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Synaptic Systems homer2

Generation of <t>Homer2</t> S117A, S216A ( Homer2 AA/AA ) mutant knock-in mouse. A , Sequencing of Homer2 S117A site and S216A site PCR-amplified genomic DNA from homozygote Homer2 AA/AA mutant mouse. Asterisks indicate mutants. The dotted underlines indicate knock-in-created Sau96I(S117A) and HpyCH4III(S216A) restriction enzyme sites for genotyping. B , PCR genotyping of wild-type (WT) and homozygous Homer2 AA/AA mutant mouse. The PCR product images of WT and homozygous Homer2 AA/AA mutant after Sau96I and HpyCH4III digestion. C , Western blots of cortical homogenates from WT and Homer2 AA/AA mutant mice demonstrate normal levels of mGlu5 and Homers 1 and 2. D , Brief, 5-min, treatment of mouse neocortical slices with bicuculline and 4-aminopyridine (4-AP) induced phosphorylation (P) of S216 Homer2 and S117 Homer1 in WT mice as detected with phosphorylation site antibodies after immunoprecipitation with a pan-Homer antibody. In neocortical slices from Homer2 AA/AA mice, P-S216 Homer2 was not detected, but normal activity-induced p(S117)-Homer1 was observed.

Homer2, supplied by Synaptic Systems, used in various techniques. Bioz Stars score: 91/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti-homer2/160+203/pmc10131536-107-24-25
Average 91 stars, based on 3 article reviews

homer2 - by Bioz Stars, 2026-10

91/100 stars

Images

1) Product Images from "Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice"

Article Title: Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice

Journal: eNeuro

doi: 10.1523/ENEURO.0423-22.2023

Generation of Homer2 S117A, S216A ( Homer2 AA/AA ) mutant knock-in mouse. A , Sequencing of Homer2 S117A site and S216A site PCR-amplified genomic DNA from homozygote Homer2 AA/AA mutant mouse. Asterisks indicate mutants. The dotted underlines indicate knock-in-created Sau96I(S117A) and HpyCH4III(S216A) restriction enzyme sites for genotyping. B , PCR genotyping of wild-type (WT) and homozygous Homer2 AA/AA mutant mouse. The PCR product images of WT and homozygous Homer2 AA/AA mutant after Sau96I and HpyCH4III digestion. C , Western blots of cortical homogenates from WT and Homer2 AA/AA mutant mice demonstrate normal levels of mGlu5 and Homers 1 and 2. D , Brief, 5-min, treatment of mouse neocortical slices with bicuculline and 4-aminopyridine (4-AP) induced phosphorylation (P) of S216 Homer2 and S117 Homer1 in WT mice as detected with phosphorylation site antibodies after immunoprecipitation with a pan-Homer antibody. In neocortical slices from Homer2 AA/AA mice, P-S216 Homer2 was not detected, but normal activity-induced p(S117)-Homer1 was observed.

Figure Legend Snippet: Generation of Homer2 S117A, S216A ( Homer2 AA/AA ) mutant knock-in mouse. A , Sequencing of Homer2 S117A site and S216A site PCR-amplified genomic DNA from homozygote Homer2 AA/AA mutant mouse. Asterisks indicate mutants. The dotted underlines indicate knock-in-created Sau96I(S117A) and HpyCH4III(S216A) restriction enzyme sites for genotyping. B , PCR genotyping of wild-type (WT) and homozygous Homer2 AA/AA mutant mouse. The PCR product images of WT and homozygous Homer2 AA/AA mutant after Sau96I and HpyCH4III digestion. C , Western blots of cortical homogenates from WT and Homer2 AA/AA mutant mice demonstrate normal levels of mGlu5 and Homers 1 and 2. D , Brief, 5-min, treatment of mouse neocortical slices with bicuculline and 4-aminopyridine (4-AP) induced phosphorylation (P) of S216 Homer2 and S117 Homer1 in WT mice as detected with phosphorylation site antibodies after immunoprecipitation with a pan-Homer antibody. In neocortical slices from Homer2 AA/AA mice, P-S216 Homer2 was not detected, but normal activity-induced p(S117)-Homer1 was observed.

Techniques Used: Mutagenesis, Knock-In, Sequencing, Amplification, Western Blot, Phospho-proteomics, Immunoprecipitation, Activity Assay

Phosphorylation site mutants of Homer2 or mGlu5 that prevent their dynamic regulation of interactions do not affect acoustic startle or PPI. Summary of the effects of the Homer2 AA/AA ( A , B ) and the GRM5 AA/AA ( C , D ) mutations on the magnitude of startle (expressed as arbitrary units or au) in response to different acoustic stimuli in the absence (st0–st100) and presence of a 74 and 90 dB prepulse (respectively, PPI74 and PPI90). The data for female mice are presented in red in the left panels, and the data for males are presented in blue in the right panels. The data represent the means ± SEMs of the number of mice indicated in parentheses.

Figure Legend Snippet: Phosphorylation site mutants of Homer2 or mGlu5 that prevent their dynamic regulation of interactions do not affect acoustic startle or PPI. Summary of the effects of the Homer2 AA/AA ( A , B ) and the GRM5 AA/AA ( C , D ) mutations on the magnitude of startle (expressed as arbitrary units or au) in response to different acoustic stimuli in the absence (st0–st100) and presence of a 74 and 90 dB prepulse (respectively, PPI74 and PPI90). The data for female mice are presented in red in the left panels, and the data for males are presented in blue in the right panels. The data represent the means ± SEMs of the number of mice indicated in parentheses.

Techniques Used: Phospho-proteomics

Summary of the descriptive statistics and results of the Genotype × Sex ANOVAs conducted on the data from the alternate indices of spatial memory recall obtained during Morris water maze testing of Homer2 AA/AA , GRM5 AA/AA , and GRM5 R/R mutants and their WT mice

Figure Legend Snippet: Summary of the descriptive statistics and results of the Genotype × Sex ANOVAs conducted on the data from the alternate indices of spatial memory recall obtained during Morris water maze testing of Homer2 AA/AA , GRM5 AA/AA , and GRM5 R/R mutants and their WT mice

Techniques Used: Mutagenesis

Summary of the descriptive statistics and results of the Genotype × Sex ANOVAs for data pertaining to the spontaneous locomotor activity of Homer2 AA/AA and their WT mice

Figure Legend Snippet: Summary of the descriptive statistics and results of the Genotype × Sex ANOVAs for data pertaining to the spontaneous locomotor activity of Homer2 AA/AA and their WT mice

Techniques Used: Activity Assay, Saline, Injection

Phosphorylation site mutants of Homer2 that prevent activity-regulated interactions with mGlu5 exhibit normal locomotor responses to cocaine. Summary of the effects of the Homer2 AA/AA mutation on the locomotor response to acute injection with either 3 or 30 mg/kg cocaine ( A ) and its change with repeated (4×) treatment (i.e., δ Distance; B ). The data represent the means ± SEMs of the number of mice indicated in parentheses.

Figure Legend Snippet: Phosphorylation site mutants of Homer2 that prevent activity-regulated interactions with mGlu5 exhibit normal locomotor responses to cocaine. Summary of the effects of the Homer2 AA/AA mutation on the locomotor response to acute injection with either 3 or 30 mg/kg cocaine ( A ) and its change with repeated (4×) treatment (i.e., δ Distance; B ). The data represent the means ± SEMs of the number of mice indicated in parentheses.

Techniques Used: Phospho-proteomics, Activity Assay, Mutagenesis, Injection

High-dose cocaine decreases mGluR5-Homer interactions in striatal lysates and is deficient in Homer 2AA/AA mice. A , Representative Western blottings from striatal lysates from WT or Homer2 AA/AA mice (H2 AA/AA ) 1 h following acute treatment with saline (S) or cocaine (C; 20 mg/kg, i.p.). B , Quantified group data of mGlu5 that co-immunoprecipitated with a pan-Homer antibody. Cocaine reduced the mGlu5-Homer co-IP in striatum of WT, but not Homer2 AA/AA mice. n = 8 mice/group. Error bars represent SEM, ∗ p < 0.05; Sidak’s multiple comparison test. C , Quantified group data of the ratio of phosphorylated (P) T286 and active CaMKIIα to total CaMKIIα show that cocaine induced robust activation of CaMKIIα in the striatum of both WT and Homer2 AA/AA mice; n = 8 mice/group. ** p < 0.01, ∗ p < 0.05; Sidak’s multiple comparison test. There is no change in the total levels of mGlu5, Homer2, Homer1a, CaMKIIa, and GAPDH in WT and Homer2 AA/AA mice striatal homogenates with/without 1-h cocaine administration.

Figure Legend Snippet: High-dose cocaine decreases mGluR5-Homer interactions in striatal lysates and is deficient in Homer 2AA/AA mice. A , Representative Western blottings from striatal lysates from WT or Homer2 AA/AA mice (H2 AA/AA ) 1 h following acute treatment with saline (S) or cocaine (C; 20 mg/kg, i.p.). B , Quantified group data of mGlu5 that co-immunoprecipitated with a pan-Homer antibody. Cocaine reduced the mGlu5-Homer co-IP in striatum of WT, but not Homer2 AA/AA mice. n = 8 mice/group. Error bars represent SEM, ∗ p < 0.05; Sidak’s multiple comparison test. C , Quantified group data of the ratio of phosphorylated (P) T286 and active CaMKIIα to total CaMKIIα show that cocaine induced robust activation of CaMKIIα in the striatum of both WT and Homer2 AA/AA mice; n = 8 mice/group. ** p < 0.01, ∗ p < 0.05; Sidak’s multiple comparison test. There is no change in the total levels of mGlu5, Homer2, Homer1a, CaMKIIa, and GAPDH in WT and Homer2 AA/AA mice striatal homogenates with/without 1-h cocaine administration.

Techniques Used: Western Blot, Saline, Immunoprecipitation, Co-Immunoprecipitation Assay, Comparison, Activation Assay

Figure Legend Snippet: Comparison of behavioral phenotypes expressed by Homer2 AA/AA , GRM5 R/R , and GRM5 AA/AA mice

Techniques Used: Comparison, Activity Assay, Inhibition

Phosphorylation site mutants of Homer2 or mGlu5 that prevent their dynamic regulation of interactions impair learning in a Morris water maze. Summary of the effects of the Homer2 AA/AA ( A ), the GRM5 AA/AA ( A’ , A’’ ), and the GRM5 R/R ( A’’’ ) mutations on the time taken to locate a hidden platform in a Morris water maze task. As an interaction with the Sex factor was detected only in the study of GRM5 AA/AA mice, the data are presented separately for females (red) and males (blue), while the data are collapsed across sex for the other mutants. B–B’’ , Summary of the results of the memory probe test for Homer2 AA/AA , GRM5 AA/AA , and GRM5 R/R studies, respectively, indicating no effects of the mutations on recall. C , Comparison of the total latency and distance traveled during a four-trial reversal learning test between Homer2 AA/AA mice and their WT controls, indicating no difference in reversal learning. The data represent the means ± SEMs of the number of mice indicated in parentheses. * p < 0.05 for a main Genotype effect.

Figure Legend Snippet: Phosphorylation site mutants of Homer2 or mGlu5 that prevent their dynamic regulation of interactions impair learning in a Morris water maze. Summary of the effects of the Homer2 AA/AA ( A ), the GRM5 AA/AA ( A’ , A’’ ), and the GRM5 R/R ( A’’’ ) mutations on the time taken to locate a hidden platform in a Morris water maze task. As an interaction with the Sex factor was detected only in the study of GRM5 AA/AA mice, the data are presented separately for females (red) and males (blue), while the data are collapsed across sex for the other mutants. B–B’’ , Summary of the results of the memory probe test for Homer2 AA/AA , GRM5 AA/AA , and GRM5 R/R studies, respectively, indicating no effects of the mutations on recall. C , Comparison of the total latency and distance traveled during a four-trial reversal learning test between Homer2 AA/AA mice and their WT controls, indicating no difference in reversal learning. The data represent the means ± SEMs of the number of mice indicated in parentheses. * p < 0.05 for a main Genotype effect.

Techniques Used: Phospho-proteomics, Comparison

Phosphorylation site mutants of Homer2 that prevent activity-regulated interactions with mGlu5 reduces the aversiveness of high-dose cocaine. Summary of the effects of the Homer2 AA/AA ( A ) and the GRM5 R/R ( B ) mutation on the expression of place-conditioning elicited by four pairings of 3 or 30 mg/kg cocaine, indicating greater place-preference in Homer2 AA/AA mutants at the higher cocaine dose. For panels A , B , # p < 0.05 versus 0 CPP Score (i.e., place-conditioning). Summary of the effects of the Homer2 AA/AA mutation on baseline sucrose intake ( C ) and the change in sucrose intake induced by 30 mg/kg cocaine (i.e., δ Intake; D ), indicating lower sucrose intake but blunted conditioned taste aversion in mutant mice. E , F , Comparable taste-conditioning data for GRM5 AA/AA mice indicating no effect of this mutation on sucrose intake or conditioned taste aversion. For panels C , D , * p < 0.05 main Genotype effect; + p < 0.05 main Sex effect; # p < 0.05 vs. 0 (one-sample t -test). The data represent the means ± SEMs of the number of mice indicated in parentheses.

Figure Legend Snippet: Phosphorylation site mutants of Homer2 that prevent activity-regulated interactions with mGlu5 reduces the aversiveness of high-dose cocaine. Summary of the effects of the Homer2 AA/AA ( A ) and the GRM5 R/R ( B ) mutation on the expression of place-conditioning elicited by four pairings of 3 or 30 mg/kg cocaine, indicating greater place-preference in Homer2 AA/AA mutants at the higher cocaine dose. For panels A , B , # p < 0.05 versus 0 CPP Score (i.e., place-conditioning). Summary of the effects of the Homer2 AA/AA mutation on baseline sucrose intake ( C ) and the change in sucrose intake induced by 30 mg/kg cocaine (i.e., δ Intake; D ), indicating lower sucrose intake but blunted conditioned taste aversion in mutant mice. E , F , Comparable taste-conditioning data for GRM5 AA/AA mice indicating no effect of this mutation on sucrose intake or conditioned taste aversion. For panels C , D , * p < 0.05 main Genotype effect; + p < 0.05 main Sex effect; # p < 0.05 vs. 0 (one-sample t -test). The data represent the means ± SEMs of the number of mice indicated in parentheses.

Techniques Used: Phospho-proteomics, Activity Assay, Mutagenesis, Expressing

Incubation:

Article Title: Live Neuron High-Content Screening Reveals Synaptotoxic Activity in Alzheimer Mouse Model Homogenates
Article Snippet: All cells were blocked with 5% bovine serum albumin and 0.2% Triton X-100 (Sigma-Aldrich) in PBS for 1 hour at room temperature, and then incubated with anti-Synaptobrevin 2, anti-Synapsin1, anti-PSD95, or anti-Homer2 (Synaptic Systems) antibodies at 1:500 in blocking solution overnight at 4 °C, subsequently washed in 0.1% Triton X-100 in PBS three times.

Blocking Assay:

Staining:

Transgenic Assay:

Immunocytochemistry:

Expressing:

Image Search Results

Journal: eNeuro

Article Title: Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice

doi: 10.1523/ENEURO.0423-22.2023

Figure Lengend Snippet: Generation of Homer2 S117A, S216A ( Homer2 AA/AA ) mutant knock-in mouse. A , Sequencing of Homer2 S117A site and S216A site PCR-amplified genomic DNA from homozygote Homer2 AA/AA mutant mouse. Asterisks indicate mutants. The dotted underlines indicate knock-in-created Sau96I(S117A) and HpyCH4III(S216A) restriction enzyme sites for genotyping. B , PCR genotyping of wild-type (WT) and homozygous Homer2 AA/AA mutant mouse. The PCR product images of WT and homozygous Homer2 AA/AA mutant after Sau96I and HpyCH4III digestion. C , Western blots of cortical homogenates from WT and Homer2 AA/AA mutant mice demonstrate normal levels of mGlu5 and Homers 1 and 2. D , Brief, 5-min, treatment of mouse neocortical slices with bicuculline and 4-aminopyridine (4-AP) induced phosphorylation (P) of S216 Homer2 and S117 Homer1 in WT mice as detected with phosphorylation site antibodies after immunoprecipitation with a pan-Homer antibody. In neocortical slices from Homer2 AA/AA mice, P-S216 Homer2 was not detected, but normal activity-induced p(S117)-Homer1 was observed.

Article Snippet: Antibodies used in this study for Western blotting include: pan-Homer (Santa Cruz Biotechnology, E-18; sc-8921; RRID: AB_648368 ), mGlu5 (Millipore; 6451; no RRID available), Homer2 (Synaptic Systems; 160203; RRID: AB_10807099 ), GAPDH (Millipore; MAB374; RRID: AB_2107445 ), pT286CaMKIIα (Sigma; SAB4504356; no RRID available), anti-CaMKIIα (Santa Cruz; sc-5391; RRID: AB_634553 ), Homer1 phospho-S117 Homer2 phospho-S216 ( ).

Techniques: Mutagenesis, Knock-In, Sequencing, Amplification, Western Blot, Phospho-proteomics, Immunoprecipitation, Activity Assay

Journal: eNeuro

Article Title: Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice

doi: 10.1523/ENEURO.0423-22.2023

Figure Lengend Snippet: Phosphorylation site mutants of Homer2 or mGlu5 that prevent their dynamic regulation of interactions do not affect acoustic startle or PPI. Summary of the effects of the Homer2 AA/AA ( A , B ) and the GRM5 AA/AA ( C , D ) mutations on the magnitude of startle (expressed as arbitrary units or au) in response to different acoustic stimuli in the absence (st0–st100) and presence of a 74 and 90 dB prepulse (respectively, PPI74 and PPI90). The data for female mice are presented in red in the left panels, and the data for males are presented in blue in the right panels. The data represent the means ± SEMs of the number of mice indicated in parentheses.

Techniques: Phospho-proteomics

Journal: eNeuro

Article Title: Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice

doi: 10.1523/ENEURO.0423-22.2023

Figure Lengend Snippet: Summary of the descriptive statistics and results of the Genotype × Sex ANOVAs conducted on the data from the alternate indices of spatial memory recall obtained during Morris water maze testing of Homer2 AA/AA , GRM5 AA/AA , and GRM5 R/R mutants and their WT mice

Techniques: Mutagenesis

Journal: eNeuro

Article Title: Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice

doi: 10.1523/ENEURO.0423-22.2023

Figure Lengend Snippet: Summary of the descriptive statistics and results of the Genotype × Sex ANOVAs for data pertaining to the spontaneous locomotor activity of Homer2 AA/AA and their WT mice

Techniques: Activity Assay, Saline, Injection

Journal: eNeuro

Article Title: Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice

doi: 10.1523/ENEURO.0423-22.2023

Figure Lengend Snippet: Phosphorylation site mutants of Homer2 that prevent activity-regulated interactions with mGlu5 exhibit normal locomotor responses to cocaine. Summary of the effects of the Homer2 AA/AA mutation on the locomotor response to acute injection with either 3 or 30 mg/kg cocaine ( A ) and its change with repeated (4×) treatment (i.e., δ Distance; B ). The data represent the means ± SEMs of the number of mice indicated in parentheses.

Techniques: Phospho-proteomics, Activity Assay, Mutagenesis, Injection

Journal: eNeuro

Article Title: Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice

doi: 10.1523/ENEURO.0423-22.2023

Figure Lengend Snippet: High-dose cocaine decreases mGluR5-Homer interactions in striatal lysates and is deficient in Homer 2AA/AA mice. A , Representative Western blottings from striatal lysates from WT or Homer2 AA/AA mice (H2 AA/AA ) 1 h following acute treatment with saline (S) or cocaine (C; 20 mg/kg, i.p.). B , Quantified group data of mGlu5 that co-immunoprecipitated with a pan-Homer antibody. Cocaine reduced the mGlu5-Homer co-IP in striatum of WT, but not Homer2 AA/AA mice. n = 8 mice/group. Error bars represent SEM, ∗ p < 0.05; Sidak’s multiple comparison test. C , Quantified group data of the ratio of phosphorylated (P) T286 and active CaMKIIα to total CaMKIIα show that cocaine induced robust activation of CaMKIIα in the striatum of both WT and Homer2 AA/AA mice; n = 8 mice/group. ** p < 0.01, ∗ p < 0.05; Sidak’s multiple comparison test. There is no change in the total levels of mGlu5, Homer2, Homer1a, CaMKIIa, and GAPDH in WT and Homer2 AA/AA mice striatal homogenates with/without 1-h cocaine administration.

Techniques: Western Blot, Saline, Immunoprecipitation, Co-Immunoprecipitation Assay, Comparison, Activation Assay

Journal: eNeuro

Article Title: Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice

doi: 10.1523/ENEURO.0423-22.2023

Figure Lengend Snippet: Comparison of behavioral phenotypes expressed by Homer2 AA/AA , GRM5 R/R , and GRM5 AA/AA mice

Techniques: Comparison, Activity Assay, Inhibition

Journal: eNeuro

Article Title: Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice

doi: 10.1523/ENEURO.0423-22.2023

Figure Lengend Snippet: Phosphorylation site mutants of Homer2 or mGlu5 that prevent their dynamic regulation of interactions impair learning in a Morris water maze. Summary of the effects of the Homer2 AA/AA ( A ), the GRM5 AA/AA ( A’ , A’’ ), and the GRM5 R/R ( A’’’ ) mutations on the time taken to locate a hidden platform in a Morris water maze task. As an interaction with the Sex factor was detected only in the study of GRM5 AA/AA mice, the data are presented separately for females (red) and males (blue), while the data are collapsed across sex for the other mutants. B–B’’ , Summary of the results of the memory probe test for Homer2 AA/AA , GRM5 AA/AA , and GRM5 R/R studies, respectively, indicating no effects of the mutations on recall. C , Comparison of the total latency and distance traveled during a four-trial reversal learning test between Homer2 AA/AA mice and their WT controls, indicating no difference in reversal learning. The data represent the means ± SEMs of the number of mice indicated in parentheses. * p < 0.05 for a main Genotype effect.

Techniques: Phospho-proteomics, Comparison

Journal: eNeuro

Article Title: Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice

doi: 10.1523/ENEURO.0423-22.2023

Figure Lengend Snippet: Phosphorylation site mutants of Homer2 that prevent activity-regulated interactions with mGlu5 reduces the aversiveness of high-dose cocaine. Summary of the effects of the Homer2 AA/AA ( A ) and the GRM5 R/R ( B ) mutation on the expression of place-conditioning elicited by four pairings of 3 or 30 mg/kg cocaine, indicating greater place-preference in Homer2 AA/AA mutants at the higher cocaine dose. For panels A , B , # p < 0.05 versus 0 CPP Score (i.e., place-conditioning). Summary of the effects of the Homer2 AA/AA mutation on baseline sucrose intake ( C ) and the change in sucrose intake induced by 30 mg/kg cocaine (i.e., δ Intake; D ), indicating lower sucrose intake but blunted conditioned taste aversion in mutant mice. E , F , Comparable taste-conditioning data for GRM5 AA/AA mice indicating no effect of this mutation on sucrose intake or conditioned taste aversion. For panels C , D , * p < 0.05 main Genotype effect; + p < 0.05 main Sex effect; # p < 0.05 vs. 0 (one-sample t -test). The data represent the means ± SEMs of the number of mice indicated in parentheses.

Techniques: Phospho-proteomics, Activity Assay, Mutagenesis, Expressing

Decreased bone density in Homer2/3 DKO mice. (A) Microradiographic analyses of tibias in WT and Homer2/3 DKO mice. Note that in Homer2/3 DKO tibias, trabecular and cortical bone mass decreased (6 weeks). (B) Representative calcein-labeled sections of proximal tibias in WT and Homer2/3 DKO mice (scale bar, 20 μm). (C) Alkaline phosphatase (ALP) Alizarin red S (ARS) staining (n = 4). (D) μCT data of proximal femur obtained from WT and Homer2/3 DKO mice. Each parameter, including BV/TV, Tb. Th, Tb. N and Tb. Sp were calculated and presented. (E) Histomorphometric parameters. The percentage of eroded surface (ES) on bone surface (BS) increased in Homer2/3 DKO mice (left, n = 3). (F) We observed no clear difference in mineral apposition rate (MAR) between Homer2/3 DKO and WT mice (middle, n = 7). (G) Following ALP activity and ARS staining, we found no difference in osteoblastogenesis between WT and DKO mice (right, n = 4). Data were normalized to bone volume in WT mice and expressed as means ± s.e.m. *P < 0.05, **P < 0.01 compared with WT.

Journal: The Journal of endocrinology

Article Title: Homer2 and Homer3 modulate RANKL-induced NFATc1 signaling in osteoclastogenesis and bone metabolism

doi: 10.1530/JOE-19-0123

Figure Lengend Snippet: Decreased bone density in Homer2/3 DKO mice. (A) Microradiographic analyses of tibias in WT and Homer2/3 DKO mice. Note that in Homer2/3 DKO tibias, trabecular and cortical bone mass decreased (6 weeks). (B) Representative calcein-labeled sections of proximal tibias in WT and Homer2/3 DKO mice (scale bar, 20 μm). (C) Alkaline phosphatase (ALP) Alizarin red S (ARS) staining (n = 4). (D) μCT data of proximal femur obtained from WT and Homer2/3 DKO mice. Each parameter, including BV/TV, Tb. Th, Tb. N and Tb. Sp were calculated and presented. (E) Histomorphometric parameters. The percentage of eroded surface (ES) on bone surface (BS) increased in Homer2/3 DKO mice (left, n = 3). (F) We observed no clear difference in mineral apposition rate (MAR) between Homer2/3 DKO and WT mice (middle, n = 7). (G) Following ALP activity and ARS staining, we found no difference in osteoblastogenesis between WT and DKO mice (right, n = 4). Data were normalized to bone volume in WT mice and expressed as means ± s.e.m. *P < 0.05, **P < 0.01 compared with WT.

Article Snippet: Anti-Homer2, anti-Homer3 and anti-NFATc1 antibodies were obtained from Santa Cruz Biotechnology.

Techniques: Labeling, Staining, Activity Assay

RANKL-induced [Ca2+]i oscillations in WT and Homer2/3 DKO BMMs. (A) Oscillatory change in [Ca2+]i in WT and Homer2/3 DKO BMMs before and after RANKL treatment. (B) Quantitative analysis of the number of cells with [Ca2+]i oscillation induced by RANKL in WT and Homer2/3 DKO BMMs (n = 3). (C) Oscillation frequency at 24, 48 and 72 h. Data are expressed as mean ± s.e.m.

Journal: The Journal of endocrinology

Article Title: Homer2 and Homer3 modulate RANKL-induced NFATc1 signaling in osteoclastogenesis and bone metabolism

doi: 10.1530/JOE-19-0123

Figure Lengend Snippet: RANKL-induced [Ca2+]i oscillations in WT and Homer2/3 DKO BMMs. (A) Oscillatory change in [Ca2+]i in WT and Homer2/3 DKO BMMs before and after RANKL treatment. (B) Quantitative analysis of the number of cells with [Ca2+]i oscillation induced by RANKL in WT and Homer2/3 DKO BMMs (n = 3). (C) Oscillation frequency at 24, 48 and 72 h. Data are expressed as mean ± s.e.m.

Article Snippet: Anti-Homer2, anti-Homer3 and anti-NFATc1 antibodies were obtained from Santa Cruz Biotechnology.

Techniques:

RANKL-induced osteoclastogenesis is enhanced in Homer2/3 DKO BMMs. (A) RANKL-induced osteoclast differentiation in vitro in WT and Homer2/3 DKO BMMs (TRAP staining; scale bar, 50 μm). Columns show quantitative analysis of the number (middle) and the area (right) of TRAP-positive (TRAP+) multinucleated cells (MNCs; ≥3 nuclei) in WT and Homer2/3 DKO mice. The number and area of TRAP+ MNCs are significantly higher in Homer2/3 DKO mice (n = 4). (B) Pits area during osteoclastogenesis is higher in Homer2/3 DKO cells (n = 5). (C) Actin staining of TRAP+ MNCs in WT and Homer2/3 DKO cells (scale bar, 20 μm). The area of actin ring formation in TRAP+ MNCs during osteoclastogenesis is significantly higher in Homer2/3 DKO cells (n = 6). We normalized the data to the number and area of MNCs in RANKL-treated BMMs of WT mice. Results were expressed as the mean ± s.e.m. *P < 0.05 and ***P < 0.001 compared with RANKL-treated WT.

Journal: The Journal of endocrinology

Article Title: Homer2 and Homer3 modulate RANKL-induced NFATc1 signaling in osteoclastogenesis and bone metabolism

doi: 10.1530/JOE-19-0123

Figure Lengend Snippet: RANKL-induced osteoclastogenesis is enhanced in Homer2/3 DKO BMMs. (A) RANKL-induced osteoclast differentiation in vitro in WT and Homer2/3 DKO BMMs (TRAP staining; scale bar, 50 μm). Columns show quantitative analysis of the number (middle) and the area (right) of TRAP-positive (TRAP+) multinucleated cells (MNCs; ≥3 nuclei) in WT and Homer2/3 DKO mice. The number and area of TRAP+ MNCs are significantly higher in Homer2/3 DKO mice (n = 4). (B) Pits area during osteoclastogenesis is higher in Homer2/3 DKO cells (n = 5). (C) Actin staining of TRAP+ MNCs in WT and Homer2/3 DKO cells (scale bar, 20 μm). The area of actin ring formation in TRAP+ MNCs during osteoclastogenesis is significantly higher in Homer2/3 DKO cells (n = 6). We normalized the data to the number and area of MNCs in RANKL-treated BMMs of WT mice. Results were expressed as the mean ± s.e.m. *P < 0.05 and ***P < 0.001 compared with RANKL-treated WT.

Article Snippet: Anti-Homer2, anti-Homer3 and anti-NFATc1 antibodies were obtained from Santa Cruz Biotechnology.

Techniques: In Vitro, Staining

RANKL-induced NFATc1 expression and translocation depend on the interaction of Homer proteins with NFATc1. (A) Expression levels of Homer proteins (45 kDa) and β-actin (42 kDa) in WT BMMs after RANKL stimulation. (B) Expression level of NFATc1 (approximately 90~110 kDa) and β-actin in WT and Homer2/3 DKO BMMs following RANKL stimulation. (C) Mean NFATc1 expression levels in WT and Homer2/3 DKO BMMs. We analyzed by densitometry the expression levels in experiments similar to those in B. Specifically, we observed that NFATc1’s expression levels between 48 and 72 h were significantly increased in Homer2/3 DKO cells (n = 6). Data were normalized to expression level in cells from WT mice and expressed as the mean ± s.e.m. (D) NFATc1 protein’s immunostaining in WT and Homer2/3 DKO BMMs post 72 h RANKL stimulation. Of note, NFATc1’s nuclear translocation was significantly higher in Homer2/3 DKO vs WT BMMs. Arrows indicate nuclear localized NFATc1. TO-PRO3 counterstaining was performed on the nuclei (scale bar, 20 μm). (E) Quantification of cell number with nuclear NFATc1. Homer2/3 DKO cells had a significant increase in NFATc1 translocation (n = 7). (F) Homer proteins and NFATc1 co-immunoprecipitation in cell lysates prepared from WT BMMs before and after 24-h RANKL stimulation. A reduced interaction of NFATc1 with Homer3 and Homer2 was found following RANKL stimulation. As a control, inhibition of calcineurin with cyclosporine A (CsA, 0.01 μg/mL) to inhibit NFATc1 dephosphorylation increased NFATc1’s interaction with Homer3 and Homer2 and reversed RANKL stimulation’s effect. *P < 0.05 and **P < 0.01 compared with WT.

Journal: The Journal of endocrinology

Article Title: Homer2 and Homer3 modulate RANKL-induced NFATc1 signaling in osteoclastogenesis and bone metabolism

doi: 10.1530/JOE-19-0123

Figure Lengend Snippet: RANKL-induced NFATc1 expression and translocation depend on the interaction of Homer proteins with NFATc1. (A) Expression levels of Homer proteins (45 kDa) and β-actin (42 kDa) in WT BMMs after RANKL stimulation. (B) Expression level of NFATc1 (approximately 90~110 kDa) and β-actin in WT and Homer2/3 DKO BMMs following RANKL stimulation. (C) Mean NFATc1 expression levels in WT and Homer2/3 DKO BMMs. We analyzed by densitometry the expression levels in experiments similar to those in B. Specifically, we observed that NFATc1’s expression levels between 48 and 72 h were significantly increased in Homer2/3 DKO cells (n = 6). Data were normalized to expression level in cells from WT mice and expressed as the mean ± s.e.m. (D) NFATc1 protein’s immunostaining in WT and Homer2/3 DKO BMMs post 72 h RANKL stimulation. Of note, NFATc1’s nuclear translocation was significantly higher in Homer2/3 DKO vs WT BMMs. Arrows indicate nuclear localized NFATc1. TO-PRO3 counterstaining was performed on the nuclei (scale bar, 20 μm). (E) Quantification of cell number with nuclear NFATc1. Homer2/3 DKO cells had a significant increase in NFATc1 translocation (n = 7). (F) Homer proteins and NFATc1 co-immunoprecipitation in cell lysates prepared from WT BMMs before and after 24-h RANKL stimulation. A reduced interaction of NFATc1 with Homer3 and Homer2 was found following RANKL stimulation. As a control, inhibition of calcineurin with cyclosporine A (CsA, 0.01 μg/mL) to inhibit NFATc1 dephosphorylation increased NFATc1’s interaction with Homer3 and Homer2 and reversed RANKL stimulation’s effect. *P < 0.05 and **P < 0.01 compared with WT.

Article Snippet: Anti-Homer2, anti-Homer3 and anti-NFATc1 antibodies were obtained from Santa Cruz Biotechnology.

Techniques: Expressing, Translocation Assay, Immunostaining, Immunoprecipitation, Inhibition, De-Phosphorylation Assay

Validation of PSD95-mVenus postsynaptic, VAMP2-mRFP presynaptic, and colocalized puncta. The majority of anti-VAMP2 and anti-Synapsin1 stained puncta were colocalized with endogenous VAMP2-mRFP puncta. Similarly, the majority of the antibody stained anti-PSD95 and anti-Homer2 puncta were colocalized with endogenous PSD95-mVenus puncta. ( a–c ) Presynaptic VAMP2-mRPF in singly transgenic mice was validated with immunocytochemistry stained ( a ) anti-VAMP2 and ( b ) anti-Syn1, ( c ) 92.1 ± 4.8% of stained VAMP2 puncta and 80.8 ± 3.9% of stained Syn1 puncta was colocalized with endogenous VAMP2-mRFP; ( d–f ) Postsynaptic PSD95-mVenus expression in singly transgenic mice was validated with immunocytochemistry stained ( d ) anti-PSD95 and ( e ) anti-Homer2, ( f ) 107.5 ± 4.5% of stained PSD95 puncta and 113.7 ± 6.2% of stained Homer2 puncta was colocalized with endogenous PSD95-mVenus (mean ± SD%, n = 3).

Journal: Scientific Reports

Article Title: Live Neuron High-Content Screening Reveals Synaptotoxic Activity in Alzheimer Mouse Model Homogenates

doi: 10.1038/s41598-020-60118-y

Figure Lengend Snippet: Validation of PSD95-mVenus postsynaptic, VAMP2-mRFP presynaptic, and colocalized puncta. The majority of anti-VAMP2 and anti-Synapsin1 stained puncta were colocalized with endogenous VAMP2-mRFP puncta. Similarly, the majority of the antibody stained anti-PSD95 and anti-Homer2 puncta were colocalized with endogenous PSD95-mVenus puncta. ( a–c ) Presynaptic VAMP2-mRPF in singly transgenic mice was validated with immunocytochemistry stained ( a ) anti-VAMP2 and ( b ) anti-Syn1, ( c ) 92.1 ± 4.8% of stained VAMP2 puncta and 80.8 ± 3.9% of stained Syn1 puncta was colocalized with endogenous VAMP2-mRFP; ( d–f ) Postsynaptic PSD95-mVenus expression in singly transgenic mice was validated with immunocytochemistry stained ( d ) anti-PSD95 and ( e ) anti-Homer2, ( f ) 107.5 ± 4.5% of stained PSD95 puncta and 113.7 ± 6.2% of stained Homer2 puncta was colocalized with endogenous PSD95-mVenus (mean ± SD%, n = 3).

Article Snippet: All cells were blocked with 5% bovine serum albumin and 0.2% Triton X-100 (Sigma-Aldrich) in PBS for 1 hour at room temperature, and then incubated with anti-Synaptobrevin 2, anti-Synapsin1, anti-PSD95, or anti-Homer2 (Synaptic Systems) antibodies at 1:500 in blocking solution overnight at 4 °C, subsequently washed in 0.1% Triton X-100 in PBS three times.

Techniques: Staining, Transgenic Assay, Immunocytochemistry, Expressing

Expression patterns of Homer1, Homer2 and Homer3 during early stages of tooth formation. ( A – C ) Representative immunostaining of frontal sections across the first molars at embryonic day 12.5 (E12.5) showing the distribution of Homer1 ( A ), Homer2 ( B ) and Homer3 ( C ) proteins (purple). All three Homer proteins are expressed in the dental placode (epithelium) and Homer1 protein is concentrated in puncta. The jaw mesenchyme, including the mesenchyme adjacent to the dental placode, expresses Homer2 and Homer3 proteins and the vascular endothelium shows weak Homer1, moderate Homer2 and strong Homer3 immunostaining. ( D – O ) Representative in situ hybridization ( D – F , J – L ) and immunohistochemistry ( G – I , M – O ) data in frontal ( D – F , J – O ) and parasagittal ( G – I ) sections across the first molars at E13.5 ( D – I ; bud stage) and E14.5 ( J – O ; cap stage) showing expression of Homer1 , Homer2 and Homer3 transcripts (brown) and Homer1, Homer2 and Homer3 proteins (purple) in the dental epithelium and dental mesenchyme. Cells of the dental epithelium exhibit diffuse Homer immunostaining of the cytoplasm and membranes as well as puncta enriched with Homer proteins. The vascular endothelium is enriched with Homer3 protein and mRNA and exhibits weak Homer1 and moderate Homer2 immunostaining. The dotted line in ( D – F ) and ( J – L ) highlights the junction between the dental epithelium and the dental mesenchyme. BV, blood vessels; DE, dental epithelium; DPl, dental placode; DM, dental mesenchyme. Scale bars: 50 µm ( A – O ).

Journal: International Journal of Molecular Sciences

Article Title: Distinct and Overlapping Expression Patterns of the Homer Family of Scaffolding Proteins and Their Encoding Genes in Developing Murine Cephalic Tissues

doi: 10.3390/ijms21041264

Figure Lengend Snippet: Expression patterns of Homer1, Homer2 and Homer3 during early stages of tooth formation. ( A – C ) Representative immunostaining of frontal sections across the first molars at embryonic day 12.5 (E12.5) showing the distribution of Homer1 ( A ), Homer2 ( B ) and Homer3 ( C ) proteins (purple). All three Homer proteins are expressed in the dental placode (epithelium) and Homer1 protein is concentrated in puncta. The jaw mesenchyme, including the mesenchyme adjacent to the dental placode, expresses Homer2 and Homer3 proteins and the vascular endothelium shows weak Homer1, moderate Homer2 and strong Homer3 immunostaining. ( D – O ) Representative in situ hybridization ( D – F , J – L ) and immunohistochemistry ( G – I , M – O ) data in frontal ( D – F , J – O ) and parasagittal ( G – I ) sections across the first molars at E13.5 ( D – I ; bud stage) and E14.5 ( J – O ; cap stage) showing expression of Homer1 , Homer2 and Homer3 transcripts (brown) and Homer1, Homer2 and Homer3 proteins (purple) in the dental epithelium and dental mesenchyme. Cells of the dental epithelium exhibit diffuse Homer immunostaining of the cytoplasm and membranes as well as puncta enriched with Homer proteins. The vascular endothelium is enriched with Homer3 protein and mRNA and exhibits weak Homer1 and moderate Homer2 immunostaining. The dotted line in ( D – F ) and ( J – L ) highlights the junction between the dental epithelium and the dental mesenchyme. BV, blood vessels; DE, dental epithelium; DPl, dental placode; DM, dental mesenchyme. Scale bars: 50 µm ( A – O ).

Article Snippet: The affinity-purified rabbit anti-Homer2 (product No. NBP1-85487) and the affinity-purified rabbit anti-Homer3 (product No. NBP2-32607) were from Novus Biologicals (Abingdon, UK).

Techniques: Expressing, Immunostaining, In Situ Hybridization, Immunohistochemistry

Expression patterns of Homer1, Homer2 and Homer3 during the bell stage of tooth development. ( A – F ) Representative frontal ( A ) and parasagittal ( B – F ) sections across developing first molars at 1 day postpartum (1 dpp) after in situ hybridization ( A – C ) and immunohistochemistry ( D – F ) for Homer1 ( A , D ), Homer2 ( B , E ) and Homer3 ( C , F ). ( A’ – F’ ) are magnified views of the boxed areas in ( A – F ). Odontoblasts and differentiating ameloblasts are enriched with Homer proteins (purple) and mRNAs (brown) as compared to the dental papilla, stellate reticulum and inner dental epithelium. Homer2 protein and mRNA are also expressed in the stratum intermedium. Homer proteins are concentrated in intracellular puncta in odontoblasts and differentiating ameloblasts as well as in cells of the stratum intermedium and inner dental epithelium. The endothelium of blood vessels in the stellate reticulum and dental mesenchyme is enriched with Homer3 mRNA and protein and exhibits weak and moderate immunostaining for Homer1 and Homer2, respectively. Homer proteins are also detectable in osteoblasts within the developing alveolar bone ( D – F ). BV, blood vessels; dAM, differentiating ameloblasts; DP, dental papilla; IDE, inner dental epithelium; Ob, osteoblasts; Od, odontoblasts; pOd, preodontoblasts; SI, stratum intermedium; SR, stellate reticulum. Scale bars: 200 µm ( A – F ) and 100 µm ( A’ – F’ ).

Journal: International Journal of Molecular Sciences

Article Title: Distinct and Overlapping Expression Patterns of the Homer Family of Scaffolding Proteins and Their Encoding Genes in Developing Murine Cephalic Tissues

doi: 10.3390/ijms21041264

Figure Lengend Snippet: Expression patterns of Homer1, Homer2 and Homer3 during the bell stage of tooth development. ( A – F ) Representative frontal ( A ) and parasagittal ( B – F ) sections across developing first molars at 1 day postpartum (1 dpp) after in situ hybridization ( A – C ) and immunohistochemistry ( D – F ) for Homer1 ( A , D ), Homer2 ( B , E ) and Homer3 ( C , F ). ( A’ – F’ ) are magnified views of the boxed areas in ( A – F ). Odontoblasts and differentiating ameloblasts are enriched with Homer proteins (purple) and mRNAs (brown) as compared to the dental papilla, stellate reticulum and inner dental epithelium. Homer2 protein and mRNA are also expressed in the stratum intermedium. Homer proteins are concentrated in intracellular puncta in odontoblasts and differentiating ameloblasts as well as in cells of the stratum intermedium and inner dental epithelium. The endothelium of blood vessels in the stellate reticulum and dental mesenchyme is enriched with Homer3 mRNA and protein and exhibits weak and moderate immunostaining for Homer1 and Homer2, respectively. Homer proteins are also detectable in osteoblasts within the developing alveolar bone ( D – F ). BV, blood vessels; dAM, differentiating ameloblasts; DP, dental papilla; IDE, inner dental epithelium; Ob, osteoblasts; Od, odontoblasts; pOd, preodontoblasts; SI, stratum intermedium; SR, stellate reticulum. Scale bars: 200 µm ( A – F ) and 100 µm ( A’ – F’ ).

Techniques: Expressing, In Situ Hybridization, Immunohistochemistry, Immunostaining

Expression patterns of Homer1, Homer2 and Homer3 during advanced stages of tooth formation. ( A – R ) Representative in situ hybridization ( A – C , G – I ) and immunohistochemistry ( D – F , J – R ) data showing the distribution patterns of Homer1 ( A , G ), Homer2 ( B , H ) and Homer3 ( C , I ) transcripts (brown) and Homer1 ( D , J , M , P ), Homer2 ( E , K , N , Q ) and Homer3 ( F , L , O , R ) proteins (purple) in developing teeth at 12 days postpartum (12 dpp). ( A – F ) Sections across incisors at the level of the secretory stage of enamel formation. Secretory ameloblasts and young odontoblasts (cells facing a thin layer of predentin/dentin matrices) express the three Homer proteins and their encoding genes. The asterisks in ( D , F ) mark an artefactual space due to detachment of secretory ameloblasts from dentin. ( G – L ) Sections at the level of enamel maturation showing expression of the three Homer proteins and their encoding genes in maturation-stage ameloblasts and in the papillary layer. ( M – R ) Sections across molars showing expression of Homer proteins in mature odontoblasts (cells that have produced a thick layer of predentin/dentin) ( M – O ) and in Hertwig’s epithelial root sheath ( P – R ). Secretory ameloblasts, maturation-stage ameloblasts, odontoblasts and cells of the papillary layer exhibit puncta enriched with Homer proteins ( D – F , J – O ). Note that the Homer-positive(+) puncta in young odontoblasts ( D – F ) are less prominent than the Homer+ puncta in mature odontoblasts ( M – O ) and that the Homer3+ puncta in subsets of cells of the dental pulp are apparently smaller than the Homer3+ puncta in mature odontoblasts ( O ). Odontoblasts in the developing roots express Homer proteins ( P – R ). The endothelium of vascular loops penetrating the papillary layer ( I , L ) and of blood vessels in the dental pulp and dental sac mesenchyme ( C , F , I , L , O , R ) expresses Homer3 mRNA and protein and exhibits weak Homer1 ( D , J , M , P ) and moderate Homer2 ( E , K , N , Q ) immunostaining. BV, blood vessels; DS, dental sac; HS, Hertwig’s epithelial root sheath; MA, maturation-stage ameloblasts; Od, odontoblasts; P, dental pulp; PD/D, predentin/dentin matrices; PL, papillary layer; SA, secretory ameloblasts; SI, stratum intermedium. Scale bars: 50 µm ( A – R ).

Journal: International Journal of Molecular Sciences

Article Title: Distinct and Overlapping Expression Patterns of the Homer Family of Scaffolding Proteins and Their Encoding Genes in Developing Murine Cephalic Tissues

doi: 10.3390/ijms21041264

Figure Lengend Snippet: Expression patterns of Homer1, Homer2 and Homer3 during advanced stages of tooth formation. ( A – R ) Representative in situ hybridization ( A – C , G – I ) and immunohistochemistry ( D – F , J – R ) data showing the distribution patterns of Homer1 ( A , G ), Homer2 ( B , H ) and Homer3 ( C , I ) transcripts (brown) and Homer1 ( D , J , M , P ), Homer2 ( E , K , N , Q ) and Homer3 ( F , L , O , R ) proteins (purple) in developing teeth at 12 days postpartum (12 dpp). ( A – F ) Sections across incisors at the level of the secretory stage of enamel formation. Secretory ameloblasts and young odontoblasts (cells facing a thin layer of predentin/dentin matrices) express the three Homer proteins and their encoding genes. The asterisks in ( D , F ) mark an artefactual space due to detachment of secretory ameloblasts from dentin. ( G – L ) Sections at the level of enamel maturation showing expression of the three Homer proteins and their encoding genes in maturation-stage ameloblasts and in the papillary layer. ( M – R ) Sections across molars showing expression of Homer proteins in mature odontoblasts (cells that have produced a thick layer of predentin/dentin) ( M – O ) and in Hertwig’s epithelial root sheath ( P – R ). Secretory ameloblasts, maturation-stage ameloblasts, odontoblasts and cells of the papillary layer exhibit puncta enriched with Homer proteins ( D – F , J – O ). Note that the Homer-positive(+) puncta in young odontoblasts ( D – F ) are less prominent than the Homer+ puncta in mature odontoblasts ( M – O ) and that the Homer3+ puncta in subsets of cells of the dental pulp are apparently smaller than the Homer3+ puncta in mature odontoblasts ( O ). Odontoblasts in the developing roots express Homer proteins ( P – R ). The endothelium of vascular loops penetrating the papillary layer ( I , L ) and of blood vessels in the dental pulp and dental sac mesenchyme ( C , F , I , L , O , R ) expresses Homer3 mRNA and protein and exhibits weak Homer1 ( D , J , M , P ) and moderate Homer2 ( E , K , N , Q ) immunostaining. BV, blood vessels; DS, dental sac; HS, Hertwig’s epithelial root sheath; MA, maturation-stage ameloblasts; Od, odontoblasts; P, dental pulp; PD/D, predentin/dentin matrices; PL, papillary layer; SA, secretory ameloblasts; SI, stratum intermedium. Scale bars: 50 µm ( A – R ).

Techniques: Expressing, In Situ Hybridization, Immunohistochemistry, Produced, Immunostaining

Expression patterns of Homer1, Homer2 and Homer3 in the developing forebrain and trigeminal ganglion. ( A – I ) Representative sections across the forebrain and trigeminal ganglion at embryonic day 14.5 (E14.5) after in situ hybridization revealing Homer transcripts ( A – C ) and immunostaining ( D – I ) for Homer proteins. Homer transcripts (brown) and Homer proteins (purple) are expressed in the trigeminal ganglion and in different regions of the forebrain, including the striatum, neocortex, thalamus, hypothalamus and in the hippocampal formation, and Homer proteins are enriched in differentiating fields and in the apical surface of the ventricular layer. ( G’ – I’ ) are magnified views of boxed areas in ( G – I ) showing that Homer1, Homer2 and Homer3 proteins are enriched in the apical surface of cells of the choroid plexus and that in these cells Homer1 and Homer3 are also concentrated in puncta. ( G’’ – I’’ ) are magnified views of boxed areas in ( G – I ) showing the distribution of Homer proteins in the anterior hypothalamic area and concentration of Homer1 and Homer2 in intracellular puncta. The three Homer proteins are also detectable in the apical surface of the hypothalamic neuroepithelium ( G’’ – H’’ ). ( G’’’ – I’’’ ) are magnified views of boxed areas in ( G – I ), showing that in other brain regions, the intracellular Homer-positive(+) puncta are less conspicuous than the Homer+ puncta in the anterior hypothalamic area. The endothelial lining of blood vessels in the brain and meninges expresses Homer3 transcripts and proteins ( C , F , I – I’’’ ) and exhibits weak Homer1 ( D , G – G’’’ ) and moderate Homer2 immunostaining ( E , H – H’’’ ). BV, blood vessels; Ch, choroid plexus; Cx, neocortex; Hc, hippocampal formation; Ht, hypothalamus; Hn, hypothalamic neuroepithelium; Lv, lateral ventricle; St, striatum; Th, thalamus; Vg, trigeminal ganglion; V3, third ventricle. Scale bars: 500 µm ( A – I ) and 50 µm ( G’ – I’’’ ).

Journal: International Journal of Molecular Sciences

Article Title: Distinct and Overlapping Expression Patterns of the Homer Family of Scaffolding Proteins and Their Encoding Genes in Developing Murine Cephalic Tissues

doi: 10.3390/ijms21041264

Figure Lengend Snippet: Expression patterns of Homer1, Homer2 and Homer3 in the developing forebrain and trigeminal ganglion. ( A – I ) Representative sections across the forebrain and trigeminal ganglion at embryonic day 14.5 (E14.5) after in situ hybridization revealing Homer transcripts ( A – C ) and immunostaining ( D – I ) for Homer proteins. Homer transcripts (brown) and Homer proteins (purple) are expressed in the trigeminal ganglion and in different regions of the forebrain, including the striatum, neocortex, thalamus, hypothalamus and in the hippocampal formation, and Homer proteins are enriched in differentiating fields and in the apical surface of the ventricular layer. ( G’ – I’ ) are magnified views of boxed areas in ( G – I ) showing that Homer1, Homer2 and Homer3 proteins are enriched in the apical surface of cells of the choroid plexus and that in these cells Homer1 and Homer3 are also concentrated in puncta. ( G’’ – I’’ ) are magnified views of boxed areas in ( G – I ) showing the distribution of Homer proteins in the anterior hypothalamic area and concentration of Homer1 and Homer2 in intracellular puncta. The three Homer proteins are also detectable in the apical surface of the hypothalamic neuroepithelium ( G’’ – H’’ ). ( G’’’ – I’’’ ) are magnified views of boxed areas in ( G – I ), showing that in other brain regions, the intracellular Homer-positive(+) puncta are less conspicuous than the Homer+ puncta in the anterior hypothalamic area. The endothelial lining of blood vessels in the brain and meninges expresses Homer3 transcripts and proteins ( C , F , I – I’’’ ) and exhibits weak Homer1 ( D , G – G’’’ ) and moderate Homer2 immunostaining ( E , H – H’’’ ). BV, blood vessels; Ch, choroid plexus; Cx, neocortex; Hc, hippocampal formation; Ht, hypothalamus; Hn, hypothalamic neuroepithelium; Lv, lateral ventricle; St, striatum; Th, thalamus; Vg, trigeminal ganglion; V3, third ventricle. Scale bars: 500 µm ( A – I ) and 50 µm ( G’ – I’’’ ).

Techniques: Expressing, In Situ Hybridization, Immunostaining, Concentration Assay

Expression patterns of Homer1, Homer2 and Homer3 in neuronal and non-neuronal cephalic tissues. ( A – I ) Representative sections across cephalic tissues at embryonic day 14.5 (E14.5) after in situ hybridization ( A – C ) and immunohistochemistry ( D – I ). ( A’ – C’ ) and ( D’ – F’ ) are magnified views of the boxed areas in ( A – C ) and ( D – F ), respectively. ( A – F’ ) The Homer1 , Homer2 and Homer3 mRNA expression patterns (brown) are consistent with the distribution patterns of their protein products (purple) in several cephalic structures, including the olfactory bulbs, retina, lens epithelium, olfactory epithelium, submandibular salivary glands, tooth, rugae palatinae, skeletal muscle and medial epithelial seam of the secondary palate. Note that Homer2 mRNA is enriched in developing muscles of the tongue (arrowheads in B’ ). The olfactory epithelium displays strong Homer2 ( B , E ) but moderate Homer1 ( A , D ) and Homer3 ( C , F ) hybridization signals and immunolabelling. The olfactory and trigeminal nerves show moderate Homer1 ( D , D’ ) and strong Homer2 ( E , E’ ) immunostaining. Homer3 immunoreactivity is strong in olfactory nerves and moderate in trigeminal nerves ( F , F’ ). ( G – I ) Homer1, Homer2 and Homer3 proteins are enriched in intracellular puncta in the epithelium of developing submandibular glands and the three Homer proteins are detectable in nerves within the glandular stroma. Note that vascular endothelium in cephalic tissues expresses Homer3 mRNA and protein and exhibits weak Homer1 and moderate Homer2 immunostaining. ( J – L ) Representative sections across submandibular salivary glands at 1 day postpartum (1 dpp) after immunostaining for Homer1 ( J ), Homer2 ( K ) and Homer3 ( L ). ( J’ – L’ ) are magnified views of the boxed areas in ( J – K ). In epithelial cells (acinar and tubular cells) of the glands Homer proteins show overlapping and distinct subcellular distribution patterns. Homer1 is enriched in the apical surface/membranes and in numerous intracellular puncta ( J , J’ ); Homer2 is concentrated in the apical surface/membranes and is also detectable in the cytoplasm ( K , K’ ); and Homer3 is detectable in the cytoplasm, cell membranes and puncta ( L , L’ ). The Homer2-positive(+) and Homer3+ puncta are less conspicuous than the Homer1+ puncta in glandular epithelial cells ( J – L’ ) and the Homer+ puncta in 1 dpp glands ( J – K ) are relatively smaller than the Homer+ puncta in E14.5 glands ( G – I ). BV, blood vessels; L, lens epithelium; MES, medial epithelial seam; Nf, nerve fibers (in salivary glands); n5, trigeminal nerve; OB, olfactory bulb; OE, olfactory epithelium; ON, olfactory nerve; R, retina; RP, rugae palatinae; SG, submandibular salivary glands; SM, skeletal muscle (masseter); T, tongue; To, tooth. Scale bars: 1mm ( A – F ), 200 µm ( A’ – F’ ), 50 µm ( G – L ) and 10 µm ( J’ – L’ ).

Journal: International Journal of Molecular Sciences

Article Title: Distinct and Overlapping Expression Patterns of the Homer Family of Scaffolding Proteins and Their Encoding Genes in Developing Murine Cephalic Tissues

doi: 10.3390/ijms21041264

Figure Lengend Snippet: Expression patterns of Homer1, Homer2 and Homer3 in neuronal and non-neuronal cephalic tissues. ( A – I ) Representative sections across cephalic tissues at embryonic day 14.5 (E14.5) after in situ hybridization ( A – C ) and immunohistochemistry ( D – I ). ( A’ – C’ ) and ( D’ – F’ ) are magnified views of the boxed areas in ( A – C ) and ( D – F ), respectively. ( A – F’ ) The Homer1 , Homer2 and Homer3 mRNA expression patterns (brown) are consistent with the distribution patterns of their protein products (purple) in several cephalic structures, including the olfactory bulbs, retina, lens epithelium, olfactory epithelium, submandibular salivary glands, tooth, rugae palatinae, skeletal muscle and medial epithelial seam of the secondary palate. Note that Homer2 mRNA is enriched in developing muscles of the tongue (arrowheads in B’ ). The olfactory epithelium displays strong Homer2 ( B , E ) but moderate Homer1 ( A , D ) and Homer3 ( C , F ) hybridization signals and immunolabelling. The olfactory and trigeminal nerves show moderate Homer1 ( D , D’ ) and strong Homer2 ( E , E’ ) immunostaining. Homer3 immunoreactivity is strong in olfactory nerves and moderate in trigeminal nerves ( F , F’ ). ( G – I ) Homer1, Homer2 and Homer3 proteins are enriched in intracellular puncta in the epithelium of developing submandibular glands and the three Homer proteins are detectable in nerves within the glandular stroma. Note that vascular endothelium in cephalic tissues expresses Homer3 mRNA and protein and exhibits weak Homer1 and moderate Homer2 immunostaining. ( J – L ) Representative sections across submandibular salivary glands at 1 day postpartum (1 dpp) after immunostaining for Homer1 ( J ), Homer2 ( K ) and Homer3 ( L ). ( J’ – L’ ) are magnified views of the boxed areas in ( J – K ). In epithelial cells (acinar and tubular cells) of the glands Homer proteins show overlapping and distinct subcellular distribution patterns. Homer1 is enriched in the apical surface/membranes and in numerous intracellular puncta ( J , J’ ); Homer2 is concentrated in the apical surface/membranes and is also detectable in the cytoplasm ( K , K’ ); and Homer3 is detectable in the cytoplasm, cell membranes and puncta ( L , L’ ). The Homer2-positive(+) and Homer3+ puncta are less conspicuous than the Homer1+ puncta in glandular epithelial cells ( J – L’ ) and the Homer+ puncta in 1 dpp glands ( J – K ) are relatively smaller than the Homer+ puncta in E14.5 glands ( G – I ). BV, blood vessels; L, lens epithelium; MES, medial epithelial seam; Nf, nerve fibers (in salivary glands); n5, trigeminal nerve; OB, olfactory bulb; OE, olfactory epithelium; ON, olfactory nerve; R, retina; RP, rugae palatinae; SG, submandibular salivary glands; SM, skeletal muscle (masseter); T, tongue; To, tooth. Scale bars: 1mm ( A – F ), 200 µm ( A’ – F’ ), 50 µm ( G – L ) and 10 µm ( J’ – L’ ).

Techniques: Expressing, In Situ Hybridization, Immunohistochemistry, Muscles, Hybridization, Immunostaining

Expression patterns of Homer1, Homer2 and Homer3 in the olfactory and respiratory mucosae and in the cochlea. ( A – O ) Representative immunohistochemistry ( A – F , J – O ) and in situ hybridization ( G – I ) data in sections across the nasal cavity ( A – F ) and cochlea ( G – O ) at 1 day postpartum (1 dpp) showing the distribution patterns of Homer proteins (purple) and their encoding genes (brown). ( A – C ) Homer1 ( A ), Homer2 ( B ) and Homer3 ( C ) proteins are enriched in the apical surface (likely cilia of olfactory neurons and microvilli of supporting cells) of cells of the olfactory epithelium and are also detectable in intracellular puncta. Dendrites (arrowheads in A – C ) and axons, the latter forming the olfactory nerves, are Homer1-positive(+), Homer2+ and Homer3+, indicating that some of the Homer+ cells in the olfactory epithelium are olfactory neurons. ( D – F ) The respiratory epithelium and nasal glands express Homer1 ( D ), Homer2 ( E ) and Homer3 ( F ) proteins. In cells of the respiratory epithelium the Homer1+ puncta are more prominent than the Homer2+ and Homer3+ puncta. In nasal gland acinar cells Homer1 is enriched in the apical membrane and in puncta, Homer2 is readily detectable in cell membranes and in the cytoplasm and Homer3+ puncta are detectable in subsets of acinar cells. Note that the Homer1+ puncta in nasal gland acinar cells are small compared to the Homer1+ puncta in cells of the respiratory epithelium ( D ). The endothelial lining of blood vessels in the olfactory ( A – C ) and respiratory ( D – F ) mucosae shows weak Homer1, moderate Homer2 and strong Homer3 immunolabelling. ( G – O ) Expression patterns of Homer transcripts ( G – I ) and their protein products ( J – O ) in the cochlea. Homer1 ( G ), Homer2 ( H ) and Homer3 ( I ) mRNAs are detectable in various cells of the developing organ of Corti, including inner (IHC) and outer (OHC) hair cells as well as in cells forming the stria vascularis, basilar membrane and Reissner’s membrane ( G – I ). Homer1 and Homer2 transcripts are enriched in IHC and OHC ( G , H ). Homer1 ( J ), Homer2 ( K ) and Homer3 ( L ) proteins show overlapping but also distinct subcellular localization in cells of the organ of Corti. In IHC and OHC Homer1 and Homer2 are enriched in the apical surface (likely in stereocilia) and in perinuclear puncta and are also detectable in the cytoplasm. By contrast, Homer3 protein is detectable in puncta at the apical surface of IHC and OHC and in perinuclear puncta in IHC. Other cells of the organ of Corti, including cells of the greater epithelial ridge (GER), cells of Claudius and Deiter’s cells, exhibit Homer1+ and Homer3+ perinuclear puncta and show moderate Homer1, very weak Homer2 and weak Homer3 immunostaining in the cytoplasm. Homer1 is also enriched in the apical (endolymphatic) surface of the GER. Cells of the stria vascularis and Reissner’s membrane exhibit Homer1+ and Homer3+ puncta and cytoplasmic Homer2 immunostaining. Note that in IHC and OHC the Homer1+ puncta are large as compared to the Homer2+ and Homer3+ puncta and that the Homer1+ puncta in IHC and OHC are large compared to the Homer1+ puncta in the cells of Claudius and in cells of the GER and stria vascularis. ( M – O ) Neurons of the cochlear spiral ganglion show diffuse cytoplasmic immunostaining for Homer1 ( M ), Homer2 ( N ) and Homer3 ( O ) and are enriched with Homer1+ and Homer3+ puncta. Note that the vascular endothelium in the cochlea exhibits weak Homer1, moderate Homer2 and strong Homer3 immunolabelling ( J – O ). BM, basilar membrane; BV, blood vessels; Cc, cells of Claudius; Dc, Deiter’s cells; GER, greater epithelial ridge; IHC, inner hair cells; NG, nasal glands; OE, olfactory epithelium; ON, olfactory nerve; RE, respiratory epithelium; RM, Reissner’s membrane; Sg, spiral ganglion; SV, stria vascularis. Scale bars: 100 µm ( A – C ) and 50 µm ( D – O ).

Journal: International Journal of Molecular Sciences

Article Title: Distinct and Overlapping Expression Patterns of the Homer Family of Scaffolding Proteins and Their Encoding Genes in Developing Murine Cephalic Tissues

doi: 10.3390/ijms21041264

Figure Lengend Snippet: Expression patterns of Homer1, Homer2 and Homer3 in the olfactory and respiratory mucosae and in the cochlea. ( A – O ) Representative immunohistochemistry ( A – F , J – O ) and in situ hybridization ( G – I ) data in sections across the nasal cavity ( A – F ) and cochlea ( G – O ) at 1 day postpartum (1 dpp) showing the distribution patterns of Homer proteins (purple) and their encoding genes (brown). ( A – C ) Homer1 ( A ), Homer2 ( B ) and Homer3 ( C ) proteins are enriched in the apical surface (likely cilia of olfactory neurons and microvilli of supporting cells) of cells of the olfactory epithelium and are also detectable in intracellular puncta. Dendrites (arrowheads in A – C ) and axons, the latter forming the olfactory nerves, are Homer1-positive(+), Homer2+ and Homer3+, indicating that some of the Homer+ cells in the olfactory epithelium are olfactory neurons. ( D – F ) The respiratory epithelium and nasal glands express Homer1 ( D ), Homer2 ( E ) and Homer3 ( F ) proteins. In cells of the respiratory epithelium the Homer1+ puncta are more prominent than the Homer2+ and Homer3+ puncta. In nasal gland acinar cells Homer1 is enriched in the apical membrane and in puncta, Homer2 is readily detectable in cell membranes and in the cytoplasm and Homer3+ puncta are detectable in subsets of acinar cells. Note that the Homer1+ puncta in nasal gland acinar cells are small compared to the Homer1+ puncta in cells of the respiratory epithelium ( D ). The endothelial lining of blood vessels in the olfactory ( A – C ) and respiratory ( D – F ) mucosae shows weak Homer1, moderate Homer2 and strong Homer3 immunolabelling. ( G – O ) Expression patterns of Homer transcripts ( G – I ) and their protein products ( J – O ) in the cochlea. Homer1 ( G ), Homer2 ( H ) and Homer3 ( I ) mRNAs are detectable in various cells of the developing organ of Corti, including inner (IHC) and outer (OHC) hair cells as well as in cells forming the stria vascularis, basilar membrane and Reissner’s membrane ( G – I ). Homer1 and Homer2 transcripts are enriched in IHC and OHC ( G , H ). Homer1 ( J ), Homer2 ( K ) and Homer3 ( L ) proteins show overlapping but also distinct subcellular localization in cells of the organ of Corti. In IHC and OHC Homer1 and Homer2 are enriched in the apical surface (likely in stereocilia) and in perinuclear puncta and are also detectable in the cytoplasm. By contrast, Homer3 protein is detectable in puncta at the apical surface of IHC and OHC and in perinuclear puncta in IHC. Other cells of the organ of Corti, including cells of the greater epithelial ridge (GER), cells of Claudius and Deiter’s cells, exhibit Homer1+ and Homer3+ perinuclear puncta and show moderate Homer1, very weak Homer2 and weak Homer3 immunostaining in the cytoplasm. Homer1 is also enriched in the apical (endolymphatic) surface of the GER. Cells of the stria vascularis and Reissner’s membrane exhibit Homer1+ and Homer3+ puncta and cytoplasmic Homer2 immunostaining. Note that in IHC and OHC the Homer1+ puncta are large as compared to the Homer2+ and Homer3+ puncta and that the Homer1+ puncta in IHC and OHC are large compared to the Homer1+ puncta in the cells of Claudius and in cells of the GER and stria vascularis. ( M – O ) Neurons of the cochlear spiral ganglion show diffuse cytoplasmic immunostaining for Homer1 ( M ), Homer2 ( N ) and Homer3 ( O ) and are enriched with Homer1+ and Homer3+ puncta. Note that the vascular endothelium in the cochlea exhibits weak Homer1, moderate Homer2 and strong Homer3 immunolabelling ( J – O ). BM, basilar membrane; BV, blood vessels; Cc, cells of Claudius; Dc, Deiter’s cells; GER, greater epithelial ridge; IHC, inner hair cells; NG, nasal glands; OE, olfactory epithelium; ON, olfactory nerve; RE, respiratory epithelium; RM, Reissner’s membrane; Sg, spiral ganglion; SV, stria vascularis. Scale bars: 100 µm ( A – C ) and 50 µm ( D – O ).

Techniques: Expressing, Immunohistochemistry, In Situ Hybridization, Membrane, Immunostaining

Expression patterns of Homer1, Homer2 and Homer3 in the tongue and alveolar bone. ( A – O ) Representative in situ hybridization ( A – C , G – I ) and immunohistochemistry ( D – F , J – O ) data showing the distribution patterns of Homer transcripts (brown) and Homer proteins (purple). ( A – F ) Sections across the developing tongue at embryonic day 14.5 (E14.5). Homer1 mRNA ( A ) and Homer1 protein ( D ) are enriched in developing taste buds and are detectable in the lingual epithelium (LE), developing muscles of the tongue (arrows) and in the lingual mesenchyme (LM). Homer2 mRNA ( B ) and Homer2 protein ( E ) are expressed in the LE, including in developing taste buds and are enriched in developing muscle of the tongue (arrows). Homer2 protein is also detectable in nerves innervating developing fungiform papillae (arrowhead in E ). Homer3 mRNA ( C ) and Homer3 protein ( F ) are expressed in the LE, LM and in the vascular endothelium, whereas developing taste buds are virtually devoid of Homer3 immunostaining. ( G – L ) Sections across the tongue at 1 day postpartum (1 dpp). Homer1 mRNA ( G ) and Homer1 protein ( J ) are enriched in nerves innervating fungiform papillae (arrowheads in G , J ) and in taste buds. The LE and taste buds express Homer2 mRNA ( H ) and Homer2 protein ( K ) and exhibit weak hybridization signals ( I ) and immunostaining (L ) for Homer3. By contrast, Homer3 transcripts and Homer3 protein are readily detectable in the vascular endothelium. ( M – O ) sections across the alveolar bone at 12 dpp. Homer1 ( M ), Homer2 ( N ) and Homer3 ( O ) proteins are expressed in osteoblasts (arrows in M , N , O ) and osteoclasts and Homer2 and Homer3 but not Homer1, are also detectable in osteocytes (arrowheads in M , N , O ). Note that in bone cells Homer proteins are enriched in puncta. BV, blood vessels; LE, lingual epithelium; LM, lingual mesenchyme; OC, osteoclast; TB, taste bud; SM, muscles of the tongue. Scale bars: 50 µm ( A – O ).

Journal: International Journal of Molecular Sciences

Article Title: Distinct and Overlapping Expression Patterns of the Homer Family of Scaffolding Proteins and Their Encoding Genes in Developing Murine Cephalic Tissues

doi: 10.3390/ijms21041264

Figure Lengend Snippet: Expression patterns of Homer1, Homer2 and Homer3 in the tongue and alveolar bone. ( A – O ) Representative in situ hybridization ( A – C , G – I ) and immunohistochemistry ( D – F , J – O ) data showing the distribution patterns of Homer transcripts (brown) and Homer proteins (purple). ( A – F ) Sections across the developing tongue at embryonic day 14.5 (E14.5). Homer1 mRNA ( A ) and Homer1 protein ( D ) are enriched in developing taste buds and are detectable in the lingual epithelium (LE), developing muscles of the tongue (arrows) and in the lingual mesenchyme (LM). Homer2 mRNA ( B ) and Homer2 protein ( E ) are expressed in the LE, including in developing taste buds and are enriched in developing muscle of the tongue (arrows). Homer2 protein is also detectable in nerves innervating developing fungiform papillae (arrowhead in E ). Homer3 mRNA ( C ) and Homer3 protein ( F ) are expressed in the LE, LM and in the vascular endothelium, whereas developing taste buds are virtually devoid of Homer3 immunostaining. ( G – L ) Sections across the tongue at 1 day postpartum (1 dpp). Homer1 mRNA ( G ) and Homer1 protein ( J ) are enriched in nerves innervating fungiform papillae (arrowheads in G , J ) and in taste buds. The LE and taste buds express Homer2 mRNA ( H ) and Homer2 protein ( K ) and exhibit weak hybridization signals ( I ) and immunostaining (L ) for Homer3. By contrast, Homer3 transcripts and Homer3 protein are readily detectable in the vascular endothelium. ( M – O ) sections across the alveolar bone at 12 dpp. Homer1 ( M ), Homer2 ( N ) and Homer3 ( O ) proteins are expressed in osteoblasts (arrows in M , N , O ) and osteoclasts and Homer2 and Homer3 but not Homer1, are also detectable in osteocytes (arrowheads in M , N , O ). Note that in bone cells Homer proteins are enriched in puncta. BV, blood vessels; LE, lingual epithelium; LM, lingual mesenchyme; OC, osteoclast; TB, taste bud; SM, muscles of the tongue. Scale bars: 50 µm ( A – O ).

Techniques: Expressing, In Situ Hybridization, Immunohistochemistry, Muscles, Immunostaining, Hybridization

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homer2 (Synaptic Systems)

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1) Product Images from "Evidence for Phosphorylation-Dependent, Dynamic, Regulation of mGlu5 and Homer2 in Expression of Cocaine Aversion in Mice"

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