Structured Review

R&D Systems gtpγs binding assay
Effect of DAMGO, loperamide and eluxadoline on G-protein activation. (A–C) Membranes (10 μg) from spinal cords of WT, μOR −/− and δOR −/− mice were subjected to a [ 35 <t>S]GTPγS</t> binding assay using DAMGO (A), loperamide (B), and eluxadoline (C) (0–10 μM final concentration) as described in Section 2. (D–G) Membranes (20 μg) from the ileum of WT mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (D and G), loperamide (E and G), and eluxadoline (F and G) (0–10 μM final concentration) in the presence or absence of TIPPψ (10 nM final concentration) as described in Section 2. (G) Represents E max (% of basal) obtained with 10 μM final concentration of DAMGO (±10 nM final concentration of TIPPψ), eluxadoline or loperamide. Basal values determined in the absence of the agonist were taken as 100%. Results are the mean ± S.E.M. n = 3–9. n.d., Not determined. * p
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1) Product Images from "Molecular characterization of eluxadoline as a potential ligand targeting mu-delta opioid receptor heteromers"

Article Title: Molecular characterization of eluxadoline as a potential ligand targeting mu-delta opioid receptor heteromers

Journal: Biochemical pharmacology

doi: 10.1016/j.bcp.2014.09.015

Effect of DAMGO, loperamide and eluxadoline on G-protein activation. (A–C) Membranes (10 μg) from spinal cords of WT, μOR −/− and δOR −/− mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (A), loperamide (B), and eluxadoline (C) (0–10 μM final concentration) as described in Section 2. (D–G) Membranes (20 μg) from the ileum of WT mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (D and G), loperamide (E and G), and eluxadoline (F and G) (0–10 μM final concentration) in the presence or absence of TIPPψ (10 nM final concentration) as described in Section 2. (G) Represents E max (% of basal) obtained with 10 μM final concentration of DAMGO (±10 nM final concentration of TIPPψ), eluxadoline or loperamide. Basal values determined in the absence of the agonist were taken as 100%. Results are the mean ± S.E.M. n = 3–9. n.d., Not determined. * p
Figure Legend Snippet: Effect of DAMGO, loperamide and eluxadoline on G-protein activation. (A–C) Membranes (10 μg) from spinal cords of WT, μOR −/− and δOR −/− mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (A), loperamide (B), and eluxadoline (C) (0–10 μM final concentration) as described in Section 2. (D–G) Membranes (20 μg) from the ileum of WT mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (D and G), loperamide (E and G), and eluxadoline (F and G) (0–10 μM final concentration) in the presence or absence of TIPPψ (10 nM final concentration) as described in Section 2. (G) Represents E max (% of basal) obtained with 10 μM final concentration of DAMGO (±10 nM final concentration of TIPPψ), eluxadoline or loperamide. Basal values determined in the absence of the agonist were taken as 100%. Results are the mean ± S.E.M. n = 3–9. n.d., Not determined. * p

Techniques Used: Activation Assay, Mouse Assay, GTPγS Binding Assay, Concentration Assay

2) Product Images from "Chronic Morphine Treatment Attenuates Cell Growth of Human BT474 Breast Cancer Cells by Rearrangement of the ErbB Signalling Network"

Article Title: Chronic Morphine Treatment Attenuates Cell Growth of Human BT474 Breast Cancer Cells by Rearrangement of the ErbB Signalling Network

Journal: PLoS ONE

doi: 10.1371/journal.pone.0053510

Regulation of ErbB signalling by chronic Morphine in SKBR3 cells. ( A ) Identification of κ-opioid receptors in SKBR3 human mammary adenocarcinoma cells by RT-PCR. Reactions contained 10 ng of cDNA from SKBR3 cells or plasmid pcDNA3.1 containing the cloned receptor. A 322 bp fragment of the κ-opioid receptor is present in the cells (arrow). Ladder: 100 bp. ( B ) Regulation of ErbB receptor abundance by chronic Morphine treatment. Cells were cultured for 3 d in the presence or absence of Morphine (10 µM) and Naloxone (100 µM), before membranes were prepared and ErbB receptors were determined by Western blot using antibodies specific for ErbB1 (175 kDa), ErbB2 (185 kDa) and ErbB3 (185 kDa). Equal protein loading was determined using an antibody against β-tubulin. ( C ) Effect of chronic Morphine treatment on ErbB1- and ErbB3-stimulated ERK1/2 signalling. SKBR3 cells were cultured for 3 d in the absence (control) or presence of Morphine (10 µM), before the impact of protein inhibitors AG1478 (ErbB1), AG825 (ErbB2), Wortmannin (Wort; PI3K) and EGCG (metalloproteinases) on basal, EGF (100 ng/ml)- and Heregulin (40 ng/ml)-stimulated ERK1/2 phosphorylation was determined by Western blot. Controls were kept in the absence of protein inhibitors (none). Total ERK1/2 was determined using an overall reactive antibody.
Figure Legend Snippet: Regulation of ErbB signalling by chronic Morphine in SKBR3 cells. ( A ) Identification of κ-opioid receptors in SKBR3 human mammary adenocarcinoma cells by RT-PCR. Reactions contained 10 ng of cDNA from SKBR3 cells or plasmid pcDNA3.1 containing the cloned receptor. A 322 bp fragment of the κ-opioid receptor is present in the cells (arrow). Ladder: 100 bp. ( B ) Regulation of ErbB receptor abundance by chronic Morphine treatment. Cells were cultured for 3 d in the presence or absence of Morphine (10 µM) and Naloxone (100 µM), before membranes were prepared and ErbB receptors were determined by Western blot using antibodies specific for ErbB1 (175 kDa), ErbB2 (185 kDa) and ErbB3 (185 kDa). Equal protein loading was determined using an antibody against β-tubulin. ( C ) Effect of chronic Morphine treatment on ErbB1- and ErbB3-stimulated ERK1/2 signalling. SKBR3 cells were cultured for 3 d in the absence (control) or presence of Morphine (10 µM), before the impact of protein inhibitors AG1478 (ErbB1), AG825 (ErbB2), Wortmannin (Wort; PI3K) and EGCG (metalloproteinases) on basal, EGF (100 ng/ml)- and Heregulin (40 ng/ml)-stimulated ERK1/2 phosphorylation was determined by Western blot. Controls were kept in the absence of protein inhibitors (none). Total ERK1/2 was determined using an overall reactive antibody.

Techniques Used: Reverse Transcription Polymerase Chain Reaction, Plasmid Preparation, Clone Assay, Cell Culture, Western Blot

Analysis of chronic Morphine-induced changes in ErbB signalling pathways. ( A ) Effect of protein kinase blockers on basal and Heregulin-stimulated ERK1/2 and Akt phosphorylation. BT474 cells were cultured for 5 d in the absence (control) or presence of Morphine (10 µM), before the impact of ErbB1 (AG1478), ErbB2 (AG825), PI3K (Wortmannin; Wort.) and metalloproteinases (EGCG) on basal and Heregulin (40 ng/ml)-stimulated ERK1/2 and Akt signalling was determined by Western blot using phospho-specific antibodies. Controls were kept in the absence of protein inhibitors. To verify equal protein loading, controls were also stained with overall reactive anti-ERK1/2 and anti-Akt antibodies. ( B ) Involvement of ErbB2 on basal and EGF-stimulated ERK1/2 and Akt signalling. Controls and cells chronically exposed to Morphine (10 µM; 5d) were incubated with or without AG825 (50 µM; 30 min), before ERK1/2 and Akt phosphorylation was determined for 5 min in the absence or presence of EGF (100 ng/ml). Equal protein loading was verified by staining controls with overall reactive anti-ERK1/2 and anti-Akt antibodies. ( C ) Regulation of ErbB receptor abundance by chronic Morphine treatment in BT474 cells. Cells were cultured for 5 d in the presence or absence of Morphine (10 µM) and Naloxone (100 µM) as indicated and overall ErbB receptor levels were analysed by Western blot using specific antibodies for ErbB1 (175 kDa), ErbB2 (185 kDa), ErbB3 (185 kDa) and ErbB4 (170 kDa). Equal protein loading was verified by incubation of the blots with an antibody against β-tubulin. ( D ) Alteration of ErbB1 containing receptor dimers by chronic Morphine. Controls and chronically Morphine (10 µM; 5 d)-treated BT474 cells were stimulated for 5 min with or without Heregulin (40 ng/ml) to form receptor dimers. Proteins were cross-linked and ErbB1 containing dimers were immunoprecipitated using an anti-ErbB1 antibody. Individual ErbB receptors were determined in whole cell solubilisates (S) and immunoprecipitates (IP) by Western blot using type-specific antibodies. Equal protein load was verified by determination of IgG heavy chains ( F c ).
Figure Legend Snippet: Analysis of chronic Morphine-induced changes in ErbB signalling pathways. ( A ) Effect of protein kinase blockers on basal and Heregulin-stimulated ERK1/2 and Akt phosphorylation. BT474 cells were cultured for 5 d in the absence (control) or presence of Morphine (10 µM), before the impact of ErbB1 (AG1478), ErbB2 (AG825), PI3K (Wortmannin; Wort.) and metalloproteinases (EGCG) on basal and Heregulin (40 ng/ml)-stimulated ERK1/2 and Akt signalling was determined by Western blot using phospho-specific antibodies. Controls were kept in the absence of protein inhibitors. To verify equal protein loading, controls were also stained with overall reactive anti-ERK1/2 and anti-Akt antibodies. ( B ) Involvement of ErbB2 on basal and EGF-stimulated ERK1/2 and Akt signalling. Controls and cells chronically exposed to Morphine (10 µM; 5d) were incubated with or without AG825 (50 µM; 30 min), before ERK1/2 and Akt phosphorylation was determined for 5 min in the absence or presence of EGF (100 ng/ml). Equal protein loading was verified by staining controls with overall reactive anti-ERK1/2 and anti-Akt antibodies. ( C ) Regulation of ErbB receptor abundance by chronic Morphine treatment in BT474 cells. Cells were cultured for 5 d in the presence or absence of Morphine (10 µM) and Naloxone (100 µM) as indicated and overall ErbB receptor levels were analysed by Western blot using specific antibodies for ErbB1 (175 kDa), ErbB2 (185 kDa), ErbB3 (185 kDa) and ErbB4 (170 kDa). Equal protein loading was verified by incubation of the blots with an antibody against β-tubulin. ( D ) Alteration of ErbB1 containing receptor dimers by chronic Morphine. Controls and chronically Morphine (10 µM; 5 d)-treated BT474 cells were stimulated for 5 min with or without Heregulin (40 ng/ml) to form receptor dimers. Proteins were cross-linked and ErbB1 containing dimers were immunoprecipitated using an anti-ErbB1 antibody. Individual ErbB receptors were determined in whole cell solubilisates (S) and immunoprecipitates (IP) by Western blot using type-specific antibodies. Equal protein load was verified by determination of IgG heavy chains ( F c ).

Techniques Used: Cell Culture, Western Blot, Staining, Incubation, Immunoprecipitation

Model of chronic Morphine-induced changes in ErbB signalling. The scheme depicts the differences in Heregulin-stimulated ErbB signalling in control and chronically Morphine-treated BT474 cells. In control cells, stimulation with Heregulin leads to activation of ERK1/2 and Akt signalling via ErbB1/ErbB3 heterodimers. While AG1478 blocks both Heregulin-stimulated ERK1/2 and Akt signalling, inhibition of PI3K by Wortmannin specifically prevents Akt signalling. Because ErbB3 phosphorylation and PI3K activation is dependent on the presence of a dimerized ErbB member with catalytic activity, these results indicate that Heregulin-stimulated ERK1/2 signalling is predominantly mediated through ErbB1. The failure of Wortmannin to affect ERK1/2 activation in control cells further implicates that Heregulin stimulates Akt signalling via ErbB3. Chronic Morphine treatment alters mitogenic signalling by rearrangement of ErbB heterodimers. Whereas Heregulin still stimulates Akt signalling via ErbB1/ErbB3, ERK1/2 signalling is now accomplished by ErbB1/2 heterodimers. These are activated indirectly by an EGF-like ligand liberated from Heregulin in a PI3K (Wortmannin)- and metalloproteinase (EGCG)-dependent manner.
Figure Legend Snippet: Model of chronic Morphine-induced changes in ErbB signalling. The scheme depicts the differences in Heregulin-stimulated ErbB signalling in control and chronically Morphine-treated BT474 cells. In control cells, stimulation with Heregulin leads to activation of ERK1/2 and Akt signalling via ErbB1/ErbB3 heterodimers. While AG1478 blocks both Heregulin-stimulated ERK1/2 and Akt signalling, inhibition of PI3K by Wortmannin specifically prevents Akt signalling. Because ErbB3 phosphorylation and PI3K activation is dependent on the presence of a dimerized ErbB member with catalytic activity, these results indicate that Heregulin-stimulated ERK1/2 signalling is predominantly mediated through ErbB1. The failure of Wortmannin to affect ERK1/2 activation in control cells further implicates that Heregulin stimulates Akt signalling via ErbB3. Chronic Morphine treatment alters mitogenic signalling by rearrangement of ErbB heterodimers. Whereas Heregulin still stimulates Akt signalling via ErbB1/ErbB3, ERK1/2 signalling is now accomplished by ErbB1/2 heterodimers. These are activated indirectly by an EGF-like ligand liberated from Heregulin in a PI3K (Wortmannin)- and metalloproteinase (EGCG)-dependent manner.

Techniques Used: Activation Assay, Inhibition, Activity Assay

Regulation of BT474 cell growth and migration by Morphine. ( A ) BT474 cells were cultured for 5 d in the presence or absence of Morphine (10 µM), Naloxone (100 µM), and Heregulin (40 ng/ml), before cell growth was determined by crystal violet staining. Top: Photograph of tissue culture wells from a representative experiment before solubilisation of the dye. Bottom: Data of n = 6 independent experiments normalized to controls. Note that co-incubation of the cells with Morphine significantly attenuates Heregulin-stimulated cell growth (**, p
Figure Legend Snippet: Regulation of BT474 cell growth and migration by Morphine. ( A ) BT474 cells were cultured for 5 d in the presence or absence of Morphine (10 µM), Naloxone (100 µM), and Heregulin (40 ng/ml), before cell growth was determined by crystal violet staining. Top: Photograph of tissue culture wells from a representative experiment before solubilisation of the dye. Bottom: Data of n = 6 independent experiments normalized to controls. Note that co-incubation of the cells with Morphine significantly attenuates Heregulin-stimulated cell growth (**, p

Techniques Used: Migration, Cell Culture, Staining, Incubation

Regulation of cell survival and apoptosis by Morphine. ( A ) Determination of Akt activation in control and chronically Morphine (10 µM; 5d)-treated cells. Cells were incubated for 5 min at 37°C in the presence or absence of Morphine (10 µM), Naloxone (100 µM) and Heregulin (40 ng/ml), before Akt phosphorylation was determined by Western blot using a phosphor-specific antibody. The overall amount of Akt was determined by a phosphorylation-insensitive antibody. Insets show representative Western blots of the corresponding proteins (60 kDa) and β-tubulin (loading control). Immunoreactive bands were quantified and normalized to Heregulin-stimulated values in control cells, which was set to 100%. The data shown are from n = 4 independent experiments. ( B ) Comparison of basal and Heregulin (40 ng/ml)-stimulated Akt activation in control and Morphine (10 µM; 5d)-treated cells. Samples were run on the same gel and stained for phospho-Akt, total Akt and β-tubulin as loading control. Note that chronic morphine treatment increases basal and Heregulin (40 ng/ml)-stimulated levels of Akt phosphorylation. ( C ) Determination of PARP cleavage in BT474 cells. Cells were cultured in the absence (control) or presence of Morphine (10 µM; 5 d), before cells were washed and grown for an additional 6 h in serum-free Medium either in the absence or presence of Heregulin (40 ng/ml) Morphine (10 µM) and Naloxone (100 µM) as indicated. Samples were analysed by Western blot using an antibody recognizing full length (116 kDa) and cleaved (89 kDa) PARP. The same samples were blotted for β-tubulin (loading control). ( D ) Determination of apoptosis by Annexin V/propidium iodide staining. BT474 cells were cultured on coverslips for 5 d in the presence or absence of Morphine (10 µM), Naloxone (100 µM) and Heregulin (40 ng/ml) alone or in combination as indicated. Cells were sequentially stained with Annexin-FITC (green), propidium iodide (red), fixed and analysed by confocal microscopy. Bar: 20 µm.
Figure Legend Snippet: Regulation of cell survival and apoptosis by Morphine. ( A ) Determination of Akt activation in control and chronically Morphine (10 µM; 5d)-treated cells. Cells were incubated for 5 min at 37°C in the presence or absence of Morphine (10 µM), Naloxone (100 µM) and Heregulin (40 ng/ml), before Akt phosphorylation was determined by Western blot using a phosphor-specific antibody. The overall amount of Akt was determined by a phosphorylation-insensitive antibody. Insets show representative Western blots of the corresponding proteins (60 kDa) and β-tubulin (loading control). Immunoreactive bands were quantified and normalized to Heregulin-stimulated values in control cells, which was set to 100%. The data shown are from n = 4 independent experiments. ( B ) Comparison of basal and Heregulin (40 ng/ml)-stimulated Akt activation in control and Morphine (10 µM; 5d)-treated cells. Samples were run on the same gel and stained for phospho-Akt, total Akt and β-tubulin as loading control. Note that chronic morphine treatment increases basal and Heregulin (40 ng/ml)-stimulated levels of Akt phosphorylation. ( C ) Determination of PARP cleavage in BT474 cells. Cells were cultured in the absence (control) or presence of Morphine (10 µM; 5 d), before cells were washed and grown for an additional 6 h in serum-free Medium either in the absence or presence of Heregulin (40 ng/ml) Morphine (10 µM) and Naloxone (100 µM) as indicated. Samples were analysed by Western blot using an antibody recognizing full length (116 kDa) and cleaved (89 kDa) PARP. The same samples were blotted for β-tubulin (loading control). ( D ) Determination of apoptosis by Annexin V/propidium iodide staining. BT474 cells were cultured on coverslips for 5 d in the presence or absence of Morphine (10 µM), Naloxone (100 µM) and Heregulin (40 ng/ml) alone or in combination as indicated. Cells were sequentially stained with Annexin-FITC (green), propidium iodide (red), fixed and analysed by confocal microscopy. Bar: 20 µm.

Techniques Used: Activation Assay, Incubation, Western Blot, Staining, Cell Culture, Confocal Microscopy

Regulation of BT474 cell proliferation by Morphine. ( A ) Determination of ERK1/2 activation in control and chronically Morphine (10 µM; 5d)-treated cells. Reactions were for 5 min at 37°C in the presence or absence of Morphine (10 µM), Naloxone (100 µM) and Heregulin (40 ng/ml), before ERK1/2 phosphorylation was determined by Western blot using a phospho-specific antibody. Samples from control and chronically Morphine-treated cells were run on the same gel. Immunoreactivity was quantified by video densitometry and normalized to Heregulin-stimulated values in control cells, which were set to 100%. Overall ERK1/2 abundance (42 and 44 kDa forms) was determined on the same samples using a pan reactive ERK1/2 antibody. Equal protein loading was verifies by staining with a β-tubulin antibody. Insets show representative Western blots. *; significantly different at p
Figure Legend Snippet: Regulation of BT474 cell proliferation by Morphine. ( A ) Determination of ERK1/2 activation in control and chronically Morphine (10 µM; 5d)-treated cells. Reactions were for 5 min at 37°C in the presence or absence of Morphine (10 µM), Naloxone (100 µM) and Heregulin (40 ng/ml), before ERK1/2 phosphorylation was determined by Western blot using a phospho-specific antibody. Samples from control and chronically Morphine-treated cells were run on the same gel. Immunoreactivity was quantified by video densitometry and normalized to Heregulin-stimulated values in control cells, which were set to 100%. Overall ERK1/2 abundance (42 and 44 kDa forms) was determined on the same samples using a pan reactive ERK1/2 antibody. Equal protein loading was verifies by staining with a β-tubulin antibody. Insets show representative Western blots. *; significantly different at p

Techniques Used: Activation Assay, Western Blot, Staining

3) Product Images from "BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES"

Article Title: BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES

Journal: Journal of immunology (Baltimore, Md. : 1950)

doi: 10.4049/jimmunol.1302647

Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes
Figure Legend Snippet: Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes

Techniques Used:

Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics
Figure Legend Snippet: Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics

Techniques Used:

Buprenorphine reduces monocyte chemotaxis towards CCL2
Figure Legend Snippet: Buprenorphine reduces monocyte chemotaxis towards CCL2

Techniques Used: Chemotaxis Assay

Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization
Figure Legend Snippet: Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization

Techniques Used:

Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation
Figure Legend Snippet: Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation

Techniques Used:

Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation
Figure Legend Snippet: Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation

Techniques Used:

Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2
Figure Legend Snippet: Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2

Techniques Used:

4) Product Images from "BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES"

Article Title: BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES

Journal: Journal of immunology (Baltimore, Md. : 1950)

doi: 10.4049/jimmunol.1302647

Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes
Figure Legend Snippet: Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes

Techniques Used:

Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics
Figure Legend Snippet: Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics

Techniques Used:

Buprenorphine reduces monocyte chemotaxis towards CCL2
Figure Legend Snippet: Buprenorphine reduces monocyte chemotaxis towards CCL2

Techniques Used: Chemotaxis Assay

Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization
Figure Legend Snippet: Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization

Techniques Used:

Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation
Figure Legend Snippet: Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation

Techniques Used:

Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation
Figure Legend Snippet: Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation

Techniques Used:

Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2
Figure Legend Snippet: Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2

Techniques Used:

5) Product Images from "BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES"

Article Title: BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES

Journal: Journal of immunology (Baltimore, Md. : 1950)

doi: 10.4049/jimmunol.1302647

Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes
Figure Legend Snippet: Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes

Techniques Used:

Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics
Figure Legend Snippet: Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics

Techniques Used:

Buprenorphine reduces monocyte chemotaxis towards CCL2
Figure Legend Snippet: Buprenorphine reduces monocyte chemotaxis towards CCL2

Techniques Used: Chemotaxis Assay

Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization
Figure Legend Snippet: Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization

Techniques Used:

Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation
Figure Legend Snippet: Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation

Techniques Used:

Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation
Figure Legend Snippet: Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation

Techniques Used:

Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2
Figure Legend Snippet: Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2

Techniques Used:

6) Product Images from "RAPID HETEROLOGOUS DESENSITIZATION OF ANTINOCICEPTIVE ACTIVITY BETWEEN MU OR DELTA OPIOID RECEPTORS AND CHEMOKINE RECEPTORS IN RATS"

Article Title: RAPID HETEROLOGOUS DESENSITIZATION OF ANTINOCICEPTIVE ACTIVITY BETWEEN MU OR DELTA OPIOID RECEPTORS AND CHEMOKINE RECEPTORS IN RATS

Journal:

doi: 10.1016/j.drugalcdep.2006.09.010

Antinociception induced by PAG injection of morphine (A) or DPDPE (B) blocked by pretreatment with PAG injection of CXCL12/SDF-1alpha. Rats were given a PAG injection of CXCL12/SDF-1alpha (100 ng) or aCSF 30 min before injection of 100 ng morphine (A)
Figure Legend Snippet: Antinociception induced by PAG injection of morphine (A) or DPDPE (B) blocked by pretreatment with PAG injection of CXCL12/SDF-1alpha. Rats were given a PAG injection of CXCL12/SDF-1alpha (100 ng) or aCSF 30 min before injection of 100 ng morphine (A)

Techniques Used: Injection

Antinociception induced by PAG injection of DAMGO (A) or DPDPE (B) reduced by simultaneous PAG injection of CXCL12/SDF-1alpha. Rats were given a PAG injection of CXCL12/SDF-1alpha (100 ng) or aCSF at the same time as injection of 400 ng DAMGO (A), or
Figure Legend Snippet: Antinociception induced by PAG injection of DAMGO (A) or DPDPE (B) reduced by simultaneous PAG injection of CXCL12/SDF-1alpha. Rats were given a PAG injection of CXCL12/SDF-1alpha (100 ng) or aCSF at the same time as injection of 400 ng DAMGO (A), or

Techniques Used: Injection

7) Product Images from "Central Amygdala Circuits Mediate Hyperalgesia in Alcohol-Dependent Rats"

Article Title: Central Amygdala Circuits Mediate Hyperalgesia in Alcohol-Dependent Rats

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.0483-18.2018

MC4R in CeA and MOR in vlPAG modulate thermal nociception. A , Hindpaw withdrawal latencies of naive (white) and alcohol-dependent (red) rats following intra-CeA infusion of HS014. * p
Figure Legend Snippet: MC4R in CeA and MOR in vlPAG modulate thermal nociception. A , Hindpaw withdrawal latencies of naive (white) and alcohol-dependent (red) rats following intra-CeA infusion of HS014. * p

Techniques Used:

8) Product Images from "BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES"

Article Title: BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES

Journal: Journal of immunology (Baltimore, Md. : 1950)

doi: 10.4049/jimmunol.1302647

Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes
Figure Legend Snippet: Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes

Techniques Used:

Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics
Figure Legend Snippet: Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics

Techniques Used:

Buprenorphine reduces monocyte chemotaxis towards CCL2
Figure Legend Snippet: Buprenorphine reduces monocyte chemotaxis towards CCL2

Techniques Used: Chemotaxis Assay

Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization
Figure Legend Snippet: Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization

Techniques Used:

Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation
Figure Legend Snippet: Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation

Techniques Used:

Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation
Figure Legend Snippet: Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation

Techniques Used:

Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2
Figure Legend Snippet: Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2

Techniques Used:

9) Product Images from "Molecular characterization of eluxadoline as a potential ligand targeting mu-delta opioid receptor heteromers"

Article Title: Molecular characterization of eluxadoline as a potential ligand targeting mu-delta opioid receptor heteromers

Journal: Biochemical pharmacology

doi: 10.1016/j.bcp.2014.09.015

Effect of DAMGO, loperamide and eluxadoline on G-protein activation. (A–C) Membranes (10 μg) from spinal cords of WT, μOR −/− and δOR −/− mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (A), loperamide (B), and eluxadoline (C) (0–10 μM final concentration) as described in Section 2. (D–G) Membranes (20 μg) from the ileum of WT mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (D and G), loperamide (E and G), and eluxadoline (F and G) (0–10 μM final concentration) in the presence or absence of TIPPψ (10 nM final concentration) as described in Section 2. (G) Represents E max (% of basal) obtained with 10 μM final concentration of DAMGO (±10 nM final concentration of TIPPψ), eluxadoline or loperamide. Basal values determined in the absence of the agonist were taken as 100%. Results are the mean ± S.E.M. n = 3–9. n.d., Not determined. * p
Figure Legend Snippet: Effect of DAMGO, loperamide and eluxadoline on G-protein activation. (A–C) Membranes (10 μg) from spinal cords of WT, μOR −/− and δOR −/− mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (A), loperamide (B), and eluxadoline (C) (0–10 μM final concentration) as described in Section 2. (D–G) Membranes (20 μg) from the ileum of WT mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (D and G), loperamide (E and G), and eluxadoline (F and G) (0–10 μM final concentration) in the presence or absence of TIPPψ (10 nM final concentration) as described in Section 2. (G) Represents E max (% of basal) obtained with 10 μM final concentration of DAMGO (±10 nM final concentration of TIPPψ), eluxadoline or loperamide. Basal values determined in the absence of the agonist were taken as 100%. Results are the mean ± S.E.M. n = 3–9. n.d., Not determined. * p

Techniques Used: Activation Assay, Mouse Assay, GTPγS Binding Assay, Concentration Assay

Effect of DAMGO, loperamide and eluxadoline on β-arrestin recruitment. Cells (5000/well) expressing either μ βgal OR (A–C) or μ βgal OR-δOR (D–F) were treated with either DAMGO (A and D), loperamide (B and E), eluxadoline (C and F) (0–10 μM final concentration) in the absence or presence of the δOR antagonist, TIPPψ (10 nM final concentration) for 60 min at 37 °C and β-arrestin recruitment was measured as described in Section 2. Results are the mean ± S.E.M. n = 4–12. * p
Figure Legend Snippet: Effect of DAMGO, loperamide and eluxadoline on β-arrestin recruitment. Cells (5000/well) expressing either μ βgal OR (A–C) or μ βgal OR-δOR (D–F) were treated with either DAMGO (A and D), loperamide (B and E), eluxadoline (C and F) (0–10 μM final concentration) in the absence or presence of the δOR antagonist, TIPPψ (10 nM final concentration) for 60 min at 37 °C and β-arrestin recruitment was measured as described in Section 2. Results are the mean ± S.E.M. n = 4–12. * p

Techniques Used: Expressing, Concentration Assay

10) Product Images from "RAPID HETEROLOGOUS DESENSITIZATION OF ANTINOCICEPTIVE ACTIVITY BETWEEN MU OR DELTA OPIOID RECEPTORS AND CHEMOKINE RECEPTORS IN RATS"

Article Title: RAPID HETEROLOGOUS DESENSITIZATION OF ANTINOCICEPTIVE ACTIVITY BETWEEN MU OR DELTA OPIOID RECEPTORS AND CHEMOKINE RECEPTORS IN RATS

Journal:

doi: 10.1016/j.drugalcdep.2006.09.010

Antinociception induced by PAG injection of morphine (A) or DPDPE (B) blocked by pretreatment with PAG injection of CCL5/RANTES. Rats were given a PAG injection of CCL5/RANTES (100 ng) or aCSF 30 min before injection of 100 ng morphine (A) or 100 ng DPDPE
Figure Legend Snippet: Antinociception induced by PAG injection of morphine (A) or DPDPE (B) blocked by pretreatment with PAG injection of CCL5/RANTES. Rats were given a PAG injection of CCL5/RANTES (100 ng) or aCSF 30 min before injection of 100 ng morphine (A) or 100 ng DPDPE

Techniques Used: Injection

Antinociception induced by PAG injection of DAMGO (A) or DPDPE (B) reduced by simultaneous PAG injection of CCL5/RANTES. Rats were given a PAG injection of CCL5/RANTES (100 ng) or aCSF at the same time as injection of 400 ng DAMGO (A) or 100 ng DPDPE
Figure Legend Snippet: Antinociception induced by PAG injection of DAMGO (A) or DPDPE (B) reduced by simultaneous PAG injection of CCL5/RANTES. Rats were given a PAG injection of CCL5/RANTES (100 ng) or aCSF at the same time as injection of 400 ng DAMGO (A) or 100 ng DPDPE

Techniques Used: Injection

11) Product Images from "BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES"

Article Title: BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES

Journal: Journal of immunology (Baltimore, Md. : 1950)

doi: 10.4049/jimmunol.1302647

Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes
Figure Legend Snippet: Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes

Techniques Used:

Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics
Figure Legend Snippet: Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics

Techniques Used:

Buprenorphine reduces monocyte chemotaxis towards CCL2
Figure Legend Snippet: Buprenorphine reduces monocyte chemotaxis towards CCL2

Techniques Used: Chemotaxis Assay

Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization
Figure Legend Snippet: Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization

Techniques Used:

Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation
Figure Legend Snippet: Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation

Techniques Used:

Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation
Figure Legend Snippet: Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation

Techniques Used:

Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2
Figure Legend Snippet: Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2

Techniques Used:

12) Product Images from "Modulation of neuronal CXCR4 by the μ-opioid agonist DAMGO"

Article Title: Modulation of neuronal CXCR4 by the μ-opioid agonist DAMGO

Journal: Journal of neurovirology

doi: 10.1080/13550280601064798

Effect of DAMGO on surface expression of CXCR4 in SH-SY5Y cells. Surface expression of CXCR4 in SH-SY5Y cells was assessed by flow cytometry (all experiments repeated twice). ( A ) Untreated = blue; DAMGO 10 μ M = green; CXCL12 (1 h) = red; IgG2B-PE isotype control = grey. ( B ) Cells cotreated with DAMGO+CXCL12 are shown in purple.
Figure Legend Snippet: Effect of DAMGO on surface expression of CXCR4 in SH-SY5Y cells. Surface expression of CXCR4 in SH-SY5Y cells was assessed by flow cytometry (all experiments repeated twice). ( A ) Untreated = blue; DAMGO 10 μ M = green; CXCL12 (1 h) = red; IgG2B-PE isotype control = grey. ( B ) Cells cotreated with DAMGO+CXCL12 are shown in purple.

Techniques Used: Expressing, Flow Cytometry, Cytometry

MOR agonists inhibit CXCL12-mediated Akt and ERK phosphorylation in cortical neurons. The effect of DAMGO (1 or 10 μ M) or endomorphin-1 (100 nM) on Akt and ERK1/2 phosphorylation induced by CXCL12 (20 nM, 15 min) was studied by Western blot. A general opioid receptors antagonist, naloxone (NALX, 50 μ M) ( A, B ), or a MOR-selective antagonist, CTAP (1 μ M, D ) was used to determine receptors involved. After blotting with phosphospecific antibodies, membranes were stripped and reblotted using antibodies against total Akt or total ERK1/2. Graphs report average ± SEM of P-Akt or P-ERK band density from three independent experiments. ** P
Figure Legend Snippet: MOR agonists inhibit CXCL12-mediated Akt and ERK phosphorylation in cortical neurons. The effect of DAMGO (1 or 10 μ M) or endomorphin-1 (100 nM) on Akt and ERK1/2 phosphorylation induced by CXCL12 (20 nM, 15 min) was studied by Western blot. A general opioid receptors antagonist, naloxone (NALX, 50 μ M) ( A, B ), or a MOR-selective antagonist, CTAP (1 μ M, D ) was used to determine receptors involved. After blotting with phosphospecific antibodies, membranes were stripped and reblotted using antibodies against total Akt or total ERK1/2. Graphs report average ± SEM of P-Akt or P-ERK band density from three independent experiments. ** P

Techniques Used: Western Blot

DAMGO prevents CXCL12-induced neuroprotection. Cortical neurons were treated with DAMGO (24 h) and subsequently exposed to NMDA (100 μ M) and/or CXCL12 (20 nM) as detailed in the text. Results from three independent experiments with 10 μ MDAMGO are reported in A (** P
Figure Legend Snippet: DAMGO prevents CXCL12-induced neuroprotection. Cortical neurons were treated with DAMGO (24 h) and subsequently exposed to NMDA (100 μ M) and/or CXCL12 (20 nM) as detailed in the text. Results from three independent experiments with 10 μ MDAMGO are reported in A (** P

Techniques Used:

13) Product Images from "BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES"

Article Title: BUPRENORPHINE DECREASES THE CCL2-MEDIATED CHEMOTACTIC RESPONSE OF MONOCYTES

Journal: Journal of immunology (Baltimore, Md. : 1950)

doi: 10.4049/jimmunol.1302647

Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes
Figure Legend Snippet: Buprenorphine reduces CCL2 induced JAM-A phosphorylation in monocytes

Techniques Used:

Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics
Figure Legend Snippet: Identification of monocyte membrane proteins altered by CCL2 plus buprenorphine treatment using proteomics

Techniques Used:

Buprenorphine reduces monocyte chemotaxis towards CCL2
Figure Legend Snippet: Buprenorphine reduces monocyte chemotaxis towards CCL2

Techniques Used: Chemotaxis Assay

Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization
Figure Legend Snippet: Buprenorphine delays the recycling of CCR2, the CCL2 receptor, to the cell membrane after CCL2 induced receptor internalization

Techniques Used:

Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation
Figure Legend Snippet: Buprenorphine reduces CCL2 induced p38 MAPK phosphorylation

Techniques Used:

Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation
Figure Legend Snippet: Effects of buprenorphine and of opioid receptor–specific agonist and antagonists on CCL2 mediated p38 MAPK phosphorylation

Techniques Used:

Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2
Figure Legend Snippet: Buprenorphine inhibits the migratory phenotype of monocytes induced by CCL2

Techniques Used:

Related Articles

Enzyme-linked Immunosorbent Assay:

Article Title: Novel stable cytokine delivery system in physiological pH solution: chitosan oligosaccharide/heparin nanoparticles
Article Snippet: .. Human recombinant VEGF-165m (293-VE-010/CF, DVE00) and enzyme-linked immunosorbent assay kits for VEGF (460-SD-010/CF, DY460) and SDF-1α were purchased from R & D Systems (Minneapolis, MN, USA). .. Anti-VEGF antibody (Cy5) was purchased from Biorbyt LLC (San Francisco, CA, USA).

Article Title: Nanoparticle-modified chitosan-agarose-gelatin scaffold for sustained release of SDF-1 and BMP-2
Article Snippet: .. SDF-1 (460-SD-010/CF) and ELISA kits for SDF-1 were purchased from R & D Systems (DY 460). ..

Injection:

Article Title: Stromal Cell-Derived Factor-1 Alpha is Cardioprotective After Myocardial Infarction
Article Snippet: .. Each injection was 5 μl of one of the following in a collagen base: PBS; recombinant (amino acids 22–89) mature mouse SDF-1α protein (R & D Systems, catalog # 460-SD-010) at 60 ng/μl; synthetic thymosin β4 at 40 ng/μl; and SDF-1α and thymosin β4 at 60 ng/μl and 40 ng/μl, respectively. ..

Recombinant:

Article Title: CXCR7 regulates breast tumor metastasis and angiogenesis in vivo and in vitro
Article Snippet: .. Chemokines and reagents Recombinant CXCL12/SDF-1α was obtained from R & D Systems, Inc. (cat. no. 350-NS; Minneapolis, MN, USA). .. The CXCR7 antagonist CCX771 was obtained from ChemoCentryx, Inc. (Mountain View, CA, USA).

Article Title: Novel stable cytokine delivery system in physiological pH solution: chitosan oligosaccharide/heparin nanoparticles
Article Snippet: .. Human recombinant VEGF-165m (293-VE-010/CF, DVE00) and enzyme-linked immunosorbent assay kits for VEGF (460-SD-010/CF, DY460) and SDF-1α were purchased from R & D Systems (Minneapolis, MN, USA). .. Anti-VEGF antibody (Cy5) was purchased from Biorbyt LLC (San Francisco, CA, USA).

Article Title: RGS10 Regulates the Expression of Cyclooxygenase-2 and Tumor Necrosis Factor Alpha through a G Protein–Independent Mechanism
Article Snippet: .. Lipopolysaccharide was purchased from Sigma-Aldrich (St. Louis, MO), recombinant mouse CXCL12/SDF-1 alpha protein was purchased from R & D systems (Minneapolis, MN), pertussis toxin (PTX) was obtained from Tocris (Pittsburgh, PA), and lysophosphatidic acid (LPA) was obtained from Avanti Polar Lipids (Alabaster, AL). .. Real-time polymerase chain reaction was performed using the following primer sequences: mouse RGS10 forward: 5′-TCCATGACGGAGATGGGAG-3′, mouse RGS10 reverse: 5′-AACAAGACATTCTCTTCGCTGAA-3′; mouse RGS2 forward: 5′-GAGAAAATGAAGCGGACACTCT-3′, mouse RGS2 reverse: 5′-GCAGCCAGCCCATATTTACTG-3′; mouse RGS12 forward: 5′-GTGACCGTTGATGCTTTCG-3′, mouse RGS12 reverse: 5′-ATCGCATGTCCCACTATTCC-3′; and mouse RGS14 forward: 5′-AAATCCCCGCTGTACCAAG-3′, mouse RGS14 reverse: 5′-GTGACTTCCCAGGCTTCAG-3′.

Article Title: Stromal Cell-Derived Factor-1 Alpha is Cardioprotective After Myocardial Infarction
Article Snippet: .. Each injection was 5 μl of one of the following in a collagen base: PBS; recombinant (amino acids 22–89) mature mouse SDF-1α protein (R & D Systems, catalog # 460-SD-010) at 60 ng/μl; synthetic thymosin β4 at 40 ng/μl; and SDF-1α and thymosin β4 at 60 ng/μl and 40 ng/μl, respectively. ..

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    R&D Systems damgo
    Effect of <t>DAMGO,</t> loperamide and eluxadoline on G-protein activation. (A–C) Membranes (10 μg) from spinal cords of WT, μOR −/− and δOR −/− mice were subjected to a [ 35 <t>S]GTPγS</t> binding assay using DAMGO (A), loperamide (B), and eluxadoline (C) (0–10 μM final concentration) as described in Section 2. (D–G) Membranes (20 μg) from the ileum of WT mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (D and G), loperamide (E and G), and eluxadoline (F and G) (0–10 μM final concentration) in the presence or absence of TIPPψ (10 nM final concentration) as described in Section 2. (G) Represents E max (% of basal) obtained with 10 μM final concentration of DAMGO (±10 nM final concentration of TIPPψ), eluxadoline or loperamide. Basal values determined in the absence of the agonist were taken as 100%. Results are the mean ± S.E.M. n = 3–9. n.d., Not determined. * p
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    Effect of DAMGO, loperamide and eluxadoline on G-protein activation. (A–C) Membranes (10 μg) from spinal cords of WT, μOR −/− and δOR −/− mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (A), loperamide (B), and eluxadoline (C) (0–10 μM final concentration) as described in Section 2. (D–G) Membranes (20 μg) from the ileum of WT mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (D and G), loperamide (E and G), and eluxadoline (F and G) (0–10 μM final concentration) in the presence or absence of TIPPψ (10 nM final concentration) as described in Section 2. (G) Represents E max (% of basal) obtained with 10 μM final concentration of DAMGO (±10 nM final concentration of TIPPψ), eluxadoline or loperamide. Basal values determined in the absence of the agonist were taken as 100%. Results are the mean ± S.E.M. n = 3–9. n.d., Not determined. * p

    Journal: Biochemical pharmacology

    Article Title: Molecular characterization of eluxadoline as a potential ligand targeting mu-delta opioid receptor heteromers

    doi: 10.1016/j.bcp.2014.09.015

    Figure Lengend Snippet: Effect of DAMGO, loperamide and eluxadoline on G-protein activation. (A–C) Membranes (10 μg) from spinal cords of WT, μOR −/− and δOR −/− mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (A), loperamide (B), and eluxadoline (C) (0–10 μM final concentration) as described in Section 2. (D–G) Membranes (20 μg) from the ileum of WT mice were subjected to a [ 35 S]GTPγS binding assay using DAMGO (D and G), loperamide (E and G), and eluxadoline (F and G) (0–10 μM final concentration) in the presence or absence of TIPPψ (10 nM final concentration) as described in Section 2. (G) Represents E max (% of basal) obtained with 10 μM final concentration of DAMGO (±10 nM final concentration of TIPPψ), eluxadoline or loperamide. Basal values determined in the absence of the agonist were taken as 100%. Results are the mean ± S.E.M. n = 3–9. n.d., Not determined. * p

    Article Snippet: Membranes (10 or 20 μg) were subjected to a [35 S]GTPγS binding assay using DAMGO (R & D Systems, Minneapolis, USA), loperamide (Toronto Research Chemicals Inc., Ontario, Canada), eluxadoline (Furiex, Morrisville, NC, USA) (0–10 μM final concentration) in the presence or absence of TIPPψ (10 nM final concentration) (a gift from Dr. Peter Schiller, Institut de Reserches Cliniques de Montreal, Montreal, ON, Canada) as described previously [ ].

    Techniques: Activation Assay, Mouse Assay, GTPγS Binding Assay, Concentration Assay

    Effect of DAMGO, loperamide and eluxadoline on β-arrestin recruitment. Cells (5000/well) expressing either μ βgal OR (A–C) or μ βgal OR-δOR (D–F) were treated with either DAMGO (A and D), loperamide (B and E), eluxadoline (C and F) (0–10 μM final concentration) in the absence or presence of the δOR antagonist, TIPPψ (10 nM final concentration) for 60 min at 37 °C and β-arrestin recruitment was measured as described in Section 2. Results are the mean ± S.E.M. n = 4–12. * p

    Journal: Biochemical pharmacology

    Article Title: Molecular characterization of eluxadoline as a potential ligand targeting mu-delta opioid receptor heteromers

    doi: 10.1016/j.bcp.2014.09.015

    Figure Lengend Snippet: Effect of DAMGO, loperamide and eluxadoline on β-arrestin recruitment. Cells (5000/well) expressing either μ βgal OR (A–C) or μ βgal OR-δOR (D–F) were treated with either DAMGO (A and D), loperamide (B and E), eluxadoline (C and F) (0–10 μM final concentration) in the absence or presence of the δOR antagonist, TIPPψ (10 nM final concentration) for 60 min at 37 °C and β-arrestin recruitment was measured as described in Section 2. Results are the mean ± S.E.M. n = 4–12. * p

    Article Snippet: Membranes (10 or 20 μg) were subjected to a [35 S]GTPγS binding assay using DAMGO (R & D Systems, Minneapolis, USA), loperamide (Toronto Research Chemicals Inc., Ontario, Canada), eluxadoline (Furiex, Morrisville, NC, USA) (0–10 μM final concentration) in the presence or absence of TIPPψ (10 nM final concentration) (a gift from Dr. Peter Schiller, Institut de Reserches Cliniques de Montreal, Montreal, ON, Canada) as described previously [ ].

    Techniques: Expressing, Concentration Assay