intracellular trpv4  (Alomone Labs)


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    Alomone Labs intracellular trpv4
    p38 activation and macrophage phagocytosis in response to LPS is dependent on matrix stiffness. Phosphorylated and total A. p38 and B. JNK on various matrix stiffnesses in the physiologic range (1kPa, 8kPa, and 25kPa) from WT vs <t>TRPV4</t> KO BMDMs quantified for LPS 15 minutes ( *p = 0.031). C. Macrophage phagocytosis of E. coli particles ± p38 inhibition (SB, BIRB) on various matrix stiffnesses ( *p
    Intracellular Trpv4, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/intracellular trpv4/product/Alomone Labs
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    intracellular trpv4 - by Bioz Stars, 2022-05
    92/100 stars

    Images

    1) Product Images from "TRPV4 Protects the Lung from Bacterial Pneumonia via MAPK Molecular Pathway Switching"

    Article Title: TRPV4 Protects the Lung from Bacterial Pneumonia via MAPK Molecular Pathway Switching

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

    doi: 10.4049/jimmunol.1901033

    p38 activation and macrophage phagocytosis in response to LPS is dependent on matrix stiffness. Phosphorylated and total A. p38 and B. JNK on various matrix stiffnesses in the physiologic range (1kPa, 8kPa, and 25kPa) from WT vs TRPV4 KO BMDMs quantified for LPS 15 minutes ( *p = 0.031). C. Macrophage phagocytosis of E. coli particles ± p38 inhibition (SB, BIRB) on various matrix stiffnesses ( *p
    Figure Legend Snippet: p38 activation and macrophage phagocytosis in response to LPS is dependent on matrix stiffness. Phosphorylated and total A. p38 and B. JNK on various matrix stiffnesses in the physiologic range (1kPa, 8kPa, and 25kPa) from WT vs TRPV4 KO BMDMs quantified for LPS 15 minutes ( *p = 0.031). C. Macrophage phagocytosis of E. coli particles ± p38 inhibition (SB, BIRB) on various matrix stiffnesses ( *p

    Techniques Used: Activation Assay, Inhibition

    TRPV4-mediated p38 MAPK and JNK molecular switch is regulated by dual-specificity phosphatase 1 (DUSP1). WT and TRPV4 KO BMDMs were incubated ± LPS as above for indicated time, and cells were lysed and analyzed by A. immunoblot for DUSP1 and B. band density quantified as DUSP1/GAPDH from immunoblot (n = 4) ( *p
    Figure Legend Snippet: TRPV4-mediated p38 MAPK and JNK molecular switch is regulated by dual-specificity phosphatase 1 (DUSP1). WT and TRPV4 KO BMDMs were incubated ± LPS as above for indicated time, and cells were lysed and analyzed by A. immunoblot for DUSP1 and B. band density quantified as DUSP1/GAPDH from immunoblot (n = 4) ( *p

    Techniques Used: Incubation

    TRPV4 function protects against lung injury in a murine Pseudomonas aeruginosa pneumonia model. Sterile beads or P. aeruginosa (PA, PAM57–15) were instilled intratracheally in TRPV4 KO and age-matched female congenic WT mice with BAL and tissue harvest performed at Day 3 (injury phase). TRPV4 deleted mice (TRPV4 KO) have greater A. inflammatory cell infiltration and B. BAL total protein compared to WT (* p
    Figure Legend Snippet: TRPV4 function protects against lung injury in a murine Pseudomonas aeruginosa pneumonia model. Sterile beads or P. aeruginosa (PA, PAM57–15) were instilled intratracheally in TRPV4 KO and age-matched female congenic WT mice with BAL and tissue harvest performed at Day 3 (injury phase). TRPV4 deleted mice (TRPV4 KO) have greater A. inflammatory cell infiltration and B. BAL total protein compared to WT (* p

    Techniques Used: Mouse Assay

    p38 MAPK and JNK are differentially regulated by TRPV4 after LPS or Pseudomonas aeruginosa . BMDMs were incubated ± LPS as above for indicated time cultured on tissue culture-treated plastic, and cells were lysed and analyzed by immunoblot for A. phosphorylated and total p38, ERK, and JNK compared to WT BMDMs (whole cell lysate). Band density quantified from immunoblot (n = 3–6) for B. p-p38/total p38 ( *p
    Figure Legend Snippet: p38 MAPK and JNK are differentially regulated by TRPV4 after LPS or Pseudomonas aeruginosa . BMDMs were incubated ± LPS as above for indicated time cultured on tissue culture-treated plastic, and cells were lysed and analyzed by immunoblot for A. phosphorylated and total p38, ERK, and JNK compared to WT BMDMs (whole cell lysate). Band density quantified from immunoblot (n = 3–6) for B. p-p38/total p38 ( *p

    Techniques Used: Incubation, Cell Culture

    TRPV4 mediates phagocytosis after LPS in healthy human through p38 MAPK. Monocyte derived and alveolar macrophages from healthy (n = 6) control subjects were incubated ± LPS ± TRPV4 inhibitor, HC, and phagocytosis of E. coli particles was measured in A. monocyte-derived and B. alveolar macrophages in healthy controls. HC alone had no effect. Representative immunoblot for phosphorylated and total p38 in C. healthy monocyte derived macrophages ± LPS 15 minutes and D. band density quantified ( *p
    Figure Legend Snippet: TRPV4 mediates phagocytosis after LPS in healthy human through p38 MAPK. Monocyte derived and alveolar macrophages from healthy (n = 6) control subjects were incubated ± LPS ± TRPV4 inhibitor, HC, and phagocytosis of E. coli particles was measured in A. monocyte-derived and B. alveolar macrophages in healthy controls. HC alone had no effect. Representative immunoblot for phosphorylated and total p38 in C. healthy monocyte derived macrophages ± LPS 15 minutes and D. band density quantified ( *p

    Techniques Used: Derivative Assay, Incubation

    TRPV4 mediates clearance of P. aeruginosa by macrophages. WT and TRPV4 KO mice were intratracheally administered ±GFP P. aeruginosa for 3 days. Representative confocal images of whole lung lavage cytospins of macrophages (open arrowhead) and neutrophils (filled arrowhead) in WT mice given IT sterile beads or GFP- P. aeruginosa after immunofluorescence with A. TRPV4 extracellular antibody (green, TRPV4) and C. anti-GFP (green, GFP P. aeruginosa ; anti-CD45, red; dapi, blue). B, D. Quantification of A, C . * , # p
    Figure Legend Snippet: TRPV4 mediates clearance of P. aeruginosa by macrophages. WT and TRPV4 KO mice were intratracheally administered ±GFP P. aeruginosa for 3 days. Representative confocal images of whole lung lavage cytospins of macrophages (open arrowhead) and neutrophils (filled arrowhead) in WT mice given IT sterile beads or GFP- P. aeruginosa after immunofluorescence with A. TRPV4 extracellular antibody (green, TRPV4) and C. anti-GFP (green, GFP P. aeruginosa ; anti-CD45, red; dapi, blue). B, D. Quantification of A, C . * , # p

    Techniques Used: Mouse Assay, Immunofluorescence

    TRPV4 modulates pro-inflammatory cytokine production through JNK. BMDMs were incubated ± LPS (100ng/mL, 24h) ± JNK inhibitor, SP600125 (20μM, 25h) ± p38 inhibitor, SB203580 (10μM, 25h), cultured on cell culture-treated plastic, and cytokines measured via ELISA. IL-6, CXCL2, and CXCL1 secretion ± LPS in A. WT and TRPV4 KO BMDMs and B. WT BMDMs ± SP600125 ± SB203580 ( *, # p
    Figure Legend Snippet: TRPV4 modulates pro-inflammatory cytokine production through JNK. BMDMs were incubated ± LPS (100ng/mL, 24h) ± JNK inhibitor, SP600125 (20μM, 25h) ± p38 inhibitor, SB203580 (10μM, 25h), cultured on cell culture-treated plastic, and cytokines measured via ELISA. IL-6, CXCL2, and CXCL1 secretion ± LPS in A. WT and TRPV4 KO BMDMs and B. WT BMDMs ± SP600125 ± SB203580 ( *, # p

    Techniques Used: Incubation, Cell Culture, Enzyme-linked Immunosorbent Assay

    2) Product Images from "TRPV4 Protects the Lung from Bacterial Pneumonia via MAPK Molecular Pathway Switching"

    Article Title: TRPV4 Protects the Lung from Bacterial Pneumonia via MAPK Molecular Pathway Switching

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

    doi: 10.4049/jimmunol.1901033

    p38 activation and macrophage phagocytosis in response to LPS is dependent on matrix stiffness. Phosphorylated and total A. p38 and B. JNK on various matrix stiffnesses in the physiologic range (1kPa, 8kPa, and 25kPa) from WT vs TRPV4 KO BMDMs quantified for LPS 15 minutes ( *p = 0.031). C. Macrophage phagocytosis of E. coli particles ± p38 inhibition (SB, BIRB) on various matrix stiffnesses ( *p
    Figure Legend Snippet: p38 activation and macrophage phagocytosis in response to LPS is dependent on matrix stiffness. Phosphorylated and total A. p38 and B. JNK on various matrix stiffnesses in the physiologic range (1kPa, 8kPa, and 25kPa) from WT vs TRPV4 KO BMDMs quantified for LPS 15 minutes ( *p = 0.031). C. Macrophage phagocytosis of E. coli particles ± p38 inhibition (SB, BIRB) on various matrix stiffnesses ( *p

    Techniques Used: Activation Assay, Inhibition

    TRPV4-mediated p38 MAPK and JNK molecular switch is regulated by dual-specificity phosphatase 1 (DUSP1). WT and TRPV4 KO BMDMs were incubated ± LPS as above for indicated time, and cells were lysed and analyzed by A. immunoblot for DUSP1 and B. band density quantified as DUSP1/GAPDH from immunoblot (n = 4) ( *p
    Figure Legend Snippet: TRPV4-mediated p38 MAPK and JNK molecular switch is regulated by dual-specificity phosphatase 1 (DUSP1). WT and TRPV4 KO BMDMs were incubated ± LPS as above for indicated time, and cells were lysed and analyzed by A. immunoblot for DUSP1 and B. band density quantified as DUSP1/GAPDH from immunoblot (n = 4) ( *p

    Techniques Used: Incubation

    TRPV4 function protects against lung injury in a murine Pseudomonas aeruginosa pneumonia model. Sterile beads or P. aeruginosa (PA, PAM57–15) were instilled intratracheally in TRPV4 KO and age-matched female congenic WT mice with BAL and tissue harvest performed at Day 3 (injury phase). TRPV4 deleted mice (TRPV4 KO) have greater A. inflammatory cell infiltration and B. BAL total protein compared to WT (* p
    Figure Legend Snippet: TRPV4 function protects against lung injury in a murine Pseudomonas aeruginosa pneumonia model. Sterile beads or P. aeruginosa (PA, PAM57–15) were instilled intratracheally in TRPV4 KO and age-matched female congenic WT mice with BAL and tissue harvest performed at Day 3 (injury phase). TRPV4 deleted mice (TRPV4 KO) have greater A. inflammatory cell infiltration and B. BAL total protein compared to WT (* p

    Techniques Used: Mouse Assay

    p38 MAPK and JNK are differentially regulated by TRPV4 after LPS or Pseudomonas aeruginosa . BMDMs were incubated ± LPS as above for indicated time cultured on tissue culture-treated plastic, and cells were lysed and analyzed by immunoblot for A. phosphorylated and total p38, ERK, and JNK compared to WT BMDMs (whole cell lysate). Band density quantified from immunoblot (n = 3–6) for B. p-p38/total p38 ( *p
    Figure Legend Snippet: p38 MAPK and JNK are differentially regulated by TRPV4 after LPS or Pseudomonas aeruginosa . BMDMs were incubated ± LPS as above for indicated time cultured on tissue culture-treated plastic, and cells were lysed and analyzed by immunoblot for A. phosphorylated and total p38, ERK, and JNK compared to WT BMDMs (whole cell lysate). Band density quantified from immunoblot (n = 3–6) for B. p-p38/total p38 ( *p

    Techniques Used: Incubation, Cell Culture

    TRPV4 mediates phagocytosis after LPS in healthy human through p38 MAPK. Monocyte derived and alveolar macrophages from healthy (n = 6) control subjects were incubated ± LPS ± TRPV4 inhibitor, HC, and phagocytosis of E. coli particles was measured in A. monocyte-derived and B. alveolar macrophages in healthy controls. HC alone had no effect. Representative immunoblot for phosphorylated and total p38 in C. healthy monocyte derived macrophages ± LPS 15 minutes and D. band density quantified ( *p
    Figure Legend Snippet: TRPV4 mediates phagocytosis after LPS in healthy human through p38 MAPK. Monocyte derived and alveolar macrophages from healthy (n = 6) control subjects were incubated ± LPS ± TRPV4 inhibitor, HC, and phagocytosis of E. coli particles was measured in A. monocyte-derived and B. alveolar macrophages in healthy controls. HC alone had no effect. Representative immunoblot for phosphorylated and total p38 in C. healthy monocyte derived macrophages ± LPS 15 minutes and D. band density quantified ( *p

    Techniques Used: Derivative Assay, Incubation

    TRPV4 mediates clearance of P. aeruginosa by macrophages. WT and TRPV4 KO mice were intratracheally administered ±GFP P. aeruginosa for 3 days. Representative confocal images of whole lung lavage cytospins of macrophages (open arrowhead) and neutrophils (filled arrowhead) in WT mice given IT sterile beads or GFP- P. aeruginosa after immunofluorescence with A. TRPV4 extracellular antibody (green, TRPV4) and C. anti-GFP (green, GFP P. aeruginosa ; anti-CD45, red; dapi, blue). B, D. Quantification of A, C . * , # p
    Figure Legend Snippet: TRPV4 mediates clearance of P. aeruginosa by macrophages. WT and TRPV4 KO mice were intratracheally administered ±GFP P. aeruginosa for 3 days. Representative confocal images of whole lung lavage cytospins of macrophages (open arrowhead) and neutrophils (filled arrowhead) in WT mice given IT sterile beads or GFP- P. aeruginosa after immunofluorescence with A. TRPV4 extracellular antibody (green, TRPV4) and C. anti-GFP (green, GFP P. aeruginosa ; anti-CD45, red; dapi, blue). B, D. Quantification of A, C . * , # p

    Techniques Used: Mouse Assay, Immunofluorescence

    TRPV4 modulates pro-inflammatory cytokine production through JNK. BMDMs were incubated ± LPS (100ng/mL, 24h) ± JNK inhibitor, SP600125 (20μM, 25h) ± p38 inhibitor, SB203580 (10μM, 25h), cultured on cell culture-treated plastic, and cytokines measured via ELISA. IL-6, CXCL2, and CXCL1 secretion ± LPS in A. WT and TRPV4 KO BMDMs and B. WT BMDMs ± SP600125 ± SB203580 ( *, # p
    Figure Legend Snippet: TRPV4 modulates pro-inflammatory cytokine production through JNK. BMDMs were incubated ± LPS (100ng/mL, 24h) ± JNK inhibitor, SP600125 (20μM, 25h) ± p38 inhibitor, SB203580 (10μM, 25h), cultured on cell culture-treated plastic, and cytokines measured via ELISA. IL-6, CXCL2, and CXCL1 secretion ± LPS in A. WT and TRPV4 KO BMDMs and B. WT BMDMs ± SP600125 ± SB203580 ( *, # p

    Techniques Used: Incubation, Cell Culture, Enzyme-linked Immunosorbent Assay

    3) Product Images from "TRPV4 Mechanosensitive Ion Channel Regulates LPS-Stimulated Macrophage Phagocytosis"

    Article Title: TRPV4 Mechanosensitive Ion Channel Regulates LPS-Stimulated Macrophage Phagocytosis

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

    doi: 10.4049/jimmunol.1501688

    TRPV4 modulates the cytokine response to LPS in a manner that depends on matrix stiffness
    Figure Legend Snippet: TRPV4 modulates the cytokine response to LPS in a manner that depends on matrix stiffness

    Techniques Used:

    Working model illustrating that LPS and TRPV4 signal cooperate to alter macrophage phenotypic change leading to enhanced clearance of infection and resolution of lung injury
    Figure Legend Snippet: Working model illustrating that LPS and TRPV4 signal cooperate to alter macrophage phenotypic change leading to enhanced clearance of infection and resolution of lung injury

    Techniques Used: Infection

    TRPV4 mediates LPS-stimulated macrophage phagocytosis of E. coli particles
    Figure Legend Snippet: TRPV4 mediates LPS-stimulated macrophage phagocytosis of E. coli particles

    Techniques Used:

    TRPV4 mediates LPS-stimulated macrophage phagocytosis of IgG-coated latex beads in vitro
    Figure Legend Snippet: TRPV4 mediates LPS-stimulated macrophage phagocytosis of IgG-coated latex beads in vitro

    Techniques Used: In Vitro

    TRPV4 mediates the stiffness induction effect on LPS-stimulated calcium influx and macrophage phagocytosis
    Figure Legend Snippet: TRPV4 mediates the stiffness induction effect on LPS-stimulated calcium influx and macrophage phagocytosis

    Techniques Used:

    TRPV4 mediates LPS-stimulated macrophage phagocytosis of IgG-coated latex beads in vivo
    Figure Legend Snippet: TRPV4 mediates LPS-stimulated macrophage phagocytosis of IgG-coated latex beads in vivo

    Techniques Used: In Vivo

    Functional TRPV4 is expressed in murine BMDMs
    Figure Legend Snippet: Functional TRPV4 is expressed in murine BMDMs

    Techniques Used: Functional Assay

    4) Product Images from "Rhythmic Calcium Events in the Lamina Propria Network of the Urinary Bladder of Rat Pups"

    Article Title: Rhythmic Calcium Events in the Lamina Propria Network of the Urinary Bladder of Rat Pups

    Journal: Frontiers in Systems Neuroscience

    doi: 10.3389/fnsys.2017.00087

    Whole mounts of urinary bladder tissue were prepared at the urothelial-lamina junction and contained a dense network of capillaries, small blood vessels and cells from rat pups aged ≤ P21. Capillaries, blood vessels and cells were loaded with the fluorescent dye (Fluo-2, green) (A , B,E) . Tetramethylrhodamine (TRITC; red) was picked up by urothelial cells and provided contrast to Fluo-2 loaded cells (A , B) . The cellular network in the lamina propria was heterogeneous with numerous small round, stellate or spindle shaped cells (10–20 μm) with multiple processes projecting from the soma in rat pups aged P ≤ 21. Numerous cells in the lamina propria exhibited PDGFRα-immunoreactivity (IR) whereas fewer cells exhibited TRPV4-IR (C,D) . At the urothelial-lamina propria junction, a dense capillary network was in close proximity to the network of cells expressing PDGFRα- and TRPV4-IR (E) . Capillaries were isolated using their signature, long tubular shape in the PTCL analysis software and recolored red to distinguish them from lamina propria cells. 3-D images of the capillary network and the lamina propria cell network at different angles of rotation (E , i , ii) . Calibration bar in (B) represents 10 μm (A , B) , 15 μm (C , D) . Calibration bar in (E) represents 5 μm.
    Figure Legend Snippet: Whole mounts of urinary bladder tissue were prepared at the urothelial-lamina junction and contained a dense network of capillaries, small blood vessels and cells from rat pups aged ≤ P21. Capillaries, blood vessels and cells were loaded with the fluorescent dye (Fluo-2, green) (A , B,E) . Tetramethylrhodamine (TRITC; red) was picked up by urothelial cells and provided contrast to Fluo-2 loaded cells (A , B) . The cellular network in the lamina propria was heterogeneous with numerous small round, stellate or spindle shaped cells (10–20 μm) with multiple processes projecting from the soma in rat pups aged P ≤ 21. Numerous cells in the lamina propria exhibited PDGFRα-immunoreactivity (IR) whereas fewer cells exhibited TRPV4-IR (C,D) . At the urothelial-lamina propria junction, a dense capillary network was in close proximity to the network of cells expressing PDGFRα- and TRPV4-IR (E) . Capillaries were isolated using their signature, long tubular shape in the PTCL analysis software and recolored red to distinguish them from lamina propria cells. 3-D images of the capillary network and the lamina propria cell network at different angles of rotation (E , i , ii) . Calibration bar in (B) represents 10 μm (A , B) , 15 μm (C , D) . Calibration bar in (E) represents 5 μm.

    Techniques Used: Expressing, Isolation, Software

    5) Product Images from "TRPV4 Overexpression Promotes Metastasis Through Epithelial–Mesenchymal Transition in Gastric Cancer and Correlates with Poor Prognosis"

    Article Title: TRPV4 Overexpression Promotes Metastasis Through Epithelial–Mesenchymal Transition in Gastric Cancer and Correlates with Poor Prognosis

    Journal: OncoTargets and therapy

    doi: 10.2147/OTT.S256918

    Transwell assays demonstrated that TRPV4 down-regulation greatly inhibited invasion abilities of gastric cancer cells. ( A and B ) Representative images of invasive cells following transfection with shTRPV4 or shCtrl. Magnification, ×200. ( C and D ) The column diagram of the numbers of invasive cells following transfection with shTRPV4 or shCtrl. **P
    Figure Legend Snippet: Transwell assays demonstrated that TRPV4 down-regulation greatly inhibited invasion abilities of gastric cancer cells. ( A and B ) Representative images of invasive cells following transfection with shTRPV4 or shCtrl. Magnification, ×200. ( C and D ) The column diagram of the numbers of invasive cells following transfection with shTRPV4 or shCtrl. **P

    Techniques Used: Transfection

    Detection of TRPV4 expression in gastric adenocarcinoma tissues and adjacent noncancerous tissues by IHC staining of tissue microarrays. ( A ) Representative images of TRPV4 expression in gastric adenocarcinoma tissues and adjacent noncancerous tissues. (a, b) Weakly focal positive TRPV4 expression in adjacent noncancerous gastric epithelia. (c, d) Strongly positive TRPV4 expression in a case of gastric adenocarcinoma. ( B ) Scatterplots of IHC scores of TRPV4 expression in gastric adenocarcinoma tissues and adjacent noncancerous tissues. ( C ) Percents of tissue samples with high TRPV4 expression and low TRPV4 expression based on the cut-off value of IHC scores in gastric adenocarcinoma tissues and adjacent noncancerous tissues (***P
    Figure Legend Snippet: Detection of TRPV4 expression in gastric adenocarcinoma tissues and adjacent noncancerous tissues by IHC staining of tissue microarrays. ( A ) Representative images of TRPV4 expression in gastric adenocarcinoma tissues and adjacent noncancerous tissues. (a, b) Weakly focal positive TRPV4 expression in adjacent noncancerous gastric epithelia. (c, d) Strongly positive TRPV4 expression in a case of gastric adenocarcinoma. ( B ) Scatterplots of IHC scores of TRPV4 expression in gastric adenocarcinoma tissues and adjacent noncancerous tissues. ( C ) Percents of tissue samples with high TRPV4 expression and low TRPV4 expression based on the cut-off value of IHC scores in gastric adenocarcinoma tissues and adjacent noncancerous tissues (***P

    Techniques Used: Expressing, Immunohistochemistry, Staining

    The protein expression of TRPV4 in gastric cell lines and down-regulation of TPRV4 inhibited proliferation of gastric cancer cells. ( A ) The protein expression levels of TPRV4 were detected in gastric cancer cell lines (HGC-27 and MGC-803) and normal gastric mucosa cell GES-1 by Western blot. **P
    Figure Legend Snippet: The protein expression of TRPV4 in gastric cell lines and down-regulation of TPRV4 inhibited proliferation of gastric cancer cells. ( A ) The protein expression levels of TPRV4 were detected in gastric cancer cell lines (HGC-27 and MGC-803) and normal gastric mucosa cell GES-1 by Western blot. **P

    Techniques Used: Expressing, Western Blot

    Survival curves using the Kaplan–Meier method by Log rank test. ( A and B ) The patients with high TRPV4 expression had shorter overall survival and disease-free survival than those with low TRPV4 expression. ( C and D ) The patients with low E-cadherin expression had shorter overall survival and disease-free survival than those with high E-cadherin expression. ( E and F ) The patients with high vimentin expression had shorter overall survival and disease-free survival than those with low vimentin expression. ( G ) Overall survival analysis of TRPV4 gene in gastric cancer obtained from Kaplan–Meier Plotter online ( http://kmplot.com/analysis/ ). *P
    Figure Legend Snippet: Survival curves using the Kaplan–Meier method by Log rank test. ( A and B ) The patients with high TRPV4 expression had shorter overall survival and disease-free survival than those with low TRPV4 expression. ( C and D ) The patients with low E-cadherin expression had shorter overall survival and disease-free survival than those with high E-cadherin expression. ( E and F ) The patients with high vimentin expression had shorter overall survival and disease-free survival than those with low vimentin expression. ( G ) Overall survival analysis of TRPV4 gene in gastric cancer obtained from Kaplan–Meier Plotter online ( http://kmplot.com/analysis/ ). *P

    Techniques Used: Expressing

    Representation images of TRPV4, E-cadherin and vimentin expression in gastric cancer tissues by immunohistochemical staining. Magnification, ×400. ( A – C ) High TRPV4 expression in a case of poor differentiated gastric adenocarcinoma with loss expression of E-cadherin and positive vimentin expression. ( D – F ) Low TRPV4 expression in a case of signet ring cell carcinoma with high E-cadherin expression and negative Vimentin expression. Abbreviation: TRPV4, transient receptor potential vanilloid 4.
    Figure Legend Snippet: Representation images of TRPV4, E-cadherin and vimentin expression in gastric cancer tissues by immunohistochemical staining. Magnification, ×400. ( A – C ) High TRPV4 expression in a case of poor differentiated gastric adenocarcinoma with loss expression of E-cadherin and positive vimentin expression. ( D – F ) Low TRPV4 expression in a case of signet ring cell carcinoma with high E-cadherin expression and negative Vimentin expression. Abbreviation: TRPV4, transient receptor potential vanilloid 4.

    Techniques Used: Expressing, Immunohistochemistry, Staining

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    Alomone Labs intracellular trpv4
    p38 activation and macrophage phagocytosis in response to LPS is dependent on matrix stiffness. Phosphorylated and total A. p38 and B. JNK on various matrix stiffnesses in the physiologic range (1kPa, 8kPa, and 25kPa) from WT vs <t>TRPV4</t> KO BMDMs quantified for LPS 15 minutes ( *p = 0.031). C. Macrophage phagocytosis of E. coli particles ± p38 inhibition (SB, BIRB) on various matrix stiffnesses ( *p
    Intracellular Trpv4, supplied by Alomone Labs, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/intracellular trpv4/product/Alomone Labs
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    intracellular trpv4 - by Bioz Stars, 2022-05
    92/100 stars
      Buy from Supplier

    Image Search Results


    p38 activation and macrophage phagocytosis in response to LPS is dependent on matrix stiffness. Phosphorylated and total A. p38 and B. JNK on various matrix stiffnesses in the physiologic range (1kPa, 8kPa, and 25kPa) from WT vs TRPV4 KO BMDMs quantified for LPS 15 minutes ( *p = 0.031). C. Macrophage phagocytosis of E. coli particles ± p38 inhibition (SB, BIRB) on various matrix stiffnesses ( *p

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

    Article Title: TRPV4 Protects the Lung from Bacterial Pneumonia via MAPK Molecular Pathway Switching

    doi: 10.4049/jimmunol.1901033

    Figure Lengend Snippet: p38 activation and macrophage phagocytosis in response to LPS is dependent on matrix stiffness. Phosphorylated and total A. p38 and B. JNK on various matrix stiffnesses in the physiologic range (1kPa, 8kPa, and 25kPa) from WT vs TRPV4 KO BMDMs quantified for LPS 15 minutes ( *p = 0.031). C. Macrophage phagocytosis of E. coli particles ± p38 inhibition (SB, BIRB) on various matrix stiffnesses ( *p

    Article Snippet: The following primary antibodies were purchased: intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), extracellular TRPV4 (Alomone Labs, Jerusalem, Israel), anti-phospho p38 (Thr180/Tyr182, Cell Signaling, MA), anti-p38 (Santa Cruz, CA), anti-phospho JNK (Cell Signaling), anti-JNK (Cell Signaling), anti-phospho ERK (Santa Cruz), anti-ERK (Cell Signaling), anti-phospho MK2 (Cell Signaling), anti-MK2 (Cell Signaling), anti-phospho MKK3/MKK6 (Cell Signaling), anti-MKK3 (Cell Signaling), anti-MKK6 (Cell Signaling), anti-GAPDH (Fitzgerald Industries International, Acton, MA), anti-DUSP1/MKP1 (Santa Cruz, CA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma-Aldrich, St. Louis, MO).

    Techniques: Activation Assay, Inhibition

    TRPV4-mediated p38 MAPK and JNK molecular switch is regulated by dual-specificity phosphatase 1 (DUSP1). WT and TRPV4 KO BMDMs were incubated ± LPS as above for indicated time, and cells were lysed and analyzed by A. immunoblot for DUSP1 and B. band density quantified as DUSP1/GAPDH from immunoblot (n = 4) ( *p

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

    Article Title: TRPV4 Protects the Lung from Bacterial Pneumonia via MAPK Molecular Pathway Switching

    doi: 10.4049/jimmunol.1901033

    Figure Lengend Snippet: TRPV4-mediated p38 MAPK and JNK molecular switch is regulated by dual-specificity phosphatase 1 (DUSP1). WT and TRPV4 KO BMDMs were incubated ± LPS as above for indicated time, and cells were lysed and analyzed by A. immunoblot for DUSP1 and B. band density quantified as DUSP1/GAPDH from immunoblot (n = 4) ( *p

    Article Snippet: The following primary antibodies were purchased: intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), extracellular TRPV4 (Alomone Labs, Jerusalem, Israel), anti-phospho p38 (Thr180/Tyr182, Cell Signaling, MA), anti-p38 (Santa Cruz, CA), anti-phospho JNK (Cell Signaling), anti-JNK (Cell Signaling), anti-phospho ERK (Santa Cruz), anti-ERK (Cell Signaling), anti-phospho MK2 (Cell Signaling), anti-MK2 (Cell Signaling), anti-phospho MKK3/MKK6 (Cell Signaling), anti-MKK3 (Cell Signaling), anti-MKK6 (Cell Signaling), anti-GAPDH (Fitzgerald Industries International, Acton, MA), anti-DUSP1/MKP1 (Santa Cruz, CA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma-Aldrich, St. Louis, MO).

    Techniques: Incubation

    TRPV4 function protects against lung injury in a murine Pseudomonas aeruginosa pneumonia model. Sterile beads or P. aeruginosa (PA, PAM57–15) were instilled intratracheally in TRPV4 KO and age-matched female congenic WT mice with BAL and tissue harvest performed at Day 3 (injury phase). TRPV4 deleted mice (TRPV4 KO) have greater A. inflammatory cell infiltration and B. BAL total protein compared to WT (* p

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

    Article Title: TRPV4 Protects the Lung from Bacterial Pneumonia via MAPK Molecular Pathway Switching

    doi: 10.4049/jimmunol.1901033

    Figure Lengend Snippet: TRPV4 function protects against lung injury in a murine Pseudomonas aeruginosa pneumonia model. Sterile beads or P. aeruginosa (PA, PAM57–15) were instilled intratracheally in TRPV4 KO and age-matched female congenic WT mice with BAL and tissue harvest performed at Day 3 (injury phase). TRPV4 deleted mice (TRPV4 KO) have greater A. inflammatory cell infiltration and B. BAL total protein compared to WT (* p

    Article Snippet: The following primary antibodies were purchased: intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), extracellular TRPV4 (Alomone Labs, Jerusalem, Israel), anti-phospho p38 (Thr180/Tyr182, Cell Signaling, MA), anti-p38 (Santa Cruz, CA), anti-phospho JNK (Cell Signaling), anti-JNK (Cell Signaling), anti-phospho ERK (Santa Cruz), anti-ERK (Cell Signaling), anti-phospho MK2 (Cell Signaling), anti-MK2 (Cell Signaling), anti-phospho MKK3/MKK6 (Cell Signaling), anti-MKK3 (Cell Signaling), anti-MKK6 (Cell Signaling), anti-GAPDH (Fitzgerald Industries International, Acton, MA), anti-DUSP1/MKP1 (Santa Cruz, CA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma-Aldrich, St. Louis, MO).

    Techniques: Mouse Assay

    p38 MAPK and JNK are differentially regulated by TRPV4 after LPS or Pseudomonas aeruginosa . BMDMs were incubated ± LPS as above for indicated time cultured on tissue culture-treated plastic, and cells were lysed and analyzed by immunoblot for A. phosphorylated and total p38, ERK, and JNK compared to WT BMDMs (whole cell lysate). Band density quantified from immunoblot (n = 3–6) for B. p-p38/total p38 ( *p

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

    Article Title: TRPV4 Protects the Lung from Bacterial Pneumonia via MAPK Molecular Pathway Switching

    doi: 10.4049/jimmunol.1901033

    Figure Lengend Snippet: p38 MAPK and JNK are differentially regulated by TRPV4 after LPS or Pseudomonas aeruginosa . BMDMs were incubated ± LPS as above for indicated time cultured on tissue culture-treated plastic, and cells were lysed and analyzed by immunoblot for A. phosphorylated and total p38, ERK, and JNK compared to WT BMDMs (whole cell lysate). Band density quantified from immunoblot (n = 3–6) for B. p-p38/total p38 ( *p

    Article Snippet: The following primary antibodies were purchased: intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), extracellular TRPV4 (Alomone Labs, Jerusalem, Israel), anti-phospho p38 (Thr180/Tyr182, Cell Signaling, MA), anti-p38 (Santa Cruz, CA), anti-phospho JNK (Cell Signaling), anti-JNK (Cell Signaling), anti-phospho ERK (Santa Cruz), anti-ERK (Cell Signaling), anti-phospho MK2 (Cell Signaling), anti-MK2 (Cell Signaling), anti-phospho MKK3/MKK6 (Cell Signaling), anti-MKK3 (Cell Signaling), anti-MKK6 (Cell Signaling), anti-GAPDH (Fitzgerald Industries International, Acton, MA), anti-DUSP1/MKP1 (Santa Cruz, CA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma-Aldrich, St. Louis, MO).

    Techniques: Incubation, Cell Culture

    TRPV4 mediates phagocytosis after LPS in healthy human through p38 MAPK. Monocyte derived and alveolar macrophages from healthy (n = 6) control subjects were incubated ± LPS ± TRPV4 inhibitor, HC, and phagocytosis of E. coli particles was measured in A. monocyte-derived and B. alveolar macrophages in healthy controls. HC alone had no effect. Representative immunoblot for phosphorylated and total p38 in C. healthy monocyte derived macrophages ± LPS 15 minutes and D. band density quantified ( *p

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

    Article Title: TRPV4 Protects the Lung from Bacterial Pneumonia via MAPK Molecular Pathway Switching

    doi: 10.4049/jimmunol.1901033

    Figure Lengend Snippet: TRPV4 mediates phagocytosis after LPS in healthy human through p38 MAPK. Monocyte derived and alveolar macrophages from healthy (n = 6) control subjects were incubated ± LPS ± TRPV4 inhibitor, HC, and phagocytosis of E. coli particles was measured in A. monocyte-derived and B. alveolar macrophages in healthy controls. HC alone had no effect. Representative immunoblot for phosphorylated and total p38 in C. healthy monocyte derived macrophages ± LPS 15 minutes and D. band density quantified ( *p

    Article Snippet: The following primary antibodies were purchased: intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), extracellular TRPV4 (Alomone Labs, Jerusalem, Israel), anti-phospho p38 (Thr180/Tyr182, Cell Signaling, MA), anti-p38 (Santa Cruz, CA), anti-phospho JNK (Cell Signaling), anti-JNK (Cell Signaling), anti-phospho ERK (Santa Cruz), anti-ERK (Cell Signaling), anti-phospho MK2 (Cell Signaling), anti-MK2 (Cell Signaling), anti-phospho MKK3/MKK6 (Cell Signaling), anti-MKK3 (Cell Signaling), anti-MKK6 (Cell Signaling), anti-GAPDH (Fitzgerald Industries International, Acton, MA), anti-DUSP1/MKP1 (Santa Cruz, CA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma-Aldrich, St. Louis, MO).

    Techniques: Derivative Assay, Incubation

    TRPV4 mediates clearance of P. aeruginosa by macrophages. WT and TRPV4 KO mice were intratracheally administered ±GFP P. aeruginosa for 3 days. Representative confocal images of whole lung lavage cytospins of macrophages (open arrowhead) and neutrophils (filled arrowhead) in WT mice given IT sterile beads or GFP- P. aeruginosa after immunofluorescence with A. TRPV4 extracellular antibody (green, TRPV4) and C. anti-GFP (green, GFP P. aeruginosa ; anti-CD45, red; dapi, blue). B, D. Quantification of A, C . * , # p

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

    Article Title: TRPV4 Protects the Lung from Bacterial Pneumonia via MAPK Molecular Pathway Switching

    doi: 10.4049/jimmunol.1901033

    Figure Lengend Snippet: TRPV4 mediates clearance of P. aeruginosa by macrophages. WT and TRPV4 KO mice were intratracheally administered ±GFP P. aeruginosa for 3 days. Representative confocal images of whole lung lavage cytospins of macrophages (open arrowhead) and neutrophils (filled arrowhead) in WT mice given IT sterile beads or GFP- P. aeruginosa after immunofluorescence with A. TRPV4 extracellular antibody (green, TRPV4) and C. anti-GFP (green, GFP P. aeruginosa ; anti-CD45, red; dapi, blue). B, D. Quantification of A, C . * , # p

    Article Snippet: The following primary antibodies were purchased: intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), extracellular TRPV4 (Alomone Labs, Jerusalem, Israel), anti-phospho p38 (Thr180/Tyr182, Cell Signaling, MA), anti-p38 (Santa Cruz, CA), anti-phospho JNK (Cell Signaling), anti-JNK (Cell Signaling), anti-phospho ERK (Santa Cruz), anti-ERK (Cell Signaling), anti-phospho MK2 (Cell Signaling), anti-MK2 (Cell Signaling), anti-phospho MKK3/MKK6 (Cell Signaling), anti-MKK3 (Cell Signaling), anti-MKK6 (Cell Signaling), anti-GAPDH (Fitzgerald Industries International, Acton, MA), anti-DUSP1/MKP1 (Santa Cruz, CA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma-Aldrich, St. Louis, MO).

    Techniques: Mouse Assay, Immunofluorescence

    TRPV4 modulates pro-inflammatory cytokine production through JNK. BMDMs were incubated ± LPS (100ng/mL, 24h) ± JNK inhibitor, SP600125 (20μM, 25h) ± p38 inhibitor, SB203580 (10μM, 25h), cultured on cell culture-treated plastic, and cytokines measured via ELISA. IL-6, CXCL2, and CXCL1 secretion ± LPS in A. WT and TRPV4 KO BMDMs and B. WT BMDMs ± SP600125 ± SB203580 ( *, # p

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

    Article Title: TRPV4 Protects the Lung from Bacterial Pneumonia via MAPK Molecular Pathway Switching

    doi: 10.4049/jimmunol.1901033

    Figure Lengend Snippet: TRPV4 modulates pro-inflammatory cytokine production through JNK. BMDMs were incubated ± LPS (100ng/mL, 24h) ± JNK inhibitor, SP600125 (20μM, 25h) ± p38 inhibitor, SB203580 (10μM, 25h), cultured on cell culture-treated plastic, and cytokines measured via ELISA. IL-6, CXCL2, and CXCL1 secretion ± LPS in A. WT and TRPV4 KO BMDMs and B. WT BMDMs ± SP600125 ± SB203580 ( *, # p

    Article Snippet: The following primary antibodies were purchased: intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), extracellular TRPV4 (Alomone Labs, Jerusalem, Israel), anti-phospho p38 (Thr180/Tyr182, Cell Signaling, MA), anti-p38 (Santa Cruz, CA), anti-phospho JNK (Cell Signaling), anti-JNK (Cell Signaling), anti-phospho ERK (Santa Cruz), anti-ERK (Cell Signaling), anti-phospho MK2 (Cell Signaling), anti-MK2 (Cell Signaling), anti-phospho MKK3/MKK6 (Cell Signaling), anti-MKK3 (Cell Signaling), anti-MKK6 (Cell Signaling), anti-GAPDH (Fitzgerald Industries International, Acton, MA), anti-DUSP1/MKP1 (Santa Cruz, CA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma-Aldrich, St. Louis, MO).

    Techniques: Incubation, Cell Culture, Enzyme-linked Immunosorbent Assay

    TRPV4 modulates the cytokine response to LPS in a manner that depends on matrix stiffness

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

    Article Title: TRPV4 Mechanosensitive Ion Channel Regulates LPS-Stimulated Macrophage Phagocytosis

    doi: 10.4049/jimmunol.1501688

    Figure Lengend Snippet: TRPV4 modulates the cytokine response to LPS in a manner that depends on matrix stiffness

    Article Snippet: Primary antibodies to intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), GAPDH (Fitzgerald Industries International, Acton, MA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma, St. Louis, MO) were purchased.

    Techniques:

    Working model illustrating that LPS and TRPV4 signal cooperate to alter macrophage phenotypic change leading to enhanced clearance of infection and resolution of lung injury

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

    Article Title: TRPV4 Mechanosensitive Ion Channel Regulates LPS-Stimulated Macrophage Phagocytosis

    doi: 10.4049/jimmunol.1501688

    Figure Lengend Snippet: Working model illustrating that LPS and TRPV4 signal cooperate to alter macrophage phenotypic change leading to enhanced clearance of infection and resolution of lung injury

    Article Snippet: Primary antibodies to intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), GAPDH (Fitzgerald Industries International, Acton, MA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma, St. Louis, MO) were purchased.

    Techniques: Infection

    TRPV4 mediates LPS-stimulated macrophage phagocytosis of E. coli particles

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

    Article Title: TRPV4 Mechanosensitive Ion Channel Regulates LPS-Stimulated Macrophage Phagocytosis

    doi: 10.4049/jimmunol.1501688

    Figure Lengend Snippet: TRPV4 mediates LPS-stimulated macrophage phagocytosis of E. coli particles

    Article Snippet: Primary antibodies to intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), GAPDH (Fitzgerald Industries International, Acton, MA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma, St. Louis, MO) were purchased.

    Techniques:

    TRPV4 mediates LPS-stimulated macrophage phagocytosis of IgG-coated latex beads in vitro

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

    Article Title: TRPV4 Mechanosensitive Ion Channel Regulates LPS-Stimulated Macrophage Phagocytosis

    doi: 10.4049/jimmunol.1501688

    Figure Lengend Snippet: TRPV4 mediates LPS-stimulated macrophage phagocytosis of IgG-coated latex beads in vitro

    Article Snippet: Primary antibodies to intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), GAPDH (Fitzgerald Industries International, Acton, MA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma, St. Louis, MO) were purchased.

    Techniques: In Vitro

    TRPV4 mediates the stiffness induction effect on LPS-stimulated calcium influx and macrophage phagocytosis

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

    Article Title: TRPV4 Mechanosensitive Ion Channel Regulates LPS-Stimulated Macrophage Phagocytosis

    doi: 10.4049/jimmunol.1501688

    Figure Lengend Snippet: TRPV4 mediates the stiffness induction effect on LPS-stimulated calcium influx and macrophage phagocytosis

    Article Snippet: Primary antibodies to intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), GAPDH (Fitzgerald Industries International, Acton, MA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma, St. Louis, MO) were purchased.

    Techniques:

    TRPV4 mediates LPS-stimulated macrophage phagocytosis of IgG-coated latex beads in vivo

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

    Article Title: TRPV4 Mechanosensitive Ion Channel Regulates LPS-Stimulated Macrophage Phagocytosis

    doi: 10.4049/jimmunol.1501688

    Figure Lengend Snippet: TRPV4 mediates LPS-stimulated macrophage phagocytosis of IgG-coated latex beads in vivo

    Article Snippet: Primary antibodies to intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), GAPDH (Fitzgerald Industries International, Acton, MA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma, St. Louis, MO) were purchased.

    Techniques: In Vivo

    Functional TRPV4 is expressed in murine BMDMs

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

    Article Title: TRPV4 Mechanosensitive Ion Channel Regulates LPS-Stimulated Macrophage Phagocytosis

    doi: 10.4049/jimmunol.1501688

    Figure Lengend Snippet: Functional TRPV4 is expressed in murine BMDMs

    Article Snippet: Primary antibodies to intracellular TRPV4 (Alomone Labs, Jerusalem, Israel), GAPDH (Fitzgerald Industries International, Acton, MA), α-CD45 (BD Biosciences), and purified rabbit IgG from mouse serum (Sigma, St. Louis, MO) were purchased.

    Techniques: Functional Assay

    Whole mounts of urinary bladder tissue were prepared at the urothelial-lamina junction and contained a dense network of capillaries, small blood vessels and cells from rat pups aged ≤ P21. Capillaries, blood vessels and cells were loaded with the fluorescent dye (Fluo-2, green) (A , B,E) . Tetramethylrhodamine (TRITC; red) was picked up by urothelial cells and provided contrast to Fluo-2 loaded cells (A , B) . The cellular network in the lamina propria was heterogeneous with numerous small round, stellate or spindle shaped cells (10–20 μm) with multiple processes projecting from the soma in rat pups aged P ≤ 21. Numerous cells in the lamina propria exhibited PDGFRα-immunoreactivity (IR) whereas fewer cells exhibited TRPV4-IR (C,D) . At the urothelial-lamina propria junction, a dense capillary network was in close proximity to the network of cells expressing PDGFRα- and TRPV4-IR (E) . Capillaries were isolated using their signature, long tubular shape in the PTCL analysis software and recolored red to distinguish them from lamina propria cells. 3-D images of the capillary network and the lamina propria cell network at different angles of rotation (E , i , ii) . Calibration bar in (B) represents 10 μm (A , B) , 15 μm (C , D) . Calibration bar in (E) represents 5 μm.

    Journal: Frontiers in Systems Neuroscience

    Article Title: Rhythmic Calcium Events in the Lamina Propria Network of the Urinary Bladder of Rat Pups

    doi: 10.3389/fnsys.2017.00087

    Figure Lengend Snippet: Whole mounts of urinary bladder tissue were prepared at the urothelial-lamina junction and contained a dense network of capillaries, small blood vessels and cells from rat pups aged ≤ P21. Capillaries, blood vessels and cells were loaded with the fluorescent dye (Fluo-2, green) (A , B,E) . Tetramethylrhodamine (TRITC; red) was picked up by urothelial cells and provided contrast to Fluo-2 loaded cells (A , B) . The cellular network in the lamina propria was heterogeneous with numerous small round, stellate or spindle shaped cells (10–20 μm) with multiple processes projecting from the soma in rat pups aged P ≤ 21. Numerous cells in the lamina propria exhibited PDGFRα-immunoreactivity (IR) whereas fewer cells exhibited TRPV4-IR (C,D) . At the urothelial-lamina propria junction, a dense capillary network was in close proximity to the network of cells expressing PDGFRα- and TRPV4-IR (E) . Capillaries were isolated using their signature, long tubular shape in the PTCL analysis software and recolored red to distinguish them from lamina propria cells. 3-D images of the capillary network and the lamina propria cell network at different angles of rotation (E , i , ii) . Calibration bar in (B) represents 10 μm (A , B) , 15 μm (C , D) . Calibration bar in (E) represents 5 μm.

    Article Snippet: The following primary antibodies were used: rabbit anti-TRPV4 (1:1K; Abcam, catalog #ab39260) (Merrill et al., ), rabbit anti-TRPV4-ATTO-550 (1:500; Alomone Labs, Jerusalem, Israel, catalog #ACC-034-AO), rabbit anti-PDGFRα (1:8K; Thermo-Fisher Scientific, Waltham, MA, catalog #701142), rabbit anti-PDGFRα (1:1K; MyBioSource, Inc. San Diego, CA, catalog #MBS821212).

    Techniques: Expressing, Isolation, Software