anti mglur1  (Alomone Labs)


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    Alomone Labs anti mglur1
    Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface <t>mGluR1</t> before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.
    Anti 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/result/anti mglur1/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti mglur1 - by Bioz Stars, 2023-06
    93/100 stars

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    1) Product Images from "Disassembly of Shank and Homer Synaptic Clusters Is Driven by Soluble β-Amyloid 1-40 through Divergent NMDAR-Dependent Signalling Pathways"

    Article Title: Disassembly of Shank and Homer Synaptic Clusters Is Driven by Soluble β-Amyloid 1-40 through Divergent NMDAR-Dependent Signalling Pathways

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0006011

    Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface mGluR1 before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.
    Figure Legend Snippet: Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface mGluR1 before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.

    Techniques Used:

    anti mglur1  (Alomone Labs)


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    Alomone Labs anti mglur1
    Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface <t>mGluR1</t> before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.
    Anti 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/result/anti mglur1/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti mglur1 - by Bioz Stars, 2023-06
    93/100 stars

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    1) Product Images from "Disassembly of Shank and Homer Synaptic Clusters Is Driven by Soluble β-Amyloid 1-40 through Divergent NMDAR-Dependent Signalling Pathways"

    Article Title: Disassembly of Shank and Homer Synaptic Clusters Is Driven by Soluble β-Amyloid 1-40 through Divergent NMDAR-Dependent Signalling Pathways

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0006011

    Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface mGluR1 before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.
    Figure Legend Snippet: Rat cortical neurons were treated with Aβ (1 µM) for 1 h (with or without co-treatment with the NMDAR antagonist MK801, or the VDCC blocker verapamil) and then immunostained for surface mGluR1 before fixation. (A, B) Aβ downregulates surface mGluR1 (surface cluster size 66.0±2.8%, N = 10, n = 300, p<0.05); pre-treatment with either MK801 (10 µM) or verapamil (50 µM) blocked this effect (102.9±10.5%, for MK801+Aβ vs. MK alone; 109.8±4.1%, for verapamil+Aβ vs. verapamil alone). (C, D) Aβ treatment results in decreased synaptic localization of total mGluR1 (ratio of mGluR1/synaptophysin immunopositive puncta, 47.3±5.7% of baseline, n = 600, p<0.05); pre-treatment with either MK801 or verapamil prevented this effect (102.0±7.2%, for MK801+Aβ vs. MK alone; 106.7±10.8% for verapamil+Aβ vs. verapamil alone). (C, E) Aβ treatment results in reduced size of total synaptic mGluR1 clusters (68.1±8.0%, N = 10, n = 600, p<0.05); pre-treatment with either MK801 or verapamil abolished Aβ-induced cluster shrinkage (93±11.1%, for MK801+Aβ vs. MK alone; 112.4±10.7%, for verapamil+Aβ vs. verapamil alone). Scale bar represents 5 µm.

    Techniques Used:

    metabotropic glutamate receptors  (Alomone Labs)


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    Alomone Labs metabotropic glutamate receptors
    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 <t>mGluR</t> antagonist (PCCG-13, filled triangles, 95.0±9.2%, n = 6). B) <t>mGluR1</t> 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 .
    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
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    metabotropic glutamate receptors - by Bioz Stars, 2023-06
    93/100 stars

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    1) Product Images from "Dopamine-Induced Plasticity, Phospholipase D (PLD) Activity and Cocaine-Cue Behavior Depend on PLD-Linked Metabotropic Glutamate Receptors in Amygdala"

    Article Title: Dopamine-Induced Plasticity, Phospholipase D (PLD) Activity and Cocaine-Cue Behavior Depend on PLD-Linked Metabotropic Glutamate Receptors in Amygdala

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0025639

    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 .
    Figure Legend 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 .

    Techniques Used:

    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 .
    Figure Legend 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 .

    Techniques Used: Activity Assay

    rabbit mglur1  (Alomone Labs)


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    Alomone Labs rabbit mglur1
    Rabbit 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
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    Average 93 stars, based on 1 article reviews
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    anti mglur1  (Alomone Labs)


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    Alomone Labs anti mglur1
    Anti 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/result/anti mglur1/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
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    anti mglur1  (Alomone Labs)


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    Alomone Labs anti mglur1
    Anti 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/result/anti mglur1/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
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    mglur5 1a  (Alomone Labs)


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    Alomone Labs mglur5 1a
    Mglur5 1a, 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
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    anti mglur1 antibody  (Alomone Labs)


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    Alomone Labs anti mglur1 antibody
    Anti Mglur1 Antibody, 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/result/anti mglur1 antibody/product/Alomone Labs
    Average 93 stars, based on 1 article reviews
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    goat anti mglur1  (Alomone Labs)


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    Alomone Labs goat anti mglur1
    Goat Anti 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
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    Average 93 stars, based on 1 article reviews
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    rabbit anti mglur1  (Alomone Labs)


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    Alomone Labs rabbit anti mglur1
    Dominant Mutations in GRM1 Result in a Cerebellar Phenotype (A) MRI brain imaging of case subjects. Top left: family 1, affected son (II:1); top right: family 1, affected granddaughter (III:1), both showing cerebellar atrophy. Bottom left: family 2, affected brother (II:1) showing cerebellar atrophy; bottom right: family 3, affected daughter (II:1), showing normal imaging. The cerebellum is indicated in each case by an arrow. (B) Pedigrees of affected families. Squares denote male family members, circles female family members, and black symbols affected family members. Probands are indicated in each case by an arrow. The following individuals were sequenced: family 1 I:2, II:1, and III:1; family 2 II:1, II:2, and III:1; family 3 I:1, I:2, and II:1. Asterisks ( ∗ ) indicate the presence of the mutation. (C) Schematic representation of the positions of the dominant mutations within <t>mGluR1.</t> At the N terminus, the amino-terminal domain (ATD) is followed by the cysteine-rich domain (CRD), seven transmembrane domains (TMD), and the intracellular C-terminal domain (CTD). Cysteine residues, which function in dimerization, are indicated by S. GRM1 mutations are indicated by black stars. The p.Tyr262Cys variant is located in the extracellular ligand-binding region, p.Tyr792Cys within transmembrane helix 6, and p.Gly1056Argfs ∗ 49 in the C-terminal domain of the receptor. Figure adapted from Willard and Koochekpour.
    Rabbit Anti 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
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    Average 93 stars, based on 1 article reviews
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    rabbit anti mglur1 - by Bioz Stars, 2023-06
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    1) Product Images from "Dominant Mutations in GRM1 Cause Spinocerebellar Ataxia Type 44"

    Article Title: Dominant Mutations in GRM1 Cause Spinocerebellar Ataxia Type 44

    Journal: American Journal of Human Genetics

    doi: 10.1016/j.ajhg.2017.08.005

    Dominant Mutations in GRM1 Result in a Cerebellar Phenotype (A) MRI brain imaging of case subjects. Top left: family 1, affected son (II:1); top right: family 1, affected granddaughter (III:1), both showing cerebellar atrophy. Bottom left: family 2, affected brother (II:1) showing cerebellar atrophy; bottom right: family 3, affected daughter (II:1), showing normal imaging. The cerebellum is indicated in each case by an arrow. (B) Pedigrees of affected families. Squares denote male family members, circles female family members, and black symbols affected family members. Probands are indicated in each case by an arrow. The following individuals were sequenced: family 1 I:2, II:1, and III:1; family 2 II:1, II:2, and III:1; family 3 I:1, I:2, and II:1. Asterisks ( ∗ ) indicate the presence of the mutation. (C) Schematic representation of the positions of the dominant mutations within mGluR1. At the N terminus, the amino-terminal domain (ATD) is followed by the cysteine-rich domain (CRD), seven transmembrane domains (TMD), and the intracellular C-terminal domain (CTD). Cysteine residues, which function in dimerization, are indicated by S. GRM1 mutations are indicated by black stars. The p.Tyr262Cys variant is located in the extracellular ligand-binding region, p.Tyr792Cys within transmembrane helix 6, and p.Gly1056Argfs ∗ 49 in the C-terminal domain of the receptor. Figure adapted from Willard and Koochekpour.
    Figure Legend Snippet: Dominant Mutations in GRM1 Result in a Cerebellar Phenotype (A) MRI brain imaging of case subjects. Top left: family 1, affected son (II:1); top right: family 1, affected granddaughter (III:1), both showing cerebellar atrophy. Bottom left: family 2, affected brother (II:1) showing cerebellar atrophy; bottom right: family 3, affected daughter (II:1), showing normal imaging. The cerebellum is indicated in each case by an arrow. (B) Pedigrees of affected families. Squares denote male family members, circles female family members, and black symbols affected family members. Probands are indicated in each case by an arrow. The following individuals were sequenced: family 1 I:2, II:1, and III:1; family 2 II:1, II:2, and III:1; family 3 I:1, I:2, and II:1. Asterisks ( ∗ ) indicate the presence of the mutation. (C) Schematic representation of the positions of the dominant mutations within mGluR1. At the N terminus, the amino-terminal domain (ATD) is followed by the cysteine-rich domain (CRD), seven transmembrane domains (TMD), and the intracellular C-terminal domain (CTD). Cysteine residues, which function in dimerization, are indicated by S. GRM1 mutations are indicated by black stars. The p.Tyr262Cys variant is located in the extracellular ligand-binding region, p.Tyr792Cys within transmembrane helix 6, and p.Gly1056Argfs ∗ 49 in the C-terminal domain of the receptor. Figure adapted from Willard and Koochekpour.

    Techniques Used: Imaging, Mutagenesis, Variant Assay, Ligand Binding Assay

    Deletion of the C-Terminal Domain of mGluR1 Affects Binding to Homer2b GRM1 expression constructs were generated using GRM1-Tango (Addgene plasmid 66387), into which a stop codon was inserted to prevent readthrough into the Tango element. The three dominant mutations were introduced by site-directed mutagenesis, and results were verified by Sanger sequencing. Constructs were transfected into HEK293FT cells (Invitrogen), using Lipofectamine 3000 (Thermo Fisher Scientific). 24 hr after transfection, cells were subjected to immunostaining using the following primary antibodies: mouse anti-FLAG (1:500; Sigma-Aldrich), rabbit anti-MYC (1:500; Abcam), and goat anti-mGluR1 (1:500; Santa-Cruz). Secondary antibodies: goat anti-mouse Alexa594 or Alexa488, goat anti-rabbit Alexa488, and donkey anti-goat Alexa594 (all 1:1,000; Life Technologies). Nuclei were stained with DAPI. (A) Cells transfected with FLAG-tagged mGluR1 only (left) show diffuse localization of wild-type (WT) and mutant mGluR1 (red). Co-transfection with MYC-tagged Homer2b results in clustering of WT mGluR1 and the p.Tyr262Cys and p.Tyr792Cys mutants but not the p.Gly1056Argfs ∗ 49 deletion mutant. Scale bar: 20 μm. (B) Quantitative analysis of mGluR1-Homer2b clustering. For each biological replicate, 100 cells were counted. Bars show the mean of three biological replicates ± SEM. ∗∗∗ p < 0.001 (one-way ANOVA, followed by Bonferroni’s multiple comparison test). (C) Western blot analysis of mGluR1 and components of its downstream signaling cascade. Protein extracts were prepared from cultured cells 24 hr after transfection, in ice-cold RIPA buffer (Thermo Fisher) containing 1× cOmplete, Mini, EDTA-free Protease Inhibitor Cocktail (Roche), 1× PhosSTOP (Roche), and 1 mM dithiothreitol (DTT), and analyzed by standard SDS-polyacrylamide gel electrophoresis and immunoblotting. Primary antibodies: rabbit anti-mGluR1 (1:200; Alomone Labs), rabbit anti-p44/42 MAPK (Erk1/2) and rabbit anti-phospho-p44/42 MAPK (Erk1/2) (both 1:1,000; Cell Signaling Technologies), and mouse anti-actin (1:1,000; Abcam). HRP-conjugated secondary antibodies: donkey anti-rabbit and sheep anti-mouse (both 1:10,000; GE Healthcare). A decrease in phosphorylation of Extracellular Signal-Related Kinase 1/2 (ERK1/2) was observed in cells transfected with the mGluR1 p.Gly1056Argfs ∗ 49 mutant, indicating disruption of mGluR1 downstream signaling events.
    Figure Legend Snippet: Deletion of the C-Terminal Domain of mGluR1 Affects Binding to Homer2b GRM1 expression constructs were generated using GRM1-Tango (Addgene plasmid 66387), into which a stop codon was inserted to prevent readthrough into the Tango element. The three dominant mutations were introduced by site-directed mutagenesis, and results were verified by Sanger sequencing. Constructs were transfected into HEK293FT cells (Invitrogen), using Lipofectamine 3000 (Thermo Fisher Scientific). 24 hr after transfection, cells were subjected to immunostaining using the following primary antibodies: mouse anti-FLAG (1:500; Sigma-Aldrich), rabbit anti-MYC (1:500; Abcam), and goat anti-mGluR1 (1:500; Santa-Cruz). Secondary antibodies: goat anti-mouse Alexa594 or Alexa488, goat anti-rabbit Alexa488, and donkey anti-goat Alexa594 (all 1:1,000; Life Technologies). Nuclei were stained with DAPI. (A) Cells transfected with FLAG-tagged mGluR1 only (left) show diffuse localization of wild-type (WT) and mutant mGluR1 (red). Co-transfection with MYC-tagged Homer2b results in clustering of WT mGluR1 and the p.Tyr262Cys and p.Tyr792Cys mutants but not the p.Gly1056Argfs ∗ 49 deletion mutant. Scale bar: 20 μm. (B) Quantitative analysis of mGluR1-Homer2b clustering. For each biological replicate, 100 cells were counted. Bars show the mean of three biological replicates ± SEM. ∗∗∗ p < 0.001 (one-way ANOVA, followed by Bonferroni’s multiple comparison test). (C) Western blot analysis of mGluR1 and components of its downstream signaling cascade. Protein extracts were prepared from cultured cells 24 hr after transfection, in ice-cold RIPA buffer (Thermo Fisher) containing 1× cOmplete, Mini, EDTA-free Protease Inhibitor Cocktail (Roche), 1× PhosSTOP (Roche), and 1 mM dithiothreitol (DTT), and analyzed by standard SDS-polyacrylamide gel electrophoresis and immunoblotting. Primary antibodies: rabbit anti-mGluR1 (1:200; Alomone Labs), rabbit anti-p44/42 MAPK (Erk1/2) and rabbit anti-phospho-p44/42 MAPK (Erk1/2) (both 1:1,000; Cell Signaling Technologies), and mouse anti-actin (1:1,000; Abcam). HRP-conjugated secondary antibodies: donkey anti-rabbit and sheep anti-mouse (both 1:10,000; GE Healthcare). A decrease in phosphorylation of Extracellular Signal-Related Kinase 1/2 (ERK1/2) was observed in cells transfected with the mGluR1 p.Gly1056Argfs ∗ 49 mutant, indicating disruption of mGluR1 downstream signaling events.

    Techniques Used: Binding Assay, Expressing, Construct, Generated, Plasmid Preparation, Mutagenesis, Sequencing, Transfection, Immunostaining, Staining, Cotransfection, Western Blot, Cell Culture, Protease Inhibitor, Polyacrylamide Gel Electrophoresis

    GRM1 Mutations Affect Receptor Activity and Can Be Pharmacologically Modulated In Vitro (A) Overview of the modified luciferase reporter assay used to assess mGluR1 activity. The GRM1-Tango construct, into which mutations were introduced, consists of a FLAG-tagged GRM1 sequence followed by the Tango element, i.e., a V 2 tail capable of recruiting β-arrestin, a cleavage site for the tobacco etch virus (TEV) protease, and a tetracycline-controlled transactivator (tTA). GRM1 mutations are indicated by black stars. Signaling via mGluR1 results in a conformational change in the V 2 tail and recruitment of β-arrestin, followed by TEV protease-mediated cleavage and release of tTA, which translocates to the nucleus and activates transcription of the luciferase reporter gene, resulting in a quantifiable output of mGluR1 activity in the form of luminescence (figure adapted from Kroeze et al. ). (B) Structure of the mGluR1 endogenous ligand, L-glutamate, and the inhibitors used in this study: competitive inhibitor MCPG, inverse agonist BAY36-7620, and the FDA-approved negative allosteric modulator Nitazoxanide. (C) Relative activity of mGluR1 mutants. HTLA cells, stably expressing a β-arrestin/TEV protease complex and a tTA-dependent luciferase reporter gene, were seeded at 70,000 cells/well onto poly-L-lysine-coated 96-well plates in DMEM without L-glutamine (Life Technologies), containing penicillin, streptomycin, hygromycin B, and puromycin. After 24 hr, cells were transiently transfected with the four GRM1-Tango constructs (WT, p.Tyr262Cys, p.Tyr792Cys, and p.Gly1056Argfs ∗ 49) and incubated for a further 24 hr. Cells were then treated overnight with 500 μM ( RS )-MPCG (Tocris), 10 μM BAY36-7620 (Tocris), or 10 μM Nitazoxanide (Sigma-Aldrich), diluted in assay buffer (20 mM HBSS, 1× HEPES [pH 7.4], both Life Technologies), before cell lysis in Bright-Glo solution (Promega) and luminescence reading. Data were analyzed statistically in GraphPad Prism using a two-way analysis of variance (ANOVA), followed by Bonferroni’s multiple comparison post hoc test. Significance was defined as p < 0.05 and is shown here relative to mGluR1 wild-type (WT) in the untreated condition and relative to the corresponding untreated sample for all other treatment conditions, unless otherwise indicated. Data shown are mean ± SEM from one experiment, representative of results recorded in four biological replicates, each consisting of three technical replicates per construct per condition. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.
    Figure Legend Snippet: GRM1 Mutations Affect Receptor Activity and Can Be Pharmacologically Modulated In Vitro (A) Overview of the modified luciferase reporter assay used to assess mGluR1 activity. The GRM1-Tango construct, into which mutations were introduced, consists of a FLAG-tagged GRM1 sequence followed by the Tango element, i.e., a V 2 tail capable of recruiting β-arrestin, a cleavage site for the tobacco etch virus (TEV) protease, and a tetracycline-controlled transactivator (tTA). GRM1 mutations are indicated by black stars. Signaling via mGluR1 results in a conformational change in the V 2 tail and recruitment of β-arrestin, followed by TEV protease-mediated cleavage and release of tTA, which translocates to the nucleus and activates transcription of the luciferase reporter gene, resulting in a quantifiable output of mGluR1 activity in the form of luminescence (figure adapted from Kroeze et al. ). (B) Structure of the mGluR1 endogenous ligand, L-glutamate, and the inhibitors used in this study: competitive inhibitor MCPG, inverse agonist BAY36-7620, and the FDA-approved negative allosteric modulator Nitazoxanide. (C) Relative activity of mGluR1 mutants. HTLA cells, stably expressing a β-arrestin/TEV protease complex and a tTA-dependent luciferase reporter gene, were seeded at 70,000 cells/well onto poly-L-lysine-coated 96-well plates in DMEM without L-glutamine (Life Technologies), containing penicillin, streptomycin, hygromycin B, and puromycin. After 24 hr, cells were transiently transfected with the four GRM1-Tango constructs (WT, p.Tyr262Cys, p.Tyr792Cys, and p.Gly1056Argfs ∗ 49) and incubated for a further 24 hr. Cells were then treated overnight with 500 μM ( RS )-MPCG (Tocris), 10 μM BAY36-7620 (Tocris), or 10 μM Nitazoxanide (Sigma-Aldrich), diluted in assay buffer (20 mM HBSS, 1× HEPES [pH 7.4], both Life Technologies), before cell lysis in Bright-Glo solution (Promega) and luminescence reading. Data were analyzed statistically in GraphPad Prism using a two-way analysis of variance (ANOVA), followed by Bonferroni’s multiple comparison post hoc test. Significance was defined as p < 0.05 and is shown here relative to mGluR1 wild-type (WT) in the untreated condition and relative to the corresponding untreated sample for all other treatment conditions, unless otherwise indicated. Data shown are mean ± SEM from one experiment, representative of results recorded in four biological replicates, each consisting of three technical replicates per construct per condition. ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001, ∗∗∗∗ p < 0.0001.

    Techniques Used: Activity Assay, In Vitro, Modification, Luciferase, Reporter Assay, Construct, Sequencing, Stable Transfection, Expressing, Transfection, Incubation, Lysis

    rabbit anti mglur1a b  (Alomone Labs)


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    Alomone Labs rabbit anti mglur1a b
    mGluR1, GluRδ2, and PKCγ form protein complexes in cerebellum. A, B, Silver staining of proteins coimmunoprecipitated with <t>mGluR1a</t> or anti-GluRδ2. Each protein lane was excised, divided into six pieces, and analyzed by mass spectroscopy. Proteins identified by their tryptic fragments are indicated. Contaminating IgG, keratin, and trypsin were omitted. C, PKCγ coimmunoprecipitated with mGluR1 or GluRδ2. D, GluRδ2 coimmunoprecipitated with mGluR1 or PKCγ. E, mGluR1a coimmunoprecipitated with GluRδ2 or PKCγ. F, Other metabotropic and ionotropic glutamate receptors did not coimmunoprecipitate with mGluR1, GluRδ2, or PKCγ, confirming the specificity of the IP. G, mGluR1 and GluRδ2 did not associate with other PKC subtypes; H, PKCγ did not associate with mGluR1 or GluRδ2 in cerebral cortex.
    Rabbit Anti Mglur1a B, 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
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    1) Product Images from "Glutamate Receptor δ2 Associates with Metabotropic Glutamate Receptor 1 (mGluR1), Protein Kinase Cγ, and Canonical Transient Receptor Potential 3 and Regulates mGluR1-Mediated Synaptic Transmission in Cerebellar Purkinje Neurons"

    Article Title: Glutamate Receptor δ2 Associates with Metabotropic Glutamate Receptor 1 (mGluR1), Protein Kinase Cγ, and Canonical Transient Receptor Potential 3 and Regulates mGluR1-Mediated Synaptic Transmission in Cerebellar Purkinje Neurons

    Journal: The Journal of Neuroscience

    doi: 10.1523/JNEUROSCI.0705-12.2012

    mGluR1, GluRδ2, and PKCγ form protein complexes in cerebellum. A, B, Silver staining of proteins coimmunoprecipitated with mGluR1a or anti-GluRδ2. Each protein lane was excised, divided into six pieces, and analyzed by mass spectroscopy. Proteins identified by their tryptic fragments are indicated. Contaminating IgG, keratin, and trypsin were omitted. C, PKCγ coimmunoprecipitated with mGluR1 or GluRδ2. D, GluRδ2 coimmunoprecipitated with mGluR1 or PKCγ. E, mGluR1a coimmunoprecipitated with GluRδ2 or PKCγ. F, Other metabotropic and ionotropic glutamate receptors did not coimmunoprecipitate with mGluR1, GluRδ2, or PKCγ, confirming the specificity of the IP. G, mGluR1 and GluRδ2 did not associate with other PKC subtypes; H, PKCγ did not associate with mGluR1 or GluRδ2 in cerebral cortex.
    Figure Legend Snippet: mGluR1, GluRδ2, and PKCγ form protein complexes in cerebellum. A, B, Silver staining of proteins coimmunoprecipitated with mGluR1a or anti-GluRδ2. Each protein lane was excised, divided into six pieces, and analyzed by mass spectroscopy. Proteins identified by their tryptic fragments are indicated. Contaminating IgG, keratin, and trypsin were omitted. C, PKCγ coimmunoprecipitated with mGluR1 or GluRδ2. D, GluRδ2 coimmunoprecipitated with mGluR1 or PKCγ. E, mGluR1a coimmunoprecipitated with GluRδ2 or PKCγ. F, Other metabotropic and ionotropic glutamate receptors did not coimmunoprecipitate with mGluR1, GluRδ2, or PKCγ, confirming the specificity of the IP. G, mGluR1 and GluRδ2 did not associate with other PKC subtypes; H, PKCγ did not associate with mGluR1 or GluRδ2 in cerebral cortex.

    Techniques Used: Silver Staining, Mass Spectrometry

    TRPC3 associates with mGluR–GluRδ2–PKCγ in cerebellum. Triton X-100-solubilized postnuclear membrane fractions from either wild-type or mutant mice were immunoprecipitated and blotted as indicated. A, mGluR1 coimmunoprecipitated with TRPC3 from either wild-type (A1) or GluRδ2 (A2) mutant cerebella. B1, GluRδ2 coimmunoprecipitated with TRPC3. B2, In ho-4J mice, a truncated GluRδ2 is expressed at very low levels. C, PKCγ associates with mGluR1 or TRPC3 in the presence (C1) or absence (C2) of GluRδ2. D, TRPC3 and GluRδ2 interact in the presence (D1) or absence (D2) of mGluR1. E, PKCγ associates with GluRδ2 and TRPC3, which is not affected by the presence or absence of mGluR1. F, GluK2/3 did not interact with mGluR1, GluRδ2, or TRPC3.
    Figure Legend Snippet: TRPC3 associates with mGluR–GluRδ2–PKCγ in cerebellum. Triton X-100-solubilized postnuclear membrane fractions from either wild-type or mutant mice were immunoprecipitated and blotted as indicated. A, mGluR1 coimmunoprecipitated with TRPC3 from either wild-type (A1) or GluRδ2 (A2) mutant cerebella. B1, GluRδ2 coimmunoprecipitated with TRPC3. B2, In ho-4J mice, a truncated GluRδ2 is expressed at very low levels. C, PKCγ associates with mGluR1 or TRPC3 in the presence (C1) or absence (C2) of GluRδ2. D, TRPC3 and GluRδ2 interact in the presence (D1) or absence (D2) of mGluR1. E, PKCγ associates with GluRδ2 and TRPC3, which is not affected by the presence or absence of mGluR1. F, GluK2/3 did not interact with mGluR1, GluRδ2, or TRPC3.

    Techniques Used: Mutagenesis, Immunoprecipitation

    Neither GluRδ2 nor mGluR1 mutation affects cerebellar levels of interacting proteins. A, GluRδ2 mutation results in increased levels of GluA2 but does not affect levels of mGluR1, TRPC3, or other synaptic proteins. B, Mutation of GluR1 does not affect levels of any of the proteins analyzed. Error bars indicate SEM. Statistical significance with respect to GluRδ2+/+ or mGluR1+/+ (t test). n = 4 for each sample. *p < 0.05.
    Figure Legend Snippet: Neither GluRδ2 nor mGluR1 mutation affects cerebellar levels of interacting proteins. A, GluRδ2 mutation results in increased levels of GluA2 but does not affect levels of mGluR1, TRPC3, or other synaptic proteins. B, Mutation of GluR1 does not affect levels of any of the proteins analyzed. Error bars indicate SEM. Statistical significance with respect to GluRδ2+/+ or mGluR1+/+ (t test). n = 4 for each sample. *p < 0.05.

    Techniques Used: Mutagenesis

    GluRδ2 or mGluR1 mutation does not affect immunofluorescent distribution of the interacting proteins. A–C, Immunofluorescent double labeling of sagittal cerebellar sections; the bottom panels are magnified images of the molecular layer. Specificity of staining is confirmed by elimination of immunosignal in corresponding mutant mice. A, Punctate GluRδ2 staining partially colocalizes with mGluR1 in molecular layer of wild type. The molecular layer staining patterns for GluRδ2 and mGluR1 were not dramatically altered in the mGluR1-KO or GluRδ2ho-4J/ho-4J, respectively. B, PKCγ shows strong labeling of Purkinje cell bodies, dendrites, and neuropil. The colabeling of mGluR1 and PKCγ in the molecular layer was not dramatically altered in the GluRδ2ho-4J/ho-4J, and the PKCγ distribution was not changed in the mGlu1-KO. C, mGluR1 and TRPC3 partially colocalize in wild-type mouse. No obvious difference in the staining patterns was detected in either GluRδ2ho-4J/ho-4J or mGluR1-KO. ML, Molecular layer; PC, Purkinje cell.
    Figure Legend Snippet: GluRδ2 or mGluR1 mutation does not affect immunofluorescent distribution of the interacting proteins. A–C, Immunofluorescent double labeling of sagittal cerebellar sections; the bottom panels are magnified images of the molecular layer. Specificity of staining is confirmed by elimination of immunosignal in corresponding mutant mice. A, Punctate GluRδ2 staining partially colocalizes with mGluR1 in molecular layer of wild type. The molecular layer staining patterns for GluRδ2 and mGluR1 were not dramatically altered in the mGluR1-KO or GluRδ2ho-4J/ho-4J, respectively. B, PKCγ shows strong labeling of Purkinje cell bodies, dendrites, and neuropil. The colabeling of mGluR1 and PKCγ in the molecular layer was not dramatically altered in the GluRδ2ho-4J/ho-4J, and the PKCγ distribution was not changed in the mGlu1-KO. C, mGluR1 and TRPC3 partially colocalize in wild-type mouse. No obvious difference in the staining patterns was detected in either GluRδ2ho-4J/ho-4J or mGluR1-KO. ML, Molecular layer; PC, Purkinje cell.

    Techniques Used: Mutagenesis, Labeling, Staining

    In GluRδ2ho-4J/ho-4J, TRPC3 partially redistributes to the Triton X-100-soluble fraction. A, Synaptosomal (Syp) and PSD fractions of mouse cerebella from wild-type, GluRδ2ho-4J/ho-4J, and mGluR1-KO were prepared and immunoblotted. mGluR1, GluRδ2, PKCγ, and TRPC3 are detected in the synaptosomal and PSD fractions. The blotting profiles of PSD-95 and synaptophysin validate the subcellular fractionations. B, Cerebellar homogenates were treated with 2.5% Triton X-100, followed by ultracentrifugation to yield supernatant (Sup) and pellet (Ppt). C, A greater percentage of TRPC3 was detected in Triton X-100-soluble fraction in GluRδ2ho-4J/ho-4J than in wild type (GluRδ2+/+). Error bars indicate SEM. Statistical significance with respect to GluRδ2+/+ (t test). n = 4 for each sample. *p < 0.05.
    Figure Legend Snippet: In GluRδ2ho-4J/ho-4J, TRPC3 partially redistributes to the Triton X-100-soluble fraction. A, Synaptosomal (Syp) and PSD fractions of mouse cerebella from wild-type, GluRδ2ho-4J/ho-4J, and mGluR1-KO were prepared and immunoblotted. mGluR1, GluRδ2, PKCγ, and TRPC3 are detected in the synaptosomal and PSD fractions. The blotting profiles of PSD-95 and synaptophysin validate the subcellular fractionations. B, Cerebellar homogenates were treated with 2.5% Triton X-100, followed by ultracentrifugation to yield supernatant (Sup) and pellet (Ppt). C, A greater percentage of TRPC3 was detected in Triton X-100-soluble fraction in GluRδ2ho-4J/ho-4J than in wild type (GluRδ2+/+). Error bars indicate SEM. Statistical significance with respect to GluRδ2+/+ (t test). n = 4 for each sample. *p < 0.05.

    Techniques Used:

    Effects of mGluR1 and GluRδ2 mutation on surface expression of interacting proteins. Mouse cerebellar slices were treated with a membrane-impermeable biotinylation reagent to mark cell-surface proteins. Total, internal, and surface proteins were resolved by SDS-PAGE and subjected to immunoblotting. GluRδ2 mutation increased surface expression of TRPC3 and mGluR1, whereas other components were unchanged. mGluR1b is the shorter splice variant of mGluR1. β3-Tubulin and/or synaptophysin served as internal protein controls. Error bars indicate SEM. Statistical significance with respect to GluRδ2+/+ (t test). n = 4 for mGluR1, mGluR1b, TRPC3, and GluK2/3. n = 3 for GluA2, synaptophysin, and β3-tubulin. *p < 0.05.
    Figure Legend Snippet: Effects of mGluR1 and GluRδ2 mutation on surface expression of interacting proteins. Mouse cerebellar slices were treated with a membrane-impermeable biotinylation reagent to mark cell-surface proteins. Total, internal, and surface proteins were resolved by SDS-PAGE and subjected to immunoblotting. GluRδ2 mutation increased surface expression of TRPC3 and mGluR1, whereas other components were unchanged. mGluR1b is the shorter splice variant of mGluR1. β3-Tubulin and/or synaptophysin served as internal protein controls. Error bars indicate SEM. Statistical significance with respect to GluRδ2+/+ (t test). n = 4 for mGluR1, mGluR1b, TRPC3, and GluK2/3. n = 3 for GluA2, synaptophysin, and β3-tubulin. *p < 0.05.

    Techniques Used: Mutagenesis, Expressing, SDS Page, Western Blot, Variant Assay

    GluRδ2ho-4J/ho-4J alters the time course of the mGluR1-dependent sEPSC at PF–PC synapses. A, Typical traces of sEPSCs recorded from wild-type or GluRδ2ho-4J/ho-4J mice. Application of the mGluR1 antagonist CPCCOEt blocks sEPSCs. Inset shows corresponding fEPSCs, which are blocked by CNQX. B, GluRδ2ho-4J/ho-4J shows a similar fEPSC input–output relationship as wild type. C, Stimulation intensity for fEPSCs and sEPSCs was set to evoke similar fEPSC amplitudes (∼500 pA). D, The decay constant of fEPSCs was not affected by GluRδ2 mutation. E, The amplitude of sEPSCs was not changed significantly by GluRδ2 mutation. F, The integrated area of the CPCCOEt-sensitive sEPSC was not affected by GluRδ2 mutation. G, The onset of the sEPSC was significantly slowed in GluRδ2ho-4J/ho-4J. The average duration between the stimulus and the peak of the sEPSC was calculated. H, The average FWHM for the CPCCOEt-sensitive sEPSC was calculated. I, FWHM of sEPSC was normalized by the decay constant of fEPSC. The kinetics of sEPSCs was specifically slowed in GluRδ2ho-4J/ho-4J mice. Error bars indicate SEM. C–F, GluRδ2+/+ (n = 18) and GluRδ2ho-4J/ho-4J (n = 11). G–I, GluRδ2+/+ (n = 18) and GluRδ2ho-4J/ho-4J (n = 7). The waveforms of sEPSC in 4 of 11 samples recorded from GluRδ2ho-4J/ho-4J Purkinje cells were too small to evaluate, so we omitted these samples from G–I. J, K, NMDA receptors are not involved in the slower synaptic responses at PF–PC synapses in GluRδ2ho-4J/ho-4J. J, Typical sEPSC traces from wild-type and GluRδ2ho-4J/ho-4J in the presence or absence of 100 μm AP-5. All responses were evoked by five pulses at 100 Hz in the presence of 20 μm bicuculline and 40 μm CNQX. K, Quantified AP-5-sensitive charge transfer. Statistical significance with respect to GluRδ2+/+ (t test). **p < 0.01, ***p < 0.001.
    Figure Legend Snippet: GluRδ2ho-4J/ho-4J alters the time course of the mGluR1-dependent sEPSC at PF–PC synapses. A, Typical traces of sEPSCs recorded from wild-type or GluRδ2ho-4J/ho-4J mice. Application of the mGluR1 antagonist CPCCOEt blocks sEPSCs. Inset shows corresponding fEPSCs, which are blocked by CNQX. B, GluRδ2ho-4J/ho-4J shows a similar fEPSC input–output relationship as wild type. C, Stimulation intensity for fEPSCs and sEPSCs was set to evoke similar fEPSC amplitudes (∼500 pA). D, The decay constant of fEPSCs was not affected by GluRδ2 mutation. E, The amplitude of sEPSCs was not changed significantly by GluRδ2 mutation. F, The integrated area of the CPCCOEt-sensitive sEPSC was not affected by GluRδ2 mutation. G, The onset of the sEPSC was significantly slowed in GluRδ2ho-4J/ho-4J. The average duration between the stimulus and the peak of the sEPSC was calculated. H, The average FWHM for the CPCCOEt-sensitive sEPSC was calculated. I, FWHM of sEPSC was normalized by the decay constant of fEPSC. The kinetics of sEPSCs was specifically slowed in GluRδ2ho-4J/ho-4J mice. Error bars indicate SEM. C–F, GluRδ2+/+ (n = 18) and GluRδ2ho-4J/ho-4J (n = 11). G–I, GluRδ2+/+ (n = 18) and GluRδ2ho-4J/ho-4J (n = 7). The waveforms of sEPSC in 4 of 11 samples recorded from GluRδ2ho-4J/ho-4J Purkinje cells were too small to evaluate, so we omitted these samples from G–I. J, K, NMDA receptors are not involved in the slower synaptic responses at PF–PC synapses in GluRδ2ho-4J/ho-4J. J, Typical sEPSC traces from wild-type and GluRδ2ho-4J/ho-4J in the presence or absence of 100 μm AP-5. All responses were evoked by five pulses at 100 Hz in the presence of 20 μm bicuculline and 40 μm CNQX. K, Quantified AP-5-sensitive charge transfer. Statistical significance with respect to GluRδ2+/+ (t test). **p < 0.01, ***p < 0.001.

    Techniques Used: Mutagenesis

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