), abolished the mGluR1-mediated slow EPSCs (gray line) in a WT mouse. D, Amplitudes of mGluR1-mediated slowEPSCsareplottedagainstfrequencyofPF-stimulationinmGluR1a-rescueandmGluR1b-rescuemice.Pooleddatafrom7PCs in both (mean SEM). *p 0.05 versus mGluR1a-rescue (two-way repeated ANOVA with post hoc Bonferroni test).
Article Snippet: Subsequently, the Sepharose was washed three times with 1 ml of lysis buffer, and bound proteins were immunoblotted using antibodies against the extracellular domain of
Techniques:
Journal: Journal of Neuroscience
Article Title: The Synaptic Targeting of mGluR1 by Its Carboxyl-Terminal Domain Is Crucial for Cerebellar Function
doi: 10.1523/jneurosci.3542-13.2014
Figure Lengend Snippet: Figure 7. mGluR1-mediated cation currents in cultured PCs from WT and mGluR1b-rescue mice. A, mGluR1-induced cation currents in cultured PCs. The holding potential was set at 50 mV to inactivate depolarization-evoked currents; the cation current was measured as an outward current (outward deflection is indicated as downward to facilitate comparison with the other experiments).EachsetoftracesindicatesthesamplecurrentresponsesofaculturedWTormGluR1b-rescuePCtothelabeleddoses ofDHPG.DHPGwasappliedtothewholeoftheexaminedcellthroughawide-tippedpipetteduringtheperiodindicatedbyathick bar. B, DHPG dose–response relation of cation currents. Dots and error bars indicate means and SEM, respectively (n 6–9, WT cells;n6–12,mGluR1b-rescuecells).Foreachcell,theamplitudeswith0.5nMto5MDHPGarenormalizedtothevaluewith 500 M DHPG. The sensitivity to DHPG, an mGluR1 agonist, was not different between WT and mGluR1b-rescue (1b rescue) PCs.
Article Snippet: Subsequently, the Sepharose was washed three times with 1 ml of lysis buffer, and bound proteins were immunoblotted using antibodies against the extracellular domain of
Techniques: Cell Culture, Comparison
Journal: Journal of Neuroscience
Article Title: The Synaptic Targeting of mGluR1 by Its Carboxyl-Terminal Domain Is Crucial for Cerebellar Function
doi: 10.1523/jneurosci.3542-13.2014
Figure Lengend Snippet: Figure 8. Normal motor coordination but impaired delay eyeblink conditioning in mGluR1b-rescue mice. A, Rotating rod task in WT (n 12), mGluR1-KO (KO; n 8), mGluR1a-rescue (1a rescue;n11),andmGluR1b-rescue(1brescue;n10)mice.Thestay-time(seconds)ofthemiceonarotatingrod(25rpm)isplottedversusthetrainingday.B,Fixedbartest.Thetimetheanimal could remain on the wooden bar (6 mm in width and 40 cm above the ground) was measured. A maximum of 60 s was allowed per mouse. There was no significant difference between WT (open bar,n11)andmGluR1b-rescue(closedbar,n8)mice(p0.84).C,Percentageofconditionedresponse(CR)duringdelayeyeblinkconditioninginWTmice(n12),mGluR1-KOmice(KO; n12),mGluR1a-rescuemice(1arescue;n11),andmGluR1b-rescuemice(1brescue;n14).Conditioningexperimentconsistedofanacquisitionphase(7d)andanextinctionphase(4d). mGluR1b-rescuemiceexhibitedsevereimpairmentofCRacquisition,althoughlearningwasfullyreinstatedinmGluR1a-rescuemice.D,Spontaneouseyeblinkfrequencywasmeasuredduring100 “nostimulus”trialsinthefirstsessionforacclimationbeforethedelayconditioningexperimentbegan.NodifferencewasobservedinWT(n12)andmGluR1b-rescue(n14)mice(p0.29). E,ThestartleresponsetoatoneCSwasmeasuredduring100trialsofthefirstsessionofdelayeyeblinkconditioning,indicatingthatnodifferencewasobservedbetweenWT(n12)andmGluR1b-rescue (n14)mice(p0.67).F,Pseudo-conditioning.Theeyelidresponseduringthepseudo-conditioningdidnotincreaseinWT(n6)andmGluR1b-rescue(n5)mice(F(6,54)0.58forinteractioneffect andp0.87,F(1,9)0.030forgenotypiceffect,p0.79).TheCSandUSwerepseudo-randomlypresentedwithaninterstimulusintervalrangingfrom0to20s.G,AveragedURamplitudesforWT(n12) andmGluR1b-rescue(n14)miceduringdelayconditioning.Inbothgenotypicgroups,theURamplitudeswerenearlyconstantthroughoutthe7dacquisitionphase.NodifferencewasobservedbetweenWT andmGluR1b-rescuemice(p0.59,F(6,144)0.73forinteractioneffectandp0.83,F(1,24)0.048forgenotypiceffect).
Article Snippet: Subsequently, the Sepharose was washed three times with 1 ml of lysis buffer, and bound proteins were immunoblotted using antibodies against the extracellular domain of
Techniques: