trpv2  (Alomone Labs)


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    Structured Review

    Alomone Labs trpv2
    Expression of TRPC and TRPV proteins in rat proximal and distal PVSMC and PV as determined by Western blotting using rat brain as positive control. Data show representative blots for TRPC1, TRPC4, TRPC6, <t>TRPV2,</t> TRPV4, and β-actin in rat distal PVSMC ( top : n = 5) and PV ( bottom : n = 3). * P
    Trpv2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Expression of store-operated Ca2+ entry and transient receptor potential canonical and vanilloid-related proteins in rat distal pulmonary venous smooth muscle"

    Article Title: Expression of store-operated Ca2+ entry and transient receptor potential canonical and vanilloid-related proteins in rat distal pulmonary venous smooth muscle

    Journal: American Journal of Physiology - Lung Cellular and Molecular Physiology

    doi: 10.1152/ajplung.00176.2009

    Expression of TRPC and TRPV proteins in rat proximal and distal PVSMC and PV as determined by Western blotting using rat brain as positive control. Data show representative blots for TRPC1, TRPC4, TRPC6, TRPV2, TRPV4, and β-actin in rat distal PVSMC ( top : n = 5) and PV ( bottom : n = 3). * P
    Figure Legend Snippet: Expression of TRPC and TRPV proteins in rat proximal and distal PVSMC and PV as determined by Western blotting using rat brain as positive control. Data show representative blots for TRPC1, TRPC4, TRPC6, TRPV2, TRPV4, and β-actin in rat distal PVSMC ( top : n = 5) and PV ( bottom : n = 3). * P

    Techniques Used: Expressing, Western Blot, Positive Control

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    Alomone Labs anti par2 antibody
    Immunolocalization and functional expression of <t>PAR2</t> in the CCD. A , DAPI ( panels a and c ) and PAR2 labeling ( green , panels b and d ) in CCD from WT ( panels a and b ) and PAR2 −/− mice ( panels c and d ). Exposure times were the same for WT
    Anti Par2 Antibody, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti par2 antibody/product/Alomone Labs
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti par2 antibody - by Bioz Stars, 2022-05
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    94
    Alomone Labs rabbit anti trpv2
    <t>TRPV2</t> expression in spinal cord samples from WT and EAE mice. ( A ) Immunohistochemical staining of TRPV2 in spinal cord of control and EAE-induced mice in the onset, peak and in the chronic phase, during remission. In control conditions, TRPV2 is expressed in neurons in GM (inset, arrows), and in oligodendrocytes in WM (inset, arrowheads). After EAE induction, an increase in TRPV2 expression is mainly located in inflammatory focuses at the peak clinical symptomatology in WM (empty arrowheads). ( B ) MSRA and TRPV2 protein expression in thoracic spinal cord samples from CFA and MOG mice (9, 14, 21 and 28 days post-immunization). ( B ) A significant increase in TRPV2 protein levels (#, p = 0.0014) is determined in MOG14 mice when compared with CFA ( p
    Rabbit Anti Trpv2, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti trpv2/product/Alomone Labs
    Average 94 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit anti trpv2 - by Bioz Stars, 2022-05
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    Image Search Results


    Immunolocalization and functional expression of PAR2 in the CCD. A , DAPI ( panels a and c ) and PAR2 labeling ( green , panels b and d ) in CCD from WT ( panels a and b ) and PAR2 −/− mice ( panels c and d ). Exposure times were the same for WT

    Journal: The Journal of Biological Chemistry

    Article Title: Renal Proteinase-activated Receptor 2, a New Actor in the Control of Blood Pressure and Plasma Potassium Level *

    doi: 10.1074/jbc.M112.446393

    Figure Lengend Snippet: Immunolocalization and functional expression of PAR2 in the CCD. A , DAPI ( panels a and c ) and PAR2 labeling ( green , panels b and d ) in CCD from WT ( panels a and b ) and PAR2 −/− mice ( panels c and d ). Exposure times were the same for WT

    Article Snippet: The specificity of the anti-PAR2 antibody used in this study was demonstrated by showing immunolabeling in CCDs from wild type (WT) but not PAR2−/− mice ( A ).

    Techniques: Functional Assay, Expressing, Labeling, Mouse Assay

    Role of PAR2 in the renal handling of sodium. A–D , daily urinary excretion of Na + ( U Na+ ) and Ca 2+ ( U Ca++ ) ( A and D ) in mmol of Na + or Ca 2+ /mmol of creatinine ( U Creat )) and systolic blood pressure ( B ) in PAR2 −/− ( solid line ) and

    Journal: The Journal of Biological Chemistry

    Article Title: Renal Proteinase-activated Receptor 2, a New Actor in the Control of Blood Pressure and Plasma Potassium Level *

    doi: 10.1074/jbc.M112.446393

    Figure Lengend Snippet: Role of PAR2 in the renal handling of sodium. A–D , daily urinary excretion of Na + ( U Na+ ) and Ca 2+ ( U Ca++ ) ( A and D ) in mmol of Na + or Ca 2+ /mmol of creatinine ( U Creat )) and systolic blood pressure ( B ) in PAR2 −/− ( solid line ) and

    Article Snippet: The specificity of the anti-PAR2 antibody used in this study was demonstrated by showing immunolabeling in CCDs from wild type (WT) but not PAR2−/− mice ( A ).

    Techniques:

    Role of ERK in PAR2 signaling. A , representative immunoblot and mean phospho-ERK/ERK ratio in rat CCDs incubated for 10 min at 37 °C under basal conditions ( B ) or in the presence of 40 μ m AP. Values are means ± S.E. from five experiments.

    Journal: The Journal of Biological Chemistry

    Article Title: Renal Proteinase-activated Receptor 2, a New Actor in the Control of Blood Pressure and Plasma Potassium Level *

    doi: 10.1074/jbc.M112.446393

    Figure Lengend Snippet: Role of ERK in PAR2 signaling. A , representative immunoblot and mean phospho-ERK/ERK ratio in rat CCDs incubated for 10 min at 37 °C under basal conditions ( B ) or in the presence of 40 μ m AP. Values are means ± S.E. from five experiments.

    Article Snippet: The specificity of the anti-PAR2 antibody used in this study was demonstrated by showing immunolabeling in CCDs from wild type (WT) but not PAR2−/− mice ( A ).

    Techniques: Incubation

    Effect of diuretics on sodium and calcium excretion in wild type and PAR2 −/− mice. A and B , urinary excretion of Na + ( A , U Na+ ) and Ca 2+ ( B , U Ca++ ) before and after a single administration of diuretics, at time 0, to PAR2 −/−

    Journal: The Journal of Biological Chemistry

    Article Title: Renal Proteinase-activated Receptor 2, a New Actor in the Control of Blood Pressure and Plasma Potassium Level *

    doi: 10.1074/jbc.M112.446393

    Figure Lengend Snippet: Effect of diuretics on sodium and calcium excretion in wild type and PAR2 −/− mice. A and B , urinary excretion of Na + ( A , U Na+ ) and Ca 2+ ( B , U Ca++ ) before and after a single administration of diuretics, at time 0, to PAR2 −/−

    Article Snippet: The specificity of the anti-PAR2 antibody used in this study was demonstrated by showing immunolabeling in CCDs from wild type (WT) but not PAR2−/− mice ( A ).

    Techniques: Mouse Assay

    Effect of PAR2 activation on sodium transport in the CCD. A , sodium reabsorption flux ( J Na+ , in picoequivalent of Na + /mm/min) was measured in normal rat CCDs under basal condition ( B ) or after the addition of 10 n m trypsin ( Try ) to the bath. CCDs were

    Journal: The Journal of Biological Chemistry

    Article Title: Renal Proteinase-activated Receptor 2, a New Actor in the Control of Blood Pressure and Plasma Potassium Level *

    doi: 10.1074/jbc.M112.446393

    Figure Lengend Snippet: Effect of PAR2 activation on sodium transport in the CCD. A , sodium reabsorption flux ( J Na+ , in picoequivalent of Na + /mm/min) was measured in normal rat CCDs under basal condition ( B ) or after the addition of 10 n m trypsin ( Try ) to the bath. CCDs were

    Article Snippet: The specificity of the anti-PAR2 antibody used in this study was demonstrated by showing immunolabeling in CCDs from wild type (WT) but not PAR2−/− mice ( A ).

    Techniques: Activation Assay

    PAR2 and Sodium Homeostasis

    Journal: The Journal of Biological Chemistry

    Article Title: Renal Proteinase-activated Receptor 2, a New Actor in the Control of Blood Pressure and Plasma Potassium Level *

    doi: 10.1074/jbc.M112.446393

    Figure Lengend Snippet: PAR2 and Sodium Homeostasis

    Article Snippet: The specificity of the anti-PAR2 antibody used in this study was demonstrated by showing immunolabeling in CCDs from wild type (WT) but not PAR2−/− mice ( A ).

    Techniques:

    Role of PAR2 on the renal transport of potassium. A , Na + and K + fluxes ( J Na+ and J K+ , respectively, in picoequivalent of Na + or K + /mm/min) in microperfused rat CCDs. Experiments were performed in the absence of bicarbonate, which suppresses electroneutral

    Journal: The Journal of Biological Chemistry

    Article Title: Renal Proteinase-activated Receptor 2, a New Actor in the Control of Blood Pressure and Plasma Potassium Level *

    doi: 10.1074/jbc.M112.446393

    Figure Lengend Snippet: Role of PAR2 on the renal transport of potassium. A , Na + and K + fluxes ( J Na+ and J K+ , respectively, in picoequivalent of Na + or K + /mm/min) in microperfused rat CCDs. Experiments were performed in the absence of bicarbonate, which suppresses electroneutral

    Article Snippet: The specificity of the anti-PAR2 antibody used in this study was demonstrated by showing immunolabeling in CCDs from wild type (WT) but not PAR2−/− mice ( A ).

    Techniques:

    Schematic representation of aPA-induced proinflammatory cytokine IL-8 by PAR2 pathway in HCE cells. Acanthamoeba plasminogen activator activates PAR2, but not PAR1, in corneal epithelial cells, which upregulates IL-8 transcript and protein production.

    Journal: Investigative Ophthalmology & Visual Science

    Article Title: Protease-Activated Receptor 2 (PAR2) Is Upregulated by Acanthamoeba Plasminogen Activator (aPA) and Induces Proinflammatory Cytokine in Human Corneal Epithelial Cells

    doi: 10.1167/iovs.14-14486

    Figure Lengend Snippet: Schematic representation of aPA-induced proinflammatory cytokine IL-8 by PAR2 pathway in HCE cells. Acanthamoeba plasminogen activator activates PAR2, but not PAR1, in corneal epithelial cells, which upregulates IL-8 transcript and protein production.

    Article Snippet: Anti-PAR1 antibody was diluted 1:250 in blocking solution at 0.8 mg/mL, and anti-PAR2 antibody was diluted 1:500 in blocking solution at 0.6 mg/mL overnight at 4°C.

    Techniques:

    PAR2 surface protein expression is upregulated by aPA in HCE cells. HCE cells were incubated with or without aPA (100 μg/mL), PAR1 agonist (thrombin, 10 μM), and PAR2 agonist (SLIGRL-NH2, 100 μM) for 24 hours. PAR1 ( A ) and PAR2

    Journal: Investigative Ophthalmology & Visual Science

    Article Title: Protease-Activated Receptor 2 (PAR2) Is Upregulated by Acanthamoeba Plasminogen Activator (aPA) and Induces Proinflammatory Cytokine in Human Corneal Epithelial Cells

    doi: 10.1167/iovs.14-14486

    Figure Lengend Snippet: PAR2 surface protein expression is upregulated by aPA in HCE cells. HCE cells were incubated with or without aPA (100 μg/mL), PAR1 agonist (thrombin, 10 μM), and PAR2 agonist (SLIGRL-NH2, 100 μM) for 24 hours. PAR1 ( A ) and PAR2

    Article Snippet: Anti-PAR1 antibody was diluted 1:250 in blocking solution at 0.8 mg/mL, and anti-PAR2 antibody was diluted 1:500 in blocking solution at 0.6 mg/mL overnight at 4°C.

    Techniques: Expressing, Incubation

    Acanthamoeba plasminogen activator–induced upregulation of surface PAR2 expression in HCE cells. HCE cells were incubated with or without aPA (100 μg/mL), PAR1 agonist (thrombin, 10 μM), and PAR2 agonist (SLIGRL-NH2, 100 μM)

    Journal: Investigative Ophthalmology & Visual Science

    Article Title: Protease-Activated Receptor 2 (PAR2) Is Upregulated by Acanthamoeba Plasminogen Activator (aPA) and Induces Proinflammatory Cytokine in Human Corneal Epithelial Cells

    doi: 10.1167/iovs.14-14486

    Figure Lengend Snippet: Acanthamoeba plasminogen activator–induced upregulation of surface PAR2 expression in HCE cells. HCE cells were incubated with or without aPA (100 μg/mL), PAR1 agonist (thrombin, 10 μM), and PAR2 agonist (SLIGRL-NH2, 100 μM)

    Article Snippet: Anti-PAR1 antibody was diluted 1:250 in blocking solution at 0.8 mg/mL, and anti-PAR2 antibody was diluted 1:500 in blocking solution at 0.6 mg/mL overnight at 4°C.

    Techniques: Expressing, Incubation

    Protease-activated receptor (PAR) 2, but not PAR1, is upregulated by Acanthamoeba plasminogen activator in HCE cells. HCE cells were incubated with aPA (100 μg/mL), PAR1 agonists (thrombin, 10 μM; TRAP-6, 10 μM), and PAR2 agonists

    Journal: Investigative Ophthalmology & Visual Science

    Article Title: Protease-Activated Receptor 2 (PAR2) Is Upregulated by Acanthamoeba Plasminogen Activator (aPA) and Induces Proinflammatory Cytokine in Human Corneal Epithelial Cells

    doi: 10.1167/iovs.14-14486

    Figure Lengend Snippet: Protease-activated receptor (PAR) 2, but not PAR1, is upregulated by Acanthamoeba plasminogen activator in HCE cells. HCE cells were incubated with aPA (100 μg/mL), PAR1 agonists (thrombin, 10 μM; TRAP-6, 10 μM), and PAR2 agonists

    Article Snippet: Anti-PAR1 antibody was diluted 1:250 in blocking solution at 0.8 mg/mL, and anti-PAR2 antibody was diluted 1:500 in blocking solution at 0.6 mg/mL overnight at 4°C.

    Techniques: Incubation

    Acanthamoeba plasminogen activator upregulates IL-8 by PAR2 pathway in HCE cells. HCE cells were incubated with aPA (100 μg/mL) and PAR2 agonists (SLIGRL-NH2, 100 μM; AC 55541, 10 μM) for 24 hours. Inhibition of PAR2 involved preincubating

    Journal: Investigative Ophthalmology & Visual Science

    Article Title: Protease-Activated Receptor 2 (PAR2) Is Upregulated by Acanthamoeba Plasminogen Activator (aPA) and Induces Proinflammatory Cytokine in Human Corneal Epithelial Cells

    doi: 10.1167/iovs.14-14486

    Figure Lengend Snippet: Acanthamoeba plasminogen activator upregulates IL-8 by PAR2 pathway in HCE cells. HCE cells were incubated with aPA (100 μg/mL) and PAR2 agonists (SLIGRL-NH2, 100 μM; AC 55541, 10 μM) for 24 hours. Inhibition of PAR2 involved preincubating

    Article Snippet: Anti-PAR1 antibody was diluted 1:250 in blocking solution at 0.8 mg/mL, and anti-PAR2 antibody was diluted 1:500 in blocking solution at 0.6 mg/mL overnight at 4°C.

    Techniques: Incubation, Inhibition

    PAR2 and TRPV4 expression in the hippocampus. Immunohistochemistry discloses the expression of PAR2 and TRPV4 in the hippocampus. A comparable expression pattern is observed: high levels of PAR2 and TRPV4 are detected in CA1 stratum pyramidale (pcl, pyramidal cell layer; oriens, stratum oriens; rad, stratum radiatum; la-mol, stratum lacunosum-moleculare). No pronounced colocalization between PAR2 and GFAP was detected. Scale bars: 100 and 10 μm, n = 9 slices out of three animals.

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Protease Activated Receptor 2 (PAR2) Induces Long-Term Depression in the Hippocampus through Transient Receptor Potential Vanilloid 4 (TRPV4)

    doi: 10.3389/fnmol.2017.00042

    Figure Lengend Snippet: PAR2 and TRPV4 expression in the hippocampus. Immunohistochemistry discloses the expression of PAR2 and TRPV4 in the hippocampus. A comparable expression pattern is observed: high levels of PAR2 and TRPV4 are detected in CA1 stratum pyramidale (pcl, pyramidal cell layer; oriens, stratum oriens; rad, stratum radiatum; la-mol, stratum lacunosum-moleculare). No pronounced colocalization between PAR2 and GFAP was detected. Scale bars: 100 and 10 μm, n = 9 slices out of three animals.

    Article Snippet: Immunohistochemistry The following primary antibodies were used for immunodetection: goat anti-PAR2 (sc-8205, Santa Cruz, 1:25), rabbit anti-TRPV4 (ACC-124, Alomone Labs, 1:50), rabbit anti-PAR2 (APR-032, Alomone Labs 1:500) and mouse anti-GFAP (G3893, Sigma-Aldrich, 1:2000).

    Techniques: Expressing, Immunohistochemistry

    PAR2-activation induces a depression of synaptic transmission at Schaffer collateral-CA1 synapses in the hippocampus. (A) Application of PAR2-agonist (10 μM AC55541) causes LTD. (B) Removal of the PAR2-agonist (10 μM AC55541) following induction of LTD does not affect the stability of synaptic depression. (C) In presence of a PAR2-antagonist (50 μM FSLLRY-NH 2 ) the PAR2-agonist (10 μM AC55541) is not able to induce synaptic depression. (D) Application of PAR2-agonist (10 μM AC55541) at different concentrations results in similar levels of synaptic depression. (E) In a two pathways experimental setting, low frequency stimulation (LFS, 1 Hz, 900 pulses) and PAR2-activation (10 μM AC55541) induce similar levels of LTD. (F) LFS-induced LTD is not blocked by the PAR2-antagonist. (G) In a two pathways experimental setting, the NMDAR-antagonist (50 μM APV) blocks both LFS-induced LTD and PAR2-induced LTD. (H) While the group I mGluR-antagonist MCPG (200 μM) partially affects LFS-LTD it does not influence PAR2-LTD. Averaged EPSP are plotted versus time. Representative traces at indicated times (a, b) are shown on top of each section, n = 12 slices for each experiment, refer to text for statistics.

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Protease Activated Receptor 2 (PAR2) Induces Long-Term Depression in the Hippocampus through Transient Receptor Potential Vanilloid 4 (TRPV4)

    doi: 10.3389/fnmol.2017.00042

    Figure Lengend Snippet: PAR2-activation induces a depression of synaptic transmission at Schaffer collateral-CA1 synapses in the hippocampus. (A) Application of PAR2-agonist (10 μM AC55541) causes LTD. (B) Removal of the PAR2-agonist (10 μM AC55541) following induction of LTD does not affect the stability of synaptic depression. (C) In presence of a PAR2-antagonist (50 μM FSLLRY-NH 2 ) the PAR2-agonist (10 μM AC55541) is not able to induce synaptic depression. (D) Application of PAR2-agonist (10 μM AC55541) at different concentrations results in similar levels of synaptic depression. (E) In a two pathways experimental setting, low frequency stimulation (LFS, 1 Hz, 900 pulses) and PAR2-activation (10 μM AC55541) induce similar levels of LTD. (F) LFS-induced LTD is not blocked by the PAR2-antagonist. (G) In a two pathways experimental setting, the NMDAR-antagonist (50 μM APV) blocks both LFS-induced LTD and PAR2-induced LTD. (H) While the group I mGluR-antagonist MCPG (200 μM) partially affects LFS-LTD it does not influence PAR2-LTD. Averaged EPSP are plotted versus time. Representative traces at indicated times (a, b) are shown on top of each section, n = 12 slices for each experiment, refer to text for statistics.

    Article Snippet: Immunohistochemistry The following primary antibodies were used for immunodetection: goat anti-PAR2 (sc-8205, Santa Cruz, 1:25), rabbit anti-TRPV4 (ACC-124, Alomone Labs, 1:50), rabbit anti-PAR2 (APR-032, Alomone Labs 1:500) and mouse anti-GFAP (G3893, Sigma-Aldrich, 1:2000).

    Techniques: Activation Assay, Transmission Assay

    PAR2 induces LTD through the activation of TRPV4. (A) Application of TRPV4-agonist (2 μM RN1747) causes LTD. (B) Removal of the TRPV4-agonist (2 μM RN1747) following induction of LTD does not affect the stability of synaptic depression. (C) In presence of the TRPV4-antagonist (10 μM RN1734) the TRPV4-agonist is not able to induce synaptic depression. (D) In a two pathways experimental setting, low frequency stimulation (LFS, 1 Hz, 900 pulses) and TRPV4-agonist application induce similar levels of LTD. (E) LFS-induced LTD is not blocked by the TRPV4-antagonist. (F) Application of PAR2-agonist (10 μM AC55541) in presence of a TRPV4-antagonist (10 μM RN1734) blocks PAR2-induced LTD. (G) Application of TRPV4-agonist (2 μM RN1747) in presence of PAR2-antagonist (50 μM FSLLRY-NH 2 ) does not affect TRPV4-induced LTD. (H) Once PAR2-agonist mediated LTD is established, the TRPV4-agonist (2 μM RN1747) does not further de-potentiate a second pathway at adjusted response level (upward arrow). Averaged EPSP are plotted versus time. Representative traces at indicated times (a, b) are shown on top of each section, n = 12 slices for each experiments, refer to text for statistics.

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Protease Activated Receptor 2 (PAR2) Induces Long-Term Depression in the Hippocampus through Transient Receptor Potential Vanilloid 4 (TRPV4)

    doi: 10.3389/fnmol.2017.00042

    Figure Lengend Snippet: PAR2 induces LTD through the activation of TRPV4. (A) Application of TRPV4-agonist (2 μM RN1747) causes LTD. (B) Removal of the TRPV4-agonist (2 μM RN1747) following induction of LTD does not affect the stability of synaptic depression. (C) In presence of the TRPV4-antagonist (10 μM RN1734) the TRPV4-agonist is not able to induce synaptic depression. (D) In a two pathways experimental setting, low frequency stimulation (LFS, 1 Hz, 900 pulses) and TRPV4-agonist application induce similar levels of LTD. (E) LFS-induced LTD is not blocked by the TRPV4-antagonist. (F) Application of PAR2-agonist (10 μM AC55541) in presence of a TRPV4-antagonist (10 μM RN1734) blocks PAR2-induced LTD. (G) Application of TRPV4-agonist (2 μM RN1747) in presence of PAR2-antagonist (50 μM FSLLRY-NH 2 ) does not affect TRPV4-induced LTD. (H) Once PAR2-agonist mediated LTD is established, the TRPV4-agonist (2 μM RN1747) does not further de-potentiate a second pathway at adjusted response level (upward arrow). Averaged EPSP are plotted versus time. Representative traces at indicated times (a, b) are shown on top of each section, n = 12 slices for each experiments, refer to text for statistics.

    Article Snippet: Immunohistochemistry The following primary antibodies were used for immunodetection: goat anti-PAR2 (sc-8205, Santa Cruz, 1:25), rabbit anti-TRPV4 (ACC-124, Alomone Labs, 1:50), rabbit anti-PAR2 (APR-032, Alomone Labs 1:500) and mouse anti-GFAP (G3893, Sigma-Aldrich, 1:2000).

    Techniques: Activation Assay

    TRPV4-mediated LTD depends on NMDAR-activity. (A) Similar to PAR2-induced LTD (c.f., Figures 1G,H ), the NMDAR-antagonist (50 μM APV) blocks TRPV4 (2 μM RN1747)-induced LTD, while (B) application of a TRPV4-agonist (2 μM RN1747) induces LTD in presence of the mGluR-antagonist (200 μM MCGP). Averaged EPSP are plotted versus time. Representative traces at indicated times (a, b) are shown on top of each section.

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Protease Activated Receptor 2 (PAR2) Induces Long-Term Depression in the Hippocampus through Transient Receptor Potential Vanilloid 4 (TRPV4)

    doi: 10.3389/fnmol.2017.00042

    Figure Lengend Snippet: TRPV4-mediated LTD depends on NMDAR-activity. (A) Similar to PAR2-induced LTD (c.f., Figures 1G,H ), the NMDAR-antagonist (50 μM APV) blocks TRPV4 (2 μM RN1747)-induced LTD, while (B) application of a TRPV4-agonist (2 μM RN1747) induces LTD in presence of the mGluR-antagonist (200 μM MCGP). Averaged EPSP are plotted versus time. Representative traces at indicated times (a, b) are shown on top of each section.

    Article Snippet: Immunohistochemistry The following primary antibodies were used for immunodetection: goat anti-PAR2 (sc-8205, Santa Cruz, 1:25), rabbit anti-TRPV4 (ACC-124, Alomone Labs, 1:50), rabbit anti-PAR2 (APR-032, Alomone Labs 1:500) and mouse anti-GFAP (G3893, Sigma-Aldrich, 1:2000).

    Techniques: Activity Assay

    PAR2-mediated LTD is protein kinase A (PKA)-dependent. (A) PAR2-agonist (10 μM AC55541) in presence of a PKA-inhibitor (2 μM KT5720) KT5720 (2 μM) fails to induce LTD. (B) Application of a protein kinase C (PKC) inhibitor (2 μM GF109203x) does not affect the induction of PAR2-mediated LTD. Averaged EPSP are plotted versus time. Representative traces at indicated times (a, b) are shown on top of each section.

    Journal: Frontiers in Molecular Neuroscience

    Article Title: Protease Activated Receptor 2 (PAR2) Induces Long-Term Depression in the Hippocampus through Transient Receptor Potential Vanilloid 4 (TRPV4)

    doi: 10.3389/fnmol.2017.00042

    Figure Lengend Snippet: PAR2-mediated LTD is protein kinase A (PKA)-dependent. (A) PAR2-agonist (10 μM AC55541) in presence of a PKA-inhibitor (2 μM KT5720) KT5720 (2 μM) fails to induce LTD. (B) Application of a protein kinase C (PKC) inhibitor (2 μM GF109203x) does not affect the induction of PAR2-mediated LTD. Averaged EPSP are plotted versus time. Representative traces at indicated times (a, b) are shown on top of each section.

    Article Snippet: Immunohistochemistry The following primary antibodies were used for immunodetection: goat anti-PAR2 (sc-8205, Santa Cruz, 1:25), rabbit anti-TRPV4 (ACC-124, Alomone Labs, 1:50), rabbit anti-PAR2 (APR-032, Alomone Labs 1:500) and mouse anti-GFAP (G3893, Sigma-Aldrich, 1:2000).

    Techniques:

    TRPV2 expression in spinal cord samples from WT and EAE mice. ( A ) Immunohistochemical staining of TRPV2 in spinal cord of control and EAE-induced mice in the onset, peak and in the chronic phase, during remission. In control conditions, TRPV2 is expressed in neurons in GM (inset, arrows), and in oligodendrocytes in WM (inset, arrowheads). After EAE induction, an increase in TRPV2 expression is mainly located in inflammatory focuses at the peak clinical symptomatology in WM (empty arrowheads). ( B ) MSRA and TRPV2 protein expression in thoracic spinal cord samples from CFA and MOG mice (9, 14, 21 and 28 days post-immunization). ( B ) A significant increase in TRPV2 protein levels (#, p = 0.0014) is determined in MOG14 mice when compared with CFA ( p

    Journal: International Journal of Molecular Sciences

    Article Title: TRPV2: A Key Player in Myelination Disorders of the Central Nervous System

    doi: 10.3390/ijms23073617

    Figure Lengend Snippet: TRPV2 expression in spinal cord samples from WT and EAE mice. ( A ) Immunohistochemical staining of TRPV2 in spinal cord of control and EAE-induced mice in the onset, peak and in the chronic phase, during remission. In control conditions, TRPV2 is expressed in neurons in GM (inset, arrows), and in oligodendrocytes in WM (inset, arrowheads). After EAE induction, an increase in TRPV2 expression is mainly located in inflammatory focuses at the peak clinical symptomatology in WM (empty arrowheads). ( B ) MSRA and TRPV2 protein expression in thoracic spinal cord samples from CFA and MOG mice (9, 14, 21 and 28 days post-immunization). ( B ) A significant increase in TRPV2 protein levels (#, p = 0.0014) is determined in MOG14 mice when compared with CFA ( p

    Article Snippet: After washes with 0.1 M TBS, sections were incubated for 1 h with BB, and then, overnight with rabbit anti-TRPV2 (1:100, Alomone) diluted in BB at 4 °C and 1 h at RT ( ).

    Techniques: Expressing, Mouse Assay, Immunohistochemistry, Staining

    TRPV2-centered cellular cross-talk model in physiological and pathophysiological myelination. During embryonic development, TRPV2 develops an essential role in neurite and axon outgrowth. In that period, TRPV2 is known to be expressed and activated in neurons, and putatively in OPCs, where possible cross-talk between both cells might be triggered through TRPV2 activation. In adulthood, TRPV2 expression is found in microglia, neurons and oligodendrocytes. Upon an insult such as demyelination, TRPV2, as a non-selective ion channel, is activated. Some known triggering stimuli are NO, LPC or oxidative stress, the latter causing methionine oxidation which facilitates TRPV2 sensitization. TRPV2 activation promotes a sodium/calcium inward influx from extracellular media and/or ER or endosomes. Consequently, cells are depolarized, which initiate processes such as actin polymerization or phagocytosis in microglia or innate immune cells. In those cells, TRPV2 has been involved in migration, phagocytosis or cytokine production. TRPV2 inactivation is promoted by MSRA enzyme, by reducing oxidized methionine. In our results, we observed both an increase of TRPV2 and MSRA in demyelinating scenarios. During remyelination, OPCs proliferate and migrate to the demyelinated area, where they differentiate through several stages to mature oligodendrocytes, and start myelination. Our results showed increased TRPV2 expression during this period. Overall, ubiquitous TRPV2 expression and activation in de- and remyelinating processes suggest a multicellular cross-talk that promotes myelin repair at all levels. TRPV2 is relevant in development and demyelination, making this model suitable for the recapitulation hypotheses. Created with BioRender.com (accessed on 10 January 2022) [ 8 , 9 , 10 ].

    Journal: International Journal of Molecular Sciences

    Article Title: TRPV2: A Key Player in Myelination Disorders of the Central Nervous System

    doi: 10.3390/ijms23073617

    Figure Lengend Snippet: TRPV2-centered cellular cross-talk model in physiological and pathophysiological myelination. During embryonic development, TRPV2 develops an essential role in neurite and axon outgrowth. In that period, TRPV2 is known to be expressed and activated in neurons, and putatively in OPCs, where possible cross-talk between both cells might be triggered through TRPV2 activation. In adulthood, TRPV2 expression is found in microglia, neurons and oligodendrocytes. Upon an insult such as demyelination, TRPV2, as a non-selective ion channel, is activated. Some known triggering stimuli are NO, LPC or oxidative stress, the latter causing methionine oxidation which facilitates TRPV2 sensitization. TRPV2 activation promotes a sodium/calcium inward influx from extracellular media and/or ER or endosomes. Consequently, cells are depolarized, which initiate processes such as actin polymerization or phagocytosis in microglia or innate immune cells. In those cells, TRPV2 has been involved in migration, phagocytosis or cytokine production. TRPV2 inactivation is promoted by MSRA enzyme, by reducing oxidized methionine. In our results, we observed both an increase of TRPV2 and MSRA in demyelinating scenarios. During remyelination, OPCs proliferate and migrate to the demyelinated area, where they differentiate through several stages to mature oligodendrocytes, and start myelination. Our results showed increased TRPV2 expression during this period. Overall, ubiquitous TRPV2 expression and activation in de- and remyelinating processes suggest a multicellular cross-talk that promotes myelin repair at all levels. TRPV2 is relevant in development and demyelination, making this model suitable for the recapitulation hypotheses. Created with BioRender.com (accessed on 10 January 2022) [ 8 , 9 , 10 ].

    Article Snippet: After washes with 0.1 M TBS, sections were incubated for 1 h with BB, and then, overnight with rabbit anti-TRPV2 (1:100, Alomone) diluted in BB at 4 °C and 1 h at RT ( ).

    Techniques: Activation Assay, Expressing, Migration

    TRPV2 expression in mixed glia cultures of mice after pro-inflammatory (LPS), anti-inflammatory (IL-4) and demyelinating (LPC) treatments. ( A – I ) Double immunohistochemical staining allowed for the determination of whether TRPV2 was expressed in microglia ( A – C ), astrocytes ( D – F ) or oligodendrocyte cells ( G – I ). TRPV2 was highly expressed in the cell body of some microglia (full arrowheads) but not all of them (empty arrowheads) in control conditions, and TRPV2 was spread afterwards through the cell body of activated microglia cells, with an expression pattern highly coincident with CD68+ lysosomes (arrows). While no expression of TRPV2 was found in astrocytes (empty arrowheads), OPCs showed either low or absent expression in control conditions (full and empty arrowheads, respectively) and increased expression throughout the cell body (arrows) and the principal soma (arrowheads) after both pro-inflammatory and anti-inflammatory treatments. ( J , K ) Quantification of TRPV2 protein (ng/mL) by ELISA in secondary mixed glial cultures in control conditions, and after LPS and IL-4 treatments ( J ) and in quaternary mixed glial cultures, containing myelin-binding protein (MBP)+ oligodendrocytes, in demyelinating conditions ( K ). Determination of TRPV2 showed a significant decrease in TRPV2 after LPS and LPC treatments ( J , K ), and an increase after IL-4 treatment ( p = 0.05) compared to control conditions ( J ). ( L , M ) Quantification of NO secondary mixed glial cultures in control conditions, and after LPS and IL-4 treatments ( L ) and in quaternary mixed glial cultures in demyelinating conditions ( M ). An increase in NO concentration was observed in cell cultures after LPS treatment compared to control conditions, while a significant decrease was observed after IL-4 treatment. After LPC treatment, NO remained stable compared to the control. Statistical analysis was performed by one-way ANOVA followed by Dunnett’s multiple comparison compared to the control in the LPS and IL-4 treated cultures (* p

    Journal: International Journal of Molecular Sciences

    Article Title: TRPV2: A Key Player in Myelination Disorders of the Central Nervous System

    doi: 10.3390/ijms23073617

    Figure Lengend Snippet: TRPV2 expression in mixed glia cultures of mice after pro-inflammatory (LPS), anti-inflammatory (IL-4) and demyelinating (LPC) treatments. ( A – I ) Double immunohistochemical staining allowed for the determination of whether TRPV2 was expressed in microglia ( A – C ), astrocytes ( D – F ) or oligodendrocyte cells ( G – I ). TRPV2 was highly expressed in the cell body of some microglia (full arrowheads) but not all of them (empty arrowheads) in control conditions, and TRPV2 was spread afterwards through the cell body of activated microglia cells, with an expression pattern highly coincident with CD68+ lysosomes (arrows). While no expression of TRPV2 was found in astrocytes (empty arrowheads), OPCs showed either low or absent expression in control conditions (full and empty arrowheads, respectively) and increased expression throughout the cell body (arrows) and the principal soma (arrowheads) after both pro-inflammatory and anti-inflammatory treatments. ( J , K ) Quantification of TRPV2 protein (ng/mL) by ELISA in secondary mixed glial cultures in control conditions, and after LPS and IL-4 treatments ( J ) and in quaternary mixed glial cultures, containing myelin-binding protein (MBP)+ oligodendrocytes, in demyelinating conditions ( K ). Determination of TRPV2 showed a significant decrease in TRPV2 after LPS and LPC treatments ( J , K ), and an increase after IL-4 treatment ( p = 0.05) compared to control conditions ( J ). ( L , M ) Quantification of NO secondary mixed glial cultures in control conditions, and after LPS and IL-4 treatments ( L ) and in quaternary mixed glial cultures in demyelinating conditions ( M ). An increase in NO concentration was observed in cell cultures after LPS treatment compared to control conditions, while a significant decrease was observed after IL-4 treatment. After LPC treatment, NO remained stable compared to the control. Statistical analysis was performed by one-way ANOVA followed by Dunnett’s multiple comparison compared to the control in the LPS and IL-4 treated cultures (* p

    Article Snippet: After washes with 0.1 M TBS, sections were incubated for 1 h with BB, and then, overnight with rabbit anti-TRPV2 (1:100, Alomone) diluted in BB at 4 °C and 1 h at RT ( ).

    Techniques: Expressing, Mouse Assay, Immunohistochemistry, Staining, Enzyme-linked Immunosorbent Assay, Binding Assay, Concentration Assay

    TRPV2, Opalin and MSRA expression in spinal cord of wild-type (WT) and hypomyelination jimpy mice. Immunohistochemical staining against MBP ( A , B ), TRPV2 ( D , E ), Opalin ( G , H ) and MSRA ( J , K ) were performed in spinal cord sections of 21-day-old WT and jimpy mice, and immunoreactivity was quantified and analyzed as Area x Intensity. Results show that MBP was importantly reduced in both GM ( a , b ) and WM ( a’ , b’ ) of jimpy mice compared to WT ( A – C ). TRPV2 expression was mainly located in neurons in GM ( d’ ) and glial cells, putatively oligodendrocytes, and in WM ( d ) of WT. A significant decrease in TRPV2 expression in the spinal cord of jimpy mice was observed compared to WT ( E , F , e , e’ ). Opalin expression was importantly found in WM of WT mice ( G , g ), and to a lesser extent also in GM ( g’ ), but showed a marked decrease in WM and GM of jimpy mice ( H – I , h , h’ ). MSRA was the only molecule that did not suffer an important reduction of its expression in both WM ( j , k ) and GM ( j’ , k’ ) in jimpy mice ( L ). Results were expressed as mean ± SEM. Statistical analysis of the results were performed with an unpaired Student’s t -test (** p

    Journal: International Journal of Molecular Sciences

    Article Title: TRPV2: A Key Player in Myelination Disorders of the Central Nervous System

    doi: 10.3390/ijms23073617

    Figure Lengend Snippet: TRPV2, Opalin and MSRA expression in spinal cord of wild-type (WT) and hypomyelination jimpy mice. Immunohistochemical staining against MBP ( A , B ), TRPV2 ( D , E ), Opalin ( G , H ) and MSRA ( J , K ) were performed in spinal cord sections of 21-day-old WT and jimpy mice, and immunoreactivity was quantified and analyzed as Area x Intensity. Results show that MBP was importantly reduced in both GM ( a , b ) and WM ( a’ , b’ ) of jimpy mice compared to WT ( A – C ). TRPV2 expression was mainly located in neurons in GM ( d’ ) and glial cells, putatively oligodendrocytes, and in WM ( d ) of WT. A significant decrease in TRPV2 expression in the spinal cord of jimpy mice was observed compared to WT ( E , F , e , e’ ). Opalin expression was importantly found in WM of WT mice ( G , g ), and to a lesser extent also in GM ( g’ ), but showed a marked decrease in WM and GM of jimpy mice ( H – I , h , h’ ). MSRA was the only molecule that did not suffer an important reduction of its expression in both WM ( j , k ) and GM ( j’ , k’ ) in jimpy mice ( L ). Results were expressed as mean ± SEM. Statistical analysis of the results were performed with an unpaired Student’s t -test (** p

    Article Snippet: After washes with 0.1 M TBS, sections were incubated for 1 h with BB, and then, overnight with rabbit anti-TRPV2 (1:100, Alomone) diluted in BB at 4 °C and 1 h at RT ( ).

    Techniques: Expressing, Mouse Assay, Immunohistochemistry, Staining

    TRPV2 and MSRA expression in WM of cuprizone-induced demyelination and remyelination in mice. ( A – I ) Representative images of immunohistochemical staining directed against MBP, TRPV2 and MSRA in the CC of control mice ( A , D , G ) and cuprizone-intoxicated mice after demyelination ( B , E , H , 5 weeks of treatment) and during remyelination ( C , F , I , 5 weeks of treatment + 1 week of normal diet). ( A – C ) MBP immunostaining shows the myelinated CC of WT mice in basal conditions ( A ). At 5 weeks of cuprizone treatment, the CC is largely demyelinated ( B ) with a myelination-resistant area (*), and after one week of normal diet, the CC is mostly remyelinated ( C ). Control mice show undetectable levels of TRPV2 and MSRA in the CC ( D and G ). After demyelination, variably low and high levels of TRPV2 were observed in cell bodies (empty arrowheads and arrowheads, respectively in E , F ). High levels of TRPV2 were clearly observed at remyelination (inset in F ). During remyelination, most TRPV2+ cells co-expressed APC (full arrowheads in L ), a marker for mature oligodendrocytes. In the CC area resistant to demyelination (* in E , F ), TRPV2+ cells showed high levels of expression in both conditions. An increase in MSRA levels of expression were also observed in cell bodies after demyelination and remyelination (arrowheads in H and I ). In demyelination, most cells expressed low levels of MSRA in the CC (inset in H ), while during remyelination, a lower number of MSRA+ cells expressing higher levels of MSRA were observed (inset in I ). ( J – K ) Quantification of TRPV2 and MSRA expression after cuprizone treatment. ( J ) Quantitative analysis of TRPV2 immunoreactivity in the CC confirmed the progressive increase of TRPV2 expression in demyelinating and remyelinating conditions compared to control mice, which was statistically significant in the latter. ( K ) Quantitative analysis of MSRA immunoreactivity in the CC showed that the increase of MSRA expression during demyelination was statistically significant when compared to control mice. Data are shown as ± SEM. Statistical analysis was performed by one-way ANOVA followed by Tukey’s multiple comparison test (** p

    Journal: International Journal of Molecular Sciences

    Article Title: TRPV2: A Key Player in Myelination Disorders of the Central Nervous System

    doi: 10.3390/ijms23073617

    Figure Lengend Snippet: TRPV2 and MSRA expression in WM of cuprizone-induced demyelination and remyelination in mice. ( A – I ) Representative images of immunohistochemical staining directed against MBP, TRPV2 and MSRA in the CC of control mice ( A , D , G ) and cuprizone-intoxicated mice after demyelination ( B , E , H , 5 weeks of treatment) and during remyelination ( C , F , I , 5 weeks of treatment + 1 week of normal diet). ( A – C ) MBP immunostaining shows the myelinated CC of WT mice in basal conditions ( A ). At 5 weeks of cuprizone treatment, the CC is largely demyelinated ( B ) with a myelination-resistant area (*), and after one week of normal diet, the CC is mostly remyelinated ( C ). Control mice show undetectable levels of TRPV2 and MSRA in the CC ( D and G ). After demyelination, variably low and high levels of TRPV2 were observed in cell bodies (empty arrowheads and arrowheads, respectively in E , F ). High levels of TRPV2 were clearly observed at remyelination (inset in F ). During remyelination, most TRPV2+ cells co-expressed APC (full arrowheads in L ), a marker for mature oligodendrocytes. In the CC area resistant to demyelination (* in E , F ), TRPV2+ cells showed high levels of expression in both conditions. An increase in MSRA levels of expression were also observed in cell bodies after demyelination and remyelination (arrowheads in H and I ). In demyelination, most cells expressed low levels of MSRA in the CC (inset in H ), while during remyelination, a lower number of MSRA+ cells expressing higher levels of MSRA were observed (inset in I ). ( J – K ) Quantification of TRPV2 and MSRA expression after cuprizone treatment. ( J ) Quantitative analysis of TRPV2 immunoreactivity in the CC confirmed the progressive increase of TRPV2 expression in demyelinating and remyelinating conditions compared to control mice, which was statistically significant in the latter. ( K ) Quantitative analysis of MSRA immunoreactivity in the CC showed that the increase of MSRA expression during demyelination was statistically significant when compared to control mice. Data are shown as ± SEM. Statistical analysis was performed by one-way ANOVA followed by Tukey’s multiple comparison test (** p

    Article Snippet: After washes with 0.1 M TBS, sections were incubated for 1 h with BB, and then, overnight with rabbit anti-TRPV2 (1:100, Alomone) diluted in BB at 4 °C and 1 h at RT ( ).

    Techniques: Expressing, Mouse Assay, Immunohistochemistry, Staining, Immunostaining, Marker

    MSRA and TRPV2 expression in frontal cortex samples from healthy subjects ( n = 4) and MS ( n = 6) patients. ( A ) TRPV2 mRNA ( p = 0.3314) is not changed between MS and healthy samples. ( B ) A significant upregulation in MSRA mRNA ( p = 0.0014) is found in MS; ( C ) A significant decrease in TRPV2 protein levels ( p = 0.0232) and a significant increase in MSRA protein levels ( p = 0.0124) were determined in MS samples by western blot. Bars show mean ± SEM; * p

    Journal: International Journal of Molecular Sciences

    Article Title: TRPV2: A Key Player in Myelination Disorders of the Central Nervous System

    doi: 10.3390/ijms23073617

    Figure Lengend Snippet: MSRA and TRPV2 expression in frontal cortex samples from healthy subjects ( n = 4) and MS ( n = 6) patients. ( A ) TRPV2 mRNA ( p = 0.3314) is not changed between MS and healthy samples. ( B ) A significant upregulation in MSRA mRNA ( p = 0.0014) is found in MS; ( C ) A significant decrease in TRPV2 protein levels ( p = 0.0232) and a significant increase in MSRA protein levels ( p = 0.0124) were determined in MS samples by western blot. Bars show mean ± SEM; * p

    Article Snippet: After washes with 0.1 M TBS, sections were incubated for 1 h with BB, and then, overnight with rabbit anti-TRPV2 (1:100, Alomone) diluted in BB at 4 °C and 1 h at RT ( ).

    Techniques: Expressing, Western Blot

    TRPV2 interaction with Opalin, NTM and PLP1 in vitro during basal and inflammatory conditions. ( A ) Rat TRPV2 FL protein and rat ARD of TRPV2 were immobilized on membranes and incubated with increasing concentrations of rat protein brain lysates (0–10 µg). Opalin, NTM and PLP1 were detected by immunoblot. ( B ) Immunocytochemistry in mouse mixed glial primary cultures shows TRPV2 (green), Opalin (red) and DAPI (blue). TRPV2-Opalin colocalization is shown as yellow signal (merge) and both proteins are co-expressed in some cells (arrowheads). Expression of these proteins is mainly found in the membrane. ( C ) TRPV2–Opalin colocalization expressed as Pearson’s coefficient in basal and inflammatory conditions. Both proteins show a high degree of colocalization. ( D ) TRPV2 colocalization with Opalin, expressed as Mander’s coefficient M2 (fraction of TRPV2 signal overlapping Opalin) in basal and inflammatory conditions. Both proteins show a high degree of colocalization. Results were expressed as mean ± SEM. Statistical analysis of the results were performed with an unpaired Student’s t -test ( p

    Journal: International Journal of Molecular Sciences

    Article Title: TRPV2: A Key Player in Myelination Disorders of the Central Nervous System

    doi: 10.3390/ijms23073617

    Figure Lengend Snippet: TRPV2 interaction with Opalin, NTM and PLP1 in vitro during basal and inflammatory conditions. ( A ) Rat TRPV2 FL protein and rat ARD of TRPV2 were immobilized on membranes and incubated with increasing concentrations of rat protein brain lysates (0–10 µg). Opalin, NTM and PLP1 were detected by immunoblot. ( B ) Immunocytochemistry in mouse mixed glial primary cultures shows TRPV2 (green), Opalin (red) and DAPI (blue). TRPV2-Opalin colocalization is shown as yellow signal (merge) and both proteins are co-expressed in some cells (arrowheads). Expression of these proteins is mainly found in the membrane. ( C ) TRPV2–Opalin colocalization expressed as Pearson’s coefficient in basal and inflammatory conditions. Both proteins show a high degree of colocalization. ( D ) TRPV2 colocalization with Opalin, expressed as Mander’s coefficient M2 (fraction of TRPV2 signal overlapping Opalin) in basal and inflammatory conditions. Both proteins show a high degree of colocalization. Results were expressed as mean ± SEM. Statistical analysis of the results were performed with an unpaired Student’s t -test ( p

    Article Snippet: After washes with 0.1 M TBS, sections were incubated for 1 h with BB, and then, overnight with rabbit anti-TRPV2 (1:100, Alomone) diluted in BB at 4 °C and 1 h at RT ( ).

    Techniques: In Vitro, Incubation, Immunocytochemistry, Expressing