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polyclonal goat antibody against extracellular chl1 epitopes (R&D Systems)

Name: polyclonal goat antibody against extracellular chl1 epitopes
Brand: R&D Systems
Rating: 94 (35 reviews)

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R&D Systems polyclonal goat antibody against extracellular chl1 epitopes

FIGURE 1 Association of <t>CHL1</t> and DRD2. Brain extracts from CHL1+/+ (A-C) or CHL1−/− (C) mice (input) were subjected to immunoprecipitation (IP) with anti-CHL1 (A, C), anti-NCAM (A), anti-DRD2 (B), or non-immune control antibodies (A, B) and to Western blot analysis (WB) with anti-DRD2 (A, C) or anti-CHL1 (B) antibodies. D, CHL1-Fc and NCAM-Fc were incubated with a brain extract from CHL1+/+ mice (input) followed by pull-down (PD) with Protein A beads and by Western blot analysis (WB) with anti-DRD2 antibody. A-D, Representative Western blots from three independent experiments are shown. Lanes not adjacent to each other but derived from the same blot are separated by a vertical line. Aliquots of brain extracts not subjected to immunoprecipitation or pull-down experiments are designated as input

Polyclonal Goat Antibody Against Extracellular Chl1 Epitopes, supplied by R&D Systems, used in various techniques. Bioz Stars score: 94/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/polyclonal goat antibody against extracellular chl1 epitopes/product/R&D Systems
Average 94 stars, based on 35 article reviews

polyclonal goat antibody against extracellular chl1 epitopes - by Bioz Stars, 2026-03

94/100 stars

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1) Product Images from "Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform"

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

Journal: The FASEB Journal

doi: 10.1096/fj.201900577rrrr

FIGURE 1 Association of CHL1 and DRD2. Brain extracts from CHL1+/+ (A-C) or CHL1−/− (C) mice (input) were subjected to immunoprecipitation (IP) with anti-CHL1 (A, C), anti-NCAM (A), anti-DRD2 (B), or non-immune control antibodies (A, B) and to Western blot analysis (WB) with anti-DRD2 (A, C) or anti-CHL1 (B) antibodies. D, CHL1-Fc and NCAM-Fc were incubated with a brain extract from CHL1+/+ mice (input) followed by pull-down (PD) with Protein A beads and by Western blot analysis (WB) with anti-DRD2 antibody. A-D, Representative Western blots from three independent experiments are shown. Lanes not adjacent to each other but derived from the same blot are separated by a vertical line. Aliquots of brain extracts not subjected to immunoprecipitation or pull-down experiments are designated as input

Figure Legend Snippet: FIGURE 1 Association of CHL1 and DRD2. Brain extracts from CHL1+/+ (A-C) or CHL1−/− (C) mice (input) were subjected to immunoprecipitation (IP) with anti-CHL1 (A, C), anti-NCAM (A), anti-DRD2 (B), or non-immune control antibodies (A, B) and to Western blot analysis (WB) with anti-DRD2 (A, C) or anti-CHL1 (B) antibodies. D, CHL1-Fc and NCAM-Fc were incubated with a brain extract from CHL1+/+ mice (input) followed by pull-down (PD) with Protein A beads and by Western blot analysis (WB) with anti-DRD2 antibody. A-D, Representative Western blots from three independent experiments are shown. Lanes not adjacent to each other but derived from the same blot are separated by a vertical line. Aliquots of brain extracts not subjected to immunoprecipitation or pull-down experiments are designated as input

Techniques Used: Immunoprecipitation, Control, Western Blot, Incubation, Derivative Assay

FIGURE 2 Binding of CHL1-Fc to the first extracellular loop of DRD2. Synthetic peptides comprising the first (A), second (B), or third (C) extracellular DRD2 loop or the DRD2 N-terminus (D) were coated as substrate and incubated with increasing concentrations of CHL1-Fc or NCAM-Fc. Binding was determined by ELISA using horseradish peroxidase-conjugated anti-Fc antibodies. Mean values ± standard error of the mean from three independent experiments carried out in triplicates are shown

Figure Legend Snippet: FIGURE 2 Binding of CHL1-Fc to the first extracellular loop of DRD2. Synthetic peptides comprising the first (A), second (B), or third (C) extracellular DRD2 loop or the DRD2 N-terminus (D) were coated as substrate and incubated with increasing concentrations of CHL1-Fc or NCAM-Fc. Binding was determined by ELISA using horseradish peroxidase-conjugated anti-Fc antibodies. Mean values ± standard error of the mean from three independent experiments carried out in triplicates are shown

Techniques Used: Binding Assay, Incubation, Enzyme-linked Immunosorbent Assay

FIGURE 3 Binding of CHL1-Fc to DRD2 at the cell surface of transfected HEK293 cells. Live HEK293 cell expressing DRD2-S or DRD2-L were incubated with CHL1-Fc. After fixation, cells were incubated with goat anti-CHL1 antibody and mouse anti-DRD2 antibody against the extracellular N-terminus. After washing, cells were stained with Cy2-conjugated anti-mouse (green) and Cy3- conjugated anti-goat (red) antibodies. Areas indicated by white dashed lines and arrows show areas with CHL1-immunopositive signals, which partially overlap with intense DRD2-immunopositive staining. Arrowheads indicate nuclei of CHL1- and DRD2-immunonegative untransfected cells. The experiment was performed two times. Scale bar: 10 µm

Figure Legend Snippet: FIGURE 3 Binding of CHL1-Fc to DRD2 at the cell surface of transfected HEK293 cells. Live HEK293 cell expressing DRD2-S or DRD2-L were incubated with CHL1-Fc. After fixation, cells were incubated with goat anti-CHL1 antibody and mouse anti-DRD2 antibody against the extracellular N-terminus. After washing, cells were stained with Cy2-conjugated anti-mouse (green) and Cy3- conjugated anti-goat (red) antibodies. Areas indicated by white dashed lines and arrows show areas with CHL1-immunopositive signals, which partially overlap with intense DRD2-immunopositive staining. Arrowheads indicate nuclei of CHL1- and DRD2-immunonegative untransfected cells. The experiment was performed two times. Scale bar: 10 µm

Techniques Used: Binding Assay, Transfection, Expressing, Incubation, Staining

FIGURE 4 Interaction of CHL1 with DRD2-S and DRD2-L in transfected HEK293 cells. HEK293 cells were transfected with pCAG- DRD2-S, pCAG-DRD2-L, pCAG-DRD2-S/CHL1, or pCAG-DRD2-L/CHL1 to express DRD2-S or DRD2-L alone or together with CHL1 (DRD2-S/CHL1; DRD2-L/CHL1). Transfected cells were subjected to proximity ligation assay with anti-CHL1 and anti-DRD2 antibodies. A, Representative images at low (left and middle panel) and high magnification (right panels) from two independent experiments performed in duplicates are shown and red spots indicate close interaction of CHL1 with DRD2-S and DRD2-L. Scale bars: 10 µm. B, Red spots were counted in HEK293 cells co-expressing DRD2-S or DRD2-L and CHL1 (DRD2-S/CHL1; DRD2-L/CHL1). Numbers of red spots per cell from two independent experiments performed in duplicates are shown (*P < .001; two-tailed Student's t test). C, Representative images taken with and without phase contrast are shown. Red spots are located predominantly at the cell surface (arrows) and indicate the close interaction between CHL1 and DRD2-S at the cell surface

Figure Legend Snippet: FIGURE 4 Interaction of CHL1 with DRD2-S and DRD2-L in transfected HEK293 cells. HEK293 cells were transfected with pCAG- DRD2-S, pCAG-DRD2-L, pCAG-DRD2-S/CHL1, or pCAG-DRD2-L/CHL1 to express DRD2-S or DRD2-L alone or together with CHL1 (DRD2-S/CHL1; DRD2-L/CHL1). Transfected cells were subjected to proximity ligation assay with anti-CHL1 and anti-DRD2 antibodies. A, Representative images at low (left and middle panel) and high magnification (right panels) from two independent experiments performed in duplicates are shown and red spots indicate close interaction of CHL1 with DRD2-S and DRD2-L. Scale bars: 10 µm. B, Red spots were counted in HEK293 cells co-expressing DRD2-S or DRD2-L and CHL1 (DRD2-S/CHL1; DRD2-L/CHL1). Numbers of red spots per cell from two independent experiments performed in duplicates are shown (*P < .001; two-tailed Student's t test). C, Representative images taken with and without phase contrast are shown. Red spots are located predominantly at the cell surface (arrows) and indicate the close interaction between CHL1 and DRD2-S at the cell surface

Techniques Used: Transfection, Proximity Ligation Assay, Expressing, Two Tailed Test

FIGURE 5 Quinpirole reduces the cell surface level of DRD2-S in the absence of CHL1. A-C, HEK293 expressing DRD2-S (A) or DRD2-L (B) alone or co-expressing DRD2-S and CHL1 (DRD2-S/CHL1) (A, C) or DRD2-L and CHL1 (DRD2-L/CHL1) (B, C) were incubated with (+quin) or without (−quin) quinpirole followed by cell surface biotinylation, isolation of biotinylated proteins and Western blot analysis (WB) of the biotinylated proteins (surface) and the cell lysates (total) with anti-DRD2 (A, B) and anti-CHL1 (C) antibodies. The anti-GAPDH antibody was used to control loading (A, B). Total levels indicate the levels of CHL1 and DRD2 in cell lysates before isolation of biotinylated proteins, and cell surface levels represent biotinylated DRD2 after isolation of biotinylated proteins. A-C, Shown are representative blots from three independent experiments. D, E, Cell surface levels of DRD2-S and DRD2-L and total DRD2-S and DRD2-L levels in the cell lysates were determined, cell surface levels were normalized to total levels and the ratio of relative cell surface level after quinpirole treatment (+quin) and relative cell surface level after treatment without quinpirole (−quin) was calculated. Means + standard deviation from three independent experiments are shown for the ratios of the cell surface levels with quinpirole treatment relative to the cell surface levels without quinpirole treatment (D) and for the cell surface levels without quinpirole treatment relative to the total levels without quinpirole treatment (E) (Kruskal-Wallis test with post-hoc Dunn´s multiple comparison test; **P < .01; ns: not significant)

Figure Legend Snippet: FIGURE 5 Quinpirole reduces the cell surface level of DRD2-S in the absence of CHL1. A-C, HEK293 expressing DRD2-S (A) or DRD2-L (B) alone or co-expressing DRD2-S and CHL1 (DRD2-S/CHL1) (A, C) or DRD2-L and CHL1 (DRD2-L/CHL1) (B, C) were incubated with (+quin) or without (−quin) quinpirole followed by cell surface biotinylation, isolation of biotinylated proteins and Western blot analysis (WB) of the biotinylated proteins (surface) and the cell lysates (total) with anti-DRD2 (A, B) and anti-CHL1 (C) antibodies. The anti-GAPDH antibody was used to control loading (A, B). Total levels indicate the levels of CHL1 and DRD2 in cell lysates before isolation of biotinylated proteins, and cell surface levels represent biotinylated DRD2 after isolation of biotinylated proteins. A-C, Shown are representative blots from three independent experiments. D, E, Cell surface levels of DRD2-S and DRD2-L and total DRD2-S and DRD2-L levels in the cell lysates were determined, cell surface levels were normalized to total levels and the ratio of relative cell surface level after quinpirole treatment (+quin) and relative cell surface level after treatment without quinpirole (−quin) was calculated. Means + standard deviation from three independent experiments are shown for the ratios of the cell surface levels with quinpirole treatment relative to the cell surface levels without quinpirole treatment (D) and for the cell surface levels without quinpirole treatment relative to the total levels without quinpirole treatment (E) (Kruskal-Wallis test with post-hoc Dunn´s multiple comparison test; **P < .01; ns: not significant)

Techniques Used: Expressing, Incubation, Isolation, Western Blot, Control, Standard Deviation, Comparison

FIGURE 6 Quinpirole-induced internalization of DRD2-S is reduced in the presence of CHL1. A, B, HEK293 expressing DRD2-S or co- expressing DRD2-S and CHL1 (DRD2-S/CHL1) were incubated with anti-DRD2 antibody against the extracellular N-terminus. After removal of unbound antibodies, cells were stimulated without (−quin) or with (+quin) quinpirole, fixed and incubated with Cy-3-conjugated secondary antibody. After removal of unbound secondary antibodies, cells were permeabilized and incubated with Cy-2-conjugated secondary antibody and analyzed by confocal microscopy. Cy-3-conjugated secondary antibodies (red) indicate non-internalized DRD2-bound anti-DRD2 antibodies at the cell surface and Cy-2-conjugated secondary antibodies (green) label internalized DRD2-bound anti-DRD2 antibodies. A, Representative images of HEK293 expressing DRD2-S after quinpirole treatment show surface DRD2 (red) and internalized DRD2 (green). Scale bar: 10 µm. B, Integrated densities of internalized and cell surface receptor-bound antibodies were determined and integrated densities of internalized receptor-bound antibodies were normalized to the total integrated densities (sum of integrated densities of internalized and cell surface receptor-bound antibodies). Box plots for the relative levels of internalized DRD2 are shown (**P < .01, ***P < .001; One-way ANOVA with post-hoc Student Newman- Keul's test). The experiment was performed two times in duplicates

Figure Legend Snippet: FIGURE 6 Quinpirole-induced internalization of DRD2-S is reduced in the presence of CHL1. A, B, HEK293 expressing DRD2-S or co- expressing DRD2-S and CHL1 (DRD2-S/CHL1) were incubated with anti-DRD2 antibody against the extracellular N-terminus. After removal of unbound antibodies, cells were stimulated without (−quin) or with (+quin) quinpirole, fixed and incubated with Cy-3-conjugated secondary antibody. After removal of unbound secondary antibodies, cells were permeabilized and incubated with Cy-2-conjugated secondary antibody and analyzed by confocal microscopy. Cy-3-conjugated secondary antibodies (red) indicate non-internalized DRD2-bound anti-DRD2 antibodies at the cell surface and Cy-2-conjugated secondary antibodies (green) label internalized DRD2-bound anti-DRD2 antibodies. A, Representative images of HEK293 expressing DRD2-S after quinpirole treatment show surface DRD2 (red) and internalized DRD2 (green). Scale bar: 10 µm. B, Integrated densities of internalized and cell surface receptor-bound antibodies were determined and integrated densities of internalized receptor-bound antibodies were normalized to the total integrated densities (sum of integrated densities of internalized and cell surface receptor-bound antibodies). Box plots for the relative levels of internalized DRD2 are shown (**P < .01, ***P < .001; One-way ANOVA with post-hoc Student Newman- Keul's test). The experiment was performed two times in duplicates

Techniques Used: Expressing, Incubation, Confocal Microscopy, Cell Surface Receptor Assay

FIGURE 7 Co-immunostaining of CHL1 and DRD2 in the striatum. Tissue sections from 12- to 18-week-old CHL1+/+ (A, C) and CHL1−/− (B) mice were subjected to immunostaining using goat anti-CHL1 and mouse anti-DRD2 antibodies and Cy-3-conjugated anti- mouse and Cy-2-conjugated anti-goat secondary antibodies. Nuclei are stained with DAPI. Representative image of immunofluorescence staining for DAPI (blue), CHL1 (green), and DRD2 (red) are shown and yellow signals show co- localizations. C, Close-ups of two regions indicated by boxes in (A). A-C, Scale bars: 20 µm. Three independent experiments were performed with different sets of animals

Figure Legend Snippet: FIGURE 7 Co-immunostaining of CHL1 and DRD2 in the striatum. Tissue sections from 12- to 18-week-old CHL1+/+ (A, C) and CHL1−/− (B) mice were subjected to immunostaining using goat anti-CHL1 and mouse anti-DRD2 antibodies and Cy-3-conjugated anti- mouse and Cy-2-conjugated anti-goat secondary antibodies. Nuclei are stained with DAPI. Representative image of immunofluorescence staining for DAPI (blue), CHL1 (green), and DRD2 (red) are shown and yellow signals show co- localizations. C, Close-ups of two regions indicated by boxes in (A). A-C, Scale bars: 20 µm. Three independent experiments were performed with different sets of animals

Techniques Used: Immunostaining, Staining, Immunofluorescence

FIGURE 8 Co-localization of CHL1 and DRD2 in the striatum. Tissue sections from 12- to 18-week-old CHL1+/+ and CHL1−/− mice were analyzed by proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies. Nuclei are stained with DAPI (blue). Representative images are shown at low (left and middle panel) and high (right panel) magnifications. Red spots indicate close molecular interaction of CHL1 with DRD2 in CHL1+/+ mice. CHL1−/− mice served as controls. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals

Figure Legend Snippet: FIGURE 8 Co-localization of CHL1 and DRD2 in the striatum. Tissue sections from 12- to 18-week-old CHL1+/+ and CHL1−/− mice were analyzed by proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies. Nuclei are stained with DAPI (blue). Representative images are shown at low (left and middle panel) and high (right panel) magnifications. Red spots indicate close molecular interaction of CHL1 with DRD2 in CHL1+/+ mice. CHL1−/− mice served as controls. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals

Techniques Used: Proximity Ligation Assay, Staining

FIGURE 9 Interaction of CHL1 and DRD2 on TH- and DARP32-positive neurons in striatal sections. Proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies was combined with immunostaining using rabbit anti-DARPP32 (A) or anti-TH (B) antibodies to analyze tissue sections from 12- to 18-week-old CHL1+/+ mice. Nuclei are stained with DAPI (blue). Representative images are shown. Close- ups of two regions (without DAPI staining) are indicated by boxes and arrowheads indicate red spots indicating close molecular interaction of CHL1 with DRD2. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals

Figure Legend Snippet: FIGURE 9 Interaction of CHL1 and DRD2 on TH- and DARP32-positive neurons in striatal sections. Proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies was combined with immunostaining using rabbit anti-DARPP32 (A) or anti-TH (B) antibodies to analyze tissue sections from 12- to 18-week-old CHL1+/+ mice. Nuclei are stained with DAPI (blue). Representative images are shown. Close- ups of two regions (without DAPI staining) are indicated by boxes and arrowheads indicate red spots indicating close molecular interaction of CHL1 with DRD2. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals

Techniques Used: Proximity Ligation Assay, Immunostaining, Staining

FIGURE 10 Interaction of CHL1 and DRD2 on TH- and DARP32-positive cells in cultures of ventral midbrain and striatum. Cultures of ventral midbrain (A) or striatum (B) were analyzed by proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies combined with immunofluorescent staining using rabbit anti-TH or anti-DARPP32 antibodies. Nuclei are stained with DAPI (blue). Representative images of different cells are shown. Red spots indicate close molecular interaction between CHL1 and DRD2. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals

Figure Legend Snippet: FIGURE 10 Interaction of CHL1 and DRD2 on TH- and DARP32-positive cells in cultures of ventral midbrain and striatum. Cultures of ventral midbrain (A) or striatum (B) were analyzed by proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies combined with immunofluorescent staining using rabbit anti-TH or anti-DARPP32 antibodies. Nuclei are stained with DAPI (blue). Representative images of different cells are shown. Red spots indicate close molecular interaction between CHL1 and DRD2. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals

Techniques Used: Proximity Ligation Assay, Staining

FIGURE 11 Reduced DRD2 and pSer40-TH levels in the dorsal striatum and reduced pThr34-DARPP32 levels in the ventral striatum in the absence of CHL1. The dorsal and ventral parts of the striatum were isolated from 10- to 13-week-old CHL1+/+ and CHL1−/− mice and subjected to Western blot analysis with anti-DRD2 and anti-GAPDH antibodies (A), anti-pSer40-TH and anti-TH antibodies (B) or anti-pThr34-DARPP32 and anti-DARPP32 (C) antibodies. Protein levels were determined by densitometry and DRD2 levels relative to GAPDH levels (A), pSer40-TH levels relative to total TH levels (B) and pThr34-DARPP32 levels relative to total DARPP32 levels (C) were calculated. A-C, Representative Western blots (left panels) are shown and mean values + standard error of the mean from eight CHL1−/− and 11 CHL1+/+ mice (right panels) are shown for the relative levels of DRD2 (A), pSer40-TH (B) and pThr34-DARPP32 (C) (Kruskal-Wallis test with post-hoc Dunn´s multiple comparison test; *P < .05, **P < .01). A, Lanes not adjacent to each other but derived from the same blot are separated by a vertical line

Figure Legend Snippet: FIGURE 11 Reduced DRD2 and pSer40-TH levels in the dorsal striatum and reduced pThr34-DARPP32 levels in the ventral striatum in the absence of CHL1. The dorsal and ventral parts of the striatum were isolated from 10- to 13-week-old CHL1+/+ and CHL1−/− mice and subjected to Western blot analysis with anti-DRD2 and anti-GAPDH antibodies (A), anti-pSer40-TH and anti-TH antibodies (B) or anti-pThr34-DARPP32 and anti-DARPP32 (C) antibodies. Protein levels were determined by densitometry and DRD2 levels relative to GAPDH levels (A), pSer40-TH levels relative to total TH levels (B) and pThr34-DARPP32 levels relative to total DARPP32 levels (C) were calculated. A-C, Representative Western blots (left panels) are shown and mean values + standard error of the mean from eight CHL1−/− and 11 CHL1+/+ mice (right panels) are shown for the relative levels of DRD2 (A), pSer40-TH (B) and pThr34-DARPP32 (C) (Kruskal-Wallis test with post-hoc Dunn´s multiple comparison test; *P < .05, **P < .01). A, Lanes not adjacent to each other but derived from the same blot are separated by a vertical line

Techniques Used: Isolation, Western Blot, Comparison, Derivative Assay

Image Search Results

Journal: The FASEB Journal

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

doi: 10.1096/fj.201900577rrrr

Figure Lengend Snippet: FIGURE 1 Association of CHL1 and DRD2. Brain extracts from CHL1+/+ (A-C) or CHL1−/− (C) mice (input) were subjected to immunoprecipitation (IP) with anti-CHL1 (A, C), anti-NCAM (A), anti-DRD2 (B), or non-immune control antibodies (A, B) and to Western blot analysis (WB) with anti-DRD2 (A, C) or anti-CHL1 (B) antibodies. D, CHL1-Fc and NCAM-Fc were incubated with a brain extract from CHL1+/+ mice (input) followed by pull-down (PD) with Protein A beads and by Western blot analysis (WB) with anti-DRD2 antibody. A-D, Representative Western blots from three independent experiments are shown. Lanes not adjacent to each other but derived from the same blot are separated by a vertical line. Aliquots of brain extracts not subjected to immunoprecipitation or pull-down experiments are designated as input

Article Snippet: The polyclonal rabbit antibodies against the extracellular domain of CHL1 and NCAM have been described.55,56 The polyclonal goat antibody against extracellular CHL1 epitopes (R and D Systems Cat# AF2147, RRID:AB_2079332) was from R&D Systems (Minneapolis, MN, USA).

Techniques: Immunoprecipitation, Control, Western Blot, Incubation, Derivative Assay

Journal: The FASEB Journal

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

doi: 10.1096/fj.201900577rrrr

Figure Lengend Snippet: FIGURE 2 Binding of CHL1-Fc to the first extracellular loop of DRD2. Synthetic peptides comprising the first (A), second (B), or third (C) extracellular DRD2 loop or the DRD2 N-terminus (D) were coated as substrate and incubated with increasing concentrations of CHL1-Fc or NCAM-Fc. Binding was determined by ELISA using horseradish peroxidase-conjugated anti-Fc antibodies. Mean values ± standard error of the mean from three independent experiments carried out in triplicates are shown

Techniques: Binding Assay, Incubation, Enzyme-linked Immunosorbent Assay

Journal: The FASEB Journal

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

doi: 10.1096/fj.201900577rrrr

Figure Lengend Snippet: FIGURE 3 Binding of CHL1-Fc to DRD2 at the cell surface of transfected HEK293 cells. Live HEK293 cell expressing DRD2-S or DRD2-L were incubated with CHL1-Fc. After fixation, cells were incubated with goat anti-CHL1 antibody and mouse anti-DRD2 antibody against the extracellular N-terminus. After washing, cells were stained with Cy2-conjugated anti-mouse (green) and Cy3- conjugated anti-goat (red) antibodies. Areas indicated by white dashed lines and arrows show areas with CHL1-immunopositive signals, which partially overlap with intense DRD2-immunopositive staining. Arrowheads indicate nuclei of CHL1- and DRD2-immunonegative untransfected cells. The experiment was performed two times. Scale bar: 10 µm

Techniques: Binding Assay, Transfection, Expressing, Incubation, Staining

Journal: The FASEB Journal

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

doi: 10.1096/fj.201900577rrrr

Figure Lengend Snippet: FIGURE 4 Interaction of CHL1 with DRD2-S and DRD2-L in transfected HEK293 cells. HEK293 cells were transfected with pCAG- DRD2-S, pCAG-DRD2-L, pCAG-DRD2-S/CHL1, or pCAG-DRD2-L/CHL1 to express DRD2-S or DRD2-L alone or together with CHL1 (DRD2-S/CHL1; DRD2-L/CHL1). Transfected cells were subjected to proximity ligation assay with anti-CHL1 and anti-DRD2 antibodies. A, Representative images at low (left and middle panel) and high magnification (right panels) from two independent experiments performed in duplicates are shown and red spots indicate close interaction of CHL1 with DRD2-S and DRD2-L. Scale bars: 10 µm. B, Red spots were counted in HEK293 cells co-expressing DRD2-S or DRD2-L and CHL1 (DRD2-S/CHL1; DRD2-L/CHL1). Numbers of red spots per cell from two independent experiments performed in duplicates are shown (*P < .001; two-tailed Student's t test). C, Representative images taken with and without phase contrast are shown. Red spots are located predominantly at the cell surface (arrows) and indicate the close interaction between CHL1 and DRD2-S at the cell surface

Techniques: Transfection, Proximity Ligation Assay, Expressing, Two Tailed Test

Journal: The FASEB Journal

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

doi: 10.1096/fj.201900577rrrr

Figure Lengend Snippet: FIGURE 5 Quinpirole reduces the cell surface level of DRD2-S in the absence of CHL1. A-C, HEK293 expressing DRD2-S (A) or DRD2-L (B) alone or co-expressing DRD2-S and CHL1 (DRD2-S/CHL1) (A, C) or DRD2-L and CHL1 (DRD2-L/CHL1) (B, C) were incubated with (+quin) or without (−quin) quinpirole followed by cell surface biotinylation, isolation of biotinylated proteins and Western blot analysis (WB) of the biotinylated proteins (surface) and the cell lysates (total) with anti-DRD2 (A, B) and anti-CHL1 (C) antibodies. The anti-GAPDH antibody was used to control loading (A, B). Total levels indicate the levels of CHL1 and DRD2 in cell lysates before isolation of biotinylated proteins, and cell surface levels represent biotinylated DRD2 after isolation of biotinylated proteins. A-C, Shown are representative blots from three independent experiments. D, E, Cell surface levels of DRD2-S and DRD2-L and total DRD2-S and DRD2-L levels in the cell lysates were determined, cell surface levels were normalized to total levels and the ratio of relative cell surface level after quinpirole treatment (+quin) and relative cell surface level after treatment without quinpirole (−quin) was calculated. Means + standard deviation from three independent experiments are shown for the ratios of the cell surface levels with quinpirole treatment relative to the cell surface levels without quinpirole treatment (D) and for the cell surface levels without quinpirole treatment relative to the total levels without quinpirole treatment (E) (Kruskal-Wallis test with post-hoc Dunn´s multiple comparison test; **P < .01; ns: not significant)

Techniques: Expressing, Incubation, Isolation, Western Blot, Control, Standard Deviation, Comparison

Journal: The FASEB Journal

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

doi: 10.1096/fj.201900577rrrr

Figure Lengend Snippet: FIGURE 6 Quinpirole-induced internalization of DRD2-S is reduced in the presence of CHL1. A, B, HEK293 expressing DRD2-S or co- expressing DRD2-S and CHL1 (DRD2-S/CHL1) were incubated with anti-DRD2 antibody against the extracellular N-terminus. After removal of unbound antibodies, cells were stimulated without (−quin) or with (+quin) quinpirole, fixed and incubated with Cy-3-conjugated secondary antibody. After removal of unbound secondary antibodies, cells were permeabilized and incubated with Cy-2-conjugated secondary antibody and analyzed by confocal microscopy. Cy-3-conjugated secondary antibodies (red) indicate non-internalized DRD2-bound anti-DRD2 antibodies at the cell surface and Cy-2-conjugated secondary antibodies (green) label internalized DRD2-bound anti-DRD2 antibodies. A, Representative images of HEK293 expressing DRD2-S after quinpirole treatment show surface DRD2 (red) and internalized DRD2 (green). Scale bar: 10 µm. B, Integrated densities of internalized and cell surface receptor-bound antibodies were determined and integrated densities of internalized receptor-bound antibodies were normalized to the total integrated densities (sum of integrated densities of internalized and cell surface receptor-bound antibodies). Box plots for the relative levels of internalized DRD2 are shown (**P < .01, ***P < .001; One-way ANOVA with post-hoc Student Newman- Keul's test). The experiment was performed two times in duplicates

Techniques: Expressing, Incubation, Confocal Microscopy, Cell Surface Receptor Assay

Journal: The FASEB Journal

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

doi: 10.1096/fj.201900577rrrr

Figure Lengend Snippet: FIGURE 7 Co-immunostaining of CHL1 and DRD2 in the striatum. Tissue sections from 12- to 18-week-old CHL1+/+ (A, C) and CHL1−/− (B) mice were subjected to immunostaining using goat anti-CHL1 and mouse anti-DRD2 antibodies and Cy-3-conjugated anti- mouse and Cy-2-conjugated anti-goat secondary antibodies. Nuclei are stained with DAPI. Representative image of immunofluorescence staining for DAPI (blue), CHL1 (green), and DRD2 (red) are shown and yellow signals show co- localizations. C, Close-ups of two regions indicated by boxes in (A). A-C, Scale bars: 20 µm. Three independent experiments were performed with different sets of animals

Techniques: Immunostaining, Staining, Immunofluorescence

Journal: The FASEB Journal

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

doi: 10.1096/fj.201900577rrrr

Figure Lengend Snippet: FIGURE 8 Co-localization of CHL1 and DRD2 in the striatum. Tissue sections from 12- to 18-week-old CHL1+/+ and CHL1−/− mice were analyzed by proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies. Nuclei are stained with DAPI (blue). Representative images are shown at low (left and middle panel) and high (right panel) magnifications. Red spots indicate close molecular interaction of CHL1 with DRD2 in CHL1+/+ mice. CHL1−/− mice served as controls. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals

Techniques: Proximity Ligation Assay, Staining

Journal: The FASEB Journal

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

doi: 10.1096/fj.201900577rrrr

Figure Lengend Snippet: FIGURE 9 Interaction of CHL1 and DRD2 on TH- and DARP32-positive neurons in striatal sections. Proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies was combined with immunostaining using rabbit anti-DARPP32 (A) or anti-TH (B) antibodies to analyze tissue sections from 12- to 18-week-old CHL1+/+ mice. Nuclei are stained with DAPI (blue). Representative images are shown. Close- ups of two regions (without DAPI staining) are indicated by boxes and arrowheads indicate red spots indicating close molecular interaction of CHL1 with DRD2. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals

Techniques: Proximity Ligation Assay, Immunostaining, Staining

Journal: The FASEB Journal

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

doi: 10.1096/fj.201900577rrrr

Figure Lengend Snippet: FIGURE 10 Interaction of CHL1 and DRD2 on TH- and DARP32-positive cells in cultures of ventral midbrain and striatum. Cultures of ventral midbrain (A) or striatum (B) were analyzed by proximity ligation assay using goat anti-CHL1 and mouse anti-DRD2 antibodies combined with immunofluorescent staining using rabbit anti-TH or anti-DARPP32 antibodies. Nuclei are stained with DAPI (blue). Representative images of different cells are shown. Red spots indicate close molecular interaction between CHL1 and DRD2. Scale bars: 10 µm. Three independent experiments were performed with different sets of animals

Techniques: Proximity Ligation Assay, Staining

Journal: The FASEB Journal

Article Title: Cell adhesion molecule close homolog of L1 binds to the dopamine receptor D2 and inhibits the internalization of its short isoform

doi: 10.1096/fj.201900577rrrr

Figure Lengend Snippet: FIGURE 11 Reduced DRD2 and pSer40-TH levels in the dorsal striatum and reduced pThr34-DARPP32 levels in the ventral striatum in the absence of CHL1. The dorsal and ventral parts of the striatum were isolated from 10- to 13-week-old CHL1+/+ and CHL1−/− mice and subjected to Western blot analysis with anti-DRD2 and anti-GAPDH antibodies (A), anti-pSer40-TH and anti-TH antibodies (B) or anti-pThr34-DARPP32 and anti-DARPP32 (C) antibodies. Protein levels were determined by densitometry and DRD2 levels relative to GAPDH levels (A), pSer40-TH levels relative to total TH levels (B) and pThr34-DARPP32 levels relative to total DARPP32 levels (C) were calculated. A-C, Representative Western blots (left panels) are shown and mean values + standard error of the mean from eight CHL1−/− and 11 CHL1+/+ mice (right panels) are shown for the relative levels of DRD2 (A), pSer40-TH (B) and pThr34-DARPP32 (C) (Kruskal-Wallis test with post-hoc Dunn´s multiple comparison test; *P < .05, **P < .01). A, Lanes not adjacent to each other but derived from the same blot are separated by a vertical line

Techniques: Isolation, Western Blot, Comparison, Derivative Assay

BACE1-mediated processing of APP and CHL1 is reduced in cortex of young BACE1 cKO mice following tamoxifen treatment. Cortex homogenates from TAM- or VEH-treated mice were resolved by SDS-PAGE for Western blot analysis of APP and CHL1 processing. Homogenates from aged-matched BACE +/− and BACE1 −/− were also loaded as control samples. Representative blots of ( a ) APP-full length (APP-FL) (C1/6.1), ( b ) APP-Carboxy Terminal Fragments (CTFs) (C1/6.1) and ( c ) CHL1. ( d ) Densitometry analysis of protein expression. Protein amount was normalized to protein levels in control mice (set at 1). APP-FL, pC99 and pC89 were normalized to GAPDH (MAB374) while CHL1-FL and CHL1-NTF were normalized to β-tubulin (JDR.3B8). APP processing was reduced in TAM-treated mice as demonstrated by the accumulation of APP-FL (C1/6.1), and reduced levels of the βCTFs pC99 and pC89. βCTFs were clearly identified because missing in the BACE1 −/− sample. CHL1-FL (AF2147) levels were increased while CHL1-N Terminal Fragment (CHL1-NTF) levels were not affected in cortex of TAM-treated mice. However, the CHL1-NTF/CHL1-FL ratio was significantly decreased in TAM-treated mice demonstrating reduced BACE1 processing (VEH n = 8; TAM n = 8). ( e ) Aβx-40 was quantified from brain homogenates by ELISA (VEH n = 8; TAM n = 8). Levels of Aβx-40 expressed as pMol/g of cortex were significantly reduced in TAM-treated mice (~50% decrease). Results were plotted as Mean ± SEM, ***p < 0.001; ****p < 0.0001; n.s. = not significant, Student’s t test.

Journal: Scientific Reports

Article Title: BACE1 partial deletion induces synaptic plasticity deficit in adult mice

doi: 10.1038/s41598-019-56329-7

Figure Lengend Snippet: BACE1-mediated processing of APP and CHL1 is reduced in cortex of young BACE1 cKO mice following tamoxifen treatment. Cortex homogenates from TAM- or VEH-treated mice were resolved by SDS-PAGE for Western blot analysis of APP and CHL1 processing. Homogenates from aged-matched BACE +/− and BACE1 −/− were also loaded as control samples. Representative blots of ( a ) APP-full length (APP-FL) (C1/6.1), ( b ) APP-Carboxy Terminal Fragments (CTFs) (C1/6.1) and ( c ) CHL1. ( d ) Densitometry analysis of protein expression. Protein amount was normalized to protein levels in control mice (set at 1). APP-FL, pC99 and pC89 were normalized to GAPDH (MAB374) while CHL1-FL and CHL1-NTF were normalized to β-tubulin (JDR.3B8). APP processing was reduced in TAM-treated mice as demonstrated by the accumulation of APP-FL (C1/6.1), and reduced levels of the βCTFs pC99 and pC89. βCTFs were clearly identified because missing in the BACE1 −/− sample. CHL1-FL (AF2147) levels were increased while CHL1-N Terminal Fragment (CHL1-NTF) levels were not affected in cortex of TAM-treated mice. However, the CHL1-NTF/CHL1-FL ratio was significantly decreased in TAM-treated mice demonstrating reduced BACE1 processing (VEH n = 8; TAM n = 8). ( e ) Aβx-40 was quantified from brain homogenates by ELISA (VEH n = 8; TAM n = 8). Levels of Aβx-40 expressed as pMol/g of cortex were significantly reduced in TAM-treated mice (~50% decrease). Results were plotted as Mean ± SEM, ***p < 0.001; ****p < 0.0001; n.s. = not significant, Student’s t test.

Article Snippet: Immunoblot and serial fractionation were performed as previously described with the following antibodies: rabbit monoclonal anti-BACE1 (1:1000; D10E5; Cell signaling technology); mouse monoclonal anti-APP (and APP CTFs) antibody (1:5000; C1/6.1; BioLegend); goat polyclonal anti-N-terminal CHL1 antibody (for CHL1-FL and CHL1-NTF) (1:1000; AF2147; R&D Systems); mouse monoclonal anti-GAPDH (1:10,000; MAP374; Millipore); mouse monoclonal anti-β-tubulin (1:10,000; JDR.3BR; Sigma); mouse monoclonal anti-calnexin (1:2000; 610523; BD biosciences); rabbit polyclonal anti-ADAM10 (1:1000;AB19026; Millipore); rabbit polyclonal anti-PS1 AB14 (1:1000) and rat monoclonal anti-SEZ6 (1:250) , rat monoclonal anti-APPsβ (1:40) and HRP-conjugated secondary antibodies visualized by ECL (GE Healthcare).

Techniques: SDS Page, Western Blot, Control, Expressing, Enzyme-linked Immunosorbent Assay

BACE1-mediated processing of APP and CHL1 is reduced in cortex of aged BACE1 cKO mice following tamoxifen treatment. Cortex homogenates from TAM- or VEH-treated mice were resolved by SDS-PAGE for Western blot analysis of APP and CHL1 processing. Homogenates from aged-matched BACE +/− and BACE1 −/− were also loaded as control samples. APP-FL, pC99 and pC89 were normalized to GAPDH (MAB374) while CHL1-FL and CHL1-NTF were normalized to β-tubulin (JDR.3B8). Protein amount was normalized to protein levels in control mice injected with vehicle (set at 1). Representative blots of ( a ) APP-FL (C1/6.1), ( b ) APP-CTFs (C1/6.1) and (c ) CHL1. ( d ) Densitometry analysis of protein expression. APP processing was reduced in TAM-treated mice as demonstrated by the accumulation of APP-FL (C1/6.1), and reduced levels of the βCTFs pC99 and pC89. βCTFs were clearly identified because missing in the BACE1 −/− sample. CHL1-FL (AF2147) levels were increased and CHL1-NTF levels were significantly reduced. Furthermore, the CHL1-NTF/CHL1-FL ratio was significantly decreased in TAM-treated mice demonstrating reduced BACE1 processing (VEH n = 7; TAM n = 7). ( e ) Quantification of Aβx-40 was performed by MSD immunoassay on cortex homogenates and expressed as pMol/g of cortex. The decrease of levels of Aβx-40 in TAM-treated mice was comparable to the one observed in samples collected from young TAM-treated mice (~50% decrease) (VEH n = 7; TAM n = 7). Results were plotted as Mean ± SEM, *p < 0.05; **p < 0.005; ***p < 0.001; ****p < 0.0001; n.s. = not significant, Student’s t test.

Journal: Scientific Reports

Article Title: BACE1 partial deletion induces synaptic plasticity deficit in adult mice

doi: 10.1038/s41598-019-56329-7

Figure Lengend Snippet: BACE1-mediated processing of APP and CHL1 is reduced in cortex of aged BACE1 cKO mice following tamoxifen treatment. Cortex homogenates from TAM- or VEH-treated mice were resolved by SDS-PAGE for Western blot analysis of APP and CHL1 processing. Homogenates from aged-matched BACE +/− and BACE1 −/− were also loaded as control samples. APP-FL, pC99 and pC89 were normalized to GAPDH (MAB374) while CHL1-FL and CHL1-NTF were normalized to β-tubulin (JDR.3B8). Protein amount was normalized to protein levels in control mice injected with vehicle (set at 1). Representative blots of ( a ) APP-FL (C1/6.1), ( b ) APP-CTFs (C1/6.1) and (c ) CHL1. ( d ) Densitometry analysis of protein expression. APP processing was reduced in TAM-treated mice as demonstrated by the accumulation of APP-FL (C1/6.1), and reduced levels of the βCTFs pC99 and pC89. βCTFs were clearly identified because missing in the BACE1 −/− sample. CHL1-FL (AF2147) levels were increased and CHL1-NTF levels were significantly reduced. Furthermore, the CHL1-NTF/CHL1-FL ratio was significantly decreased in TAM-treated mice demonstrating reduced BACE1 processing (VEH n = 7; TAM n = 7). ( e ) Quantification of Aβx-40 was performed by MSD immunoassay on cortex homogenates and expressed as pMol/g of cortex. The decrease of levels of Aβx-40 in TAM-treated mice was comparable to the one observed in samples collected from young TAM-treated mice (~50% decrease) (VEH n = 7; TAM n = 7). Results were plotted as Mean ± SEM, *p < 0.05; **p < 0.005; ***p < 0.001; ****p < 0.0001; n.s. = not significant, Student’s t test.

Techniques: SDS Page, Western Blot, Control, Injection, Expressing

$Axon guidance defects were absent in hippocampus mossy fibers of aged BACE1 cKO mice following partial BACE1 deletion. ( a ) Coronal sections collected from aged mice were stained with anti-synaptoporin (SPO) antibody (green) and DAPI (blue). Scale bar 50 μm. ( b) Quantification of IPB length showed no alteration in TAM-treated mice compared to controls. IPB length was normalized on the length of the CA3 stratum lucidum (VEH n = 8; TAM n = 7, 3 to 4 sections per mouse). ( c ) Representative microscopy images showing reduced BACE1 (D10E5) expression in the hippocampus of TAM-treated mice. BACE1 signal was totally absent in BACE −/− mice, used as control to evaluate the amount of background in the staining. Scale bar 200 μm. Hippocampus full homogenates from TAM- or VEH-treated mice were resolved by SDS-PAGE for analysis of APP processing and fractionated (soluble and membrane fractions) for the analysis of SEZ6 and CHL1 processing. Homogenates from aged-matched BACE +/− and BACE1 −/− were loaded as control samples. Representative blots of ( d ) APP-FL (C1/6.1) and APP- CTFs (C1/6.1), ( e ) fractionation blots of sAPPβ (BAWT), SEZ6 (14E5) and CHL1 (AF2147). ( f ) Densitometry analysis of protein expression. APP processing was reduced in TAM-treated mice as demonstrated by the accumulation of APP-FL (C1/6.1), and reduced levels of the βCTFs pC99 and pC89, and sAPPβ. βCTFs and sAPPβ were identified because missing in the BACE1 −/− sample. SEZ6 processing was decreased in TAM-treated mice with accumulation of the full length and decreased levels of the ectodomain (SEZ6-NTF) as well as decreased SEZ6-NTF/SEZ6FL ratio. Processing of CHL1 was also impaired as showed by increased of CHL1-FL levels, while CHL1-NTF was not altered. CHL1-NTF/CHL1-FL ratio was significantly decreased. APP-FL, CTFs, SEZ6-NTF and CHL1-NTF were normalized to GAPDH (MAB374), SEZ6-FL and CHL1-FL were normalized to Calnexin (610523) (VEH n = 5; TAM n = 5). ( g ) Aβx-40 was quantified from hippocampus homogenates by MSD immunoassay. TAM-treated group displayed a significant reduction of Aβx-40 levels (~50% decrease) compared to control (VEH n = 7; TAM n = 7). Results were plotted as Mean ± SEM, **p < 0.005; ***p < 0.001; n.s. = not significant, Student’s t test. DG: dentate gyrus, IPB: infrapyramidal bundle, slu: stratum lucidum, MB: main bundle.$

Journal: Scientific Reports

Article Title: BACE1 partial deletion induces synaptic plasticity deficit in adult mice

doi: 10.1038/s41598-019-56329-7

Figure Lengend Snippet: Axon guidance defects were absent in hippocampus mossy fibers of aged BACE1 cKO mice following partial BACE1 deletion. ( a ) Coronal sections collected from aged mice were stained with anti-synaptoporin (SPO) antibody (green) and DAPI (blue). Scale bar 50 μm. ( b) Quantification of IPB length showed no alteration in TAM-treated mice compared to controls. IPB length was normalized on the length of the CA3 stratum lucidum (VEH n = 8; TAM n = 7, 3 to 4 sections per mouse). ( c ) Representative microscopy images showing reduced BACE1 (D10E5) expression in the hippocampus of TAM-treated mice. BACE1 signal was totally absent in BACE −/− mice, used as control to evaluate the amount of background in the staining. Scale bar 200 μm. Hippocampus full homogenates from TAM- or VEH-treated mice were resolved by SDS-PAGE for analysis of APP processing and fractionated (soluble and membrane fractions) for the analysis of SEZ6 and CHL1 processing. Homogenates from aged-matched BACE +/− and BACE1 −/− were loaded as control samples. Representative blots of ( d ) APP-FL (C1/6.1) and APP- CTFs (C1/6.1), ( e ) fractionation blots of sAPPβ (BAWT), SEZ6 (14E5) and CHL1 (AF2147). ( f ) Densitometry analysis of protein expression. APP processing was reduced in TAM-treated mice as demonstrated by the accumulation of APP-FL (C1/6.1), and reduced levels of the βCTFs pC99 and pC89, and sAPPβ. βCTFs and sAPPβ were identified because missing in the BACE1 −/− sample. SEZ6 processing was decreased in TAM-treated mice with accumulation of the full length and decreased levels of the ectodomain (SEZ6-NTF) as well as decreased SEZ6-NTF/SEZ6FL ratio. Processing of CHL1 was also impaired as showed by increased of CHL1-FL levels, while CHL1-NTF was not altered. CHL1-NTF/CHL1-FL ratio was significantly decreased. APP-FL, CTFs, SEZ6-NTF and CHL1-NTF were normalized to GAPDH (MAB374), SEZ6-FL and CHL1-FL were normalized to Calnexin (610523) (VEH n = 5; TAM n = 5). ( g ) Aβx-40 was quantified from hippocampus homogenates by MSD immunoassay. TAM-treated group displayed a significant reduction of Aβx-40 levels (~50% decrease) compared to control (VEH n = 7; TAM n = 7). Results were plotted as Mean ± SEM, **p < 0.005; ***p < 0.001; n.s. = not significant, Student’s t test. DG: dentate gyrus, IPB: infrapyramidal bundle, slu: stratum lucidum, MB: main bundle.

Techniques: Staining, Microscopy, Expressing, Control, SDS Page, Membrane, Fractionation

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