Review

shrna lentiviral construct against sufu (Santa Cruz Biotechnology)

Santa Cruz Biotechnology is a verified supplier

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

Santa Cruz Biotechnology shrna lentiviral construct against sufu

IMP inhibits Hh signal at the level of GLI. ( A ) Western blot analysis of <t>SUFU</t> expression in wild-type (shCtrl) and SUFU-knockdown (shSUFU) Light II cells. The GAPDH was shown as a loading control. ( B ) GLI-luciferase reporter activity in shSUFU Light II cells treated with IMP (10 μM, 20 μM) or GDC (1μM) for 36 h. ( C ) Western blot analysis of GLI1 expression in shSUFU-Light II cells treated with IMP (10 μM, 20 μM) or GDC (1μM) for 24 h. The GAPDH was shown as a loading control. ( D and E ) Dose-response inhibition of GLI-luciferase activity by IMP in Light II cells with overexpression of GLI1-Flag ( D ) or GLI2-Myc ( E ). ( F ) Western blot analysis of Flag expression in Light II cells with overexpression of GLI1-Flag. The β-actin was shown as a loading control. All experiments were repeated at least three times. Statistical significance was calculated using Student t test, # P>0.05, *P <0.05.

Shrna Lentiviral Construct Against Sufu, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/sufu+shrna/Su(fu)+siRNA/pmc11586484-63-0-8
Average 92 stars, based on 8 article reviews

shrna lentiviral construct against sufu - by Bioz Stars, 2026-09

92/100 stars

Images

1) Product Images from "Imperatorin Suppresses Aberrant Hedgehog Pathway and Overcomes Smoothened Antagonist Resistance via STAT3 Inhibition"

Article Title: Imperatorin Suppresses Aberrant Hedgehog Pathway and Overcomes Smoothened Antagonist Resistance via STAT3 Inhibition

Journal: Drug Design, Development and Therapy

doi: 10.2147/DDDT.S482894

IMP inhibits Hh signal at the level of GLI. ( A ) Western blot analysis of SUFU expression in wild-type (shCtrl) and SUFU-knockdown (shSUFU) Light II cells. The GAPDH was shown as a loading control. ( B ) GLI-luciferase reporter activity in shSUFU Light II cells treated with IMP (10 μM, 20 μM) or GDC (1μM) for 36 h. ( C ) Western blot analysis of GLI1 expression in shSUFU-Light II cells treated with IMP (10 μM, 20 μM) or GDC (1μM) for 24 h. The GAPDH was shown as a loading control. ( D and E ) Dose-response inhibition of GLI-luciferase activity by IMP in Light II cells with overexpression of GLI1-Flag ( D ) or GLI2-Myc ( E ). ( F ) Western blot analysis of Flag expression in Light II cells with overexpression of GLI1-Flag. The β-actin was shown as a loading control. All experiments were repeated at least three times. Statistical significance was calculated using Student t test, # P>0.05, *P <0.05.

Figure Legend Snippet: IMP inhibits Hh signal at the level of GLI. ( A ) Western blot analysis of SUFU expression in wild-type (shCtrl) and SUFU-knockdown (shSUFU) Light II cells. The GAPDH was shown as a loading control. ( B ) GLI-luciferase reporter activity in shSUFU Light II cells treated with IMP (10 μM, 20 μM) or GDC (1μM) for 36 h. ( C ) Western blot analysis of GLI1 expression in shSUFU-Light II cells treated with IMP (10 μM, 20 μM) or GDC (1μM) for 24 h. The GAPDH was shown as a loading control. ( D and E ) Dose-response inhibition of GLI-luciferase activity by IMP in Light II cells with overexpression of GLI1-Flag ( D ) or GLI2-Myc ( E ). ( F ) Western blot analysis of Flag expression in Light II cells with overexpression of GLI1-Flag. The β-actin was shown as a loading control. All experiments were repeated at least three times. Statistical significance was calculated using Student t test, # P>0.05, *P <0.05.

Techniques Used: Western Blot, Expressing, Knockdown, Control, Luciferase, Activity Assay, Inhibition, Over Expression

Schematic illustration of the function and mechanism of IMP in overcoming the resistance of SMO inhibitors. IMP inhibited GLI1 transcription by acting at its promoter via STAT3, thereby circumventing various resistance mechanisms of clinical available anti-Hh drugs, including SMO mutations, loss of SUFU and GLI2 amplifications.

Figure Legend Snippet: Schematic illustration of the function and mechanism of IMP in overcoming the resistance of SMO inhibitors. IMP inhibited GLI1 transcription by acting at its promoter via STAT3, thereby circumventing various resistance mechanisms of clinical available anti-Hh drugs, including SMO mutations, loss of SUFU and GLI2 amplifications.

Techniques Used:

Construct:

Article Title: ABT-737 suppresses aberrant Hedgehog pathway and overcomes resistance to smoothened antagonists by blocking Gli.
Article Snippet: Abnormally activated Hedgehog (Hh) pathway has been linked to multiple types of cancers including medulloblastoma (MB).. Current Hh-targeted drug development projects mainly focus on antagonizing the upstream oncoprotein Smoothened (Smo).. However, the effectiveness of Smo inhibitors is compromised by primary and acquired resistance, which is caused by mutations of Smo or other downstream components.

shRNA:

Article Title: Saikosaponin B1 and Saikosaponin D inhibit tumor growth in medulloblastoma allograft mice via inhibiting the Hedgehog signaling pathway.
Article Snippet: Medulloblastoma (MB), accounting for nearly 10% of all childhood brain tumors, are implicated with aberrant activation of the Hedgehog (Hh) signaling pathway.. Saikosaponin B1 (SSB1) and Saikosaponin D (SSD), two bioactive constituents of Radix Bupleuri, are reported to have many biological activities including anticancer activities.. In our work, we evaluated the inhibition of SSB1 and SSD on MB tumor growth in allograft mice and explored the underlying mechanisms.

Image Search Results

Journal: Drug Design, Development and Therapy

Article Title: Imperatorin Suppresses Aberrant Hedgehog Pathway and Overcomes Smoothened Antagonist Resistance via STAT3 Inhibition

doi: 10.2147/DDDT.S482894

Figure Lengend Snippet: IMP inhibits Hh signal at the level of GLI. ( A ) Western blot analysis of SUFU expression in wild-type (shCtrl) and SUFU-knockdown (shSUFU) Light II cells. The GAPDH was shown as a loading control. ( B ) GLI-luciferase reporter activity in shSUFU Light II cells treated with IMP (10 μM, 20 μM) or GDC (1μM) for 36 h. ( C ) Western blot analysis of GLI1 expression in shSUFU-Light II cells treated with IMP (10 μM, 20 μM) or GDC (1μM) for 24 h. The GAPDH was shown as a loading control. ( D and E ) Dose-response inhibition of GLI-luciferase activity by IMP in Light II cells with overexpression of GLI1-Flag ( D ) or GLI2-Myc ( E ). ( F ) Western blot analysis of Flag expression in Light II cells with overexpression of GLI1-Flag. The β-actin was shown as a loading control. All experiments were repeated at least three times. Statistical significance was calculated using Student t test, # P>0.05, *P <0.05.

Article Snippet: shRNA lentiviral construct against SUFU was obtained from Santa Cruz (Santa Cruz, USA).

Techniques: Western Blot, Expressing, Knockdown, Control, Luciferase, Activity Assay, Inhibition, Over Expression

Journal: Drug Design, Development and Therapy

Article Title: Imperatorin Suppresses Aberrant Hedgehog Pathway and Overcomes Smoothened Antagonist Resistance via STAT3 Inhibition

doi: 10.2147/DDDT.S482894

Figure Lengend Snippet: Schematic illustration of the function and mechanism of IMP in overcoming the resistance of SMO inhibitors. IMP inhibited GLI1 transcription by acting at its promoter via STAT3, thereby circumventing various resistance mechanisms of clinical available anti-Hh drugs, including SMO mutations, loss of SUFU and GLI2 amplifications.

Article Snippet: shRNA lentiviral construct against SUFU was obtained from Santa Cruz (Santa Cruz, USA).

Techniques:

FIGURE 2 Wnt/β-catenin signalling promotes HSC contraction. LX2 human HSCs were treated with Wnt3a (50 ngml−1), XAV (10 μM), or IWR (5 μM) for 24 h or transfected with β-catenin siRNA with or without Wnt3a (50 ngml−1) for 48 h. (a) Collagen gel contraction; n = 5. (b) Cytoskeleton immunofluorescence (400× magnification, scale bars: 10 μm); n = 3. (c) Western blotting of phospho-MLC2; n = 5. (d) Immunofluorescence of phospho-MLC2 (400× magnification, scale bars: 10 μm); n = 3. In (a) and (c), *P < .05, significantly different from vehicle control or control siRNA, #P < .05, significantly different from Wnt3a + control siRNA

Journal: British journal of pharmacology

Article Title: Regulation of hepatic stellate cell contraction and cirrhotic portal hypertension by Wnt/β-catenin signalling via interaction with Gli1.

doi: 10.1111/bph.15289

Figure Lengend Snippet: FIGURE 2 Wnt/β-catenin signalling promotes HSC contraction. LX2 human HSCs were treated with Wnt3a (50 ngml−1), XAV (10 μM), or IWR (5 μM) for 24 h or transfected with β-catenin siRNA with or without Wnt3a (50 ngml−1) for 48 h. (a) Collagen gel contraction; n = 5. (b) Cytoskeleton immunofluorescence (400× magnification, scale bars: 10 μm); n = 3. (c) Western blotting of phospho-MLC2; n = 5. (d) Immunofluorescence of phospho-MLC2 (400× magnification, scale bars: 10 μm); n = 3. In (a) and (c), *P < .05, significantly different from vehicle control or control siRNA, #P < .05, significantly different from Wnt3a + control siRNA

Article Snippet: Cells were cultured in DMEM (Invitrogen, Grand Island, NY, USA) with 10% FBS (Wisent Biotechnology Co., Ltd., Nanjing, China), 1% antibiotics, and grown in a 5% CO2 humidified atmosphere at 37 C. β-Catenin siRNA (sc-29209), Gli1 siRNA (sc37911), Lrp6 siRNA (sc-37233), LARG siRNA (sc-41800), Sufu siRNA (sc-36572), TCF3 siRNA (sc-36618), TCF4 siRNA (sc-43525), and control siRNA (sc-37007) were obtained from Santa Cruz Biotechnology.

Techniques: Transfection, Immunofluorescence, Western Blot, Control

FIGURE 3 Wnt stimulates Smo-independent Gli1 nuclear translocation followed by LARG-mediated RhoA activation, leading to HSC contraction. LX2 human HSCs were treated with Wnt3a (50 ngml−1) and/or SIS3 (Smad3 inhibitor, 5 μM), SCH772984 (ERK inhibitor, 10 μM), MK2206 (AKT inhibitor, 5 μM), GANT-58 (Gli1 inhibitor, 5 μM), or PDTC (NF-κB inhibitor, 5 μM) for 24 h or transfected with β-catenin siRNA or Gli1 siRNA for 48 h. (a) Western blotting of phospho-MLC2; n = 5. (b) Collagen gel contraction; n = 5. (c) Cytoskeleton immunofluorescence (400× magnification, scale bars: 10 μm); n = 3. (d) Western blotting of active and total RhoA; n = 5. (e) Western blotting of LARG in whole cell lysates; n = 5. (f) Western blotting of active LARG in membrane lysates; n = 5. *P < .05, significantly different from vehicle control or control siRNA, #P < .05, significantly different from Wnt3a or Wnt3a + control siRNA, N.S., no significance

Journal: British journal of pharmacology

Article Title: Regulation of hepatic stellate cell contraction and cirrhotic portal hypertension by Wnt/β-catenin signalling via interaction with Gli1.

doi: 10.1111/bph.15289

Figure Lengend Snippet: FIGURE 3 Wnt stimulates Smo-independent Gli1 nuclear translocation followed by LARG-mediated RhoA activation, leading to HSC contraction. LX2 human HSCs were treated with Wnt3a (50 ngml−1) and/or SIS3 (Smad3 inhibitor, 5 μM), SCH772984 (ERK inhibitor, 10 μM), MK2206 (AKT inhibitor, 5 μM), GANT-58 (Gli1 inhibitor, 5 μM), or PDTC (NF-κB inhibitor, 5 μM) for 24 h or transfected with β-catenin siRNA or Gli1 siRNA for 48 h. (a) Western blotting of phospho-MLC2; n = 5. (b) Collagen gel contraction; n = 5. (c) Cytoskeleton immunofluorescence (400× magnification, scale bars: 10 μm); n = 3. (d) Western blotting of active and total RhoA; n = 5. (e) Western blotting of LARG in whole cell lysates; n = 5. (f) Western blotting of active LARG in membrane lysates; n = 5. *P < .05, significantly different from vehicle control or control siRNA, #P < .05, significantly different from Wnt3a or Wnt3a + control siRNA, N.S., no significance

Techniques: Translocation Assay, Activation Assay, Transfection, Western Blot, Immunofluorescence, Membrane, Control

FIGURE 4 Sufu negatively mediates Wnt interaction with Gli1 and induction of HSC contraction. LX2 human HSCs were treated with Wnt3a (50 ngml−1), XAV (10 μM), IWR (5 μM), or C59 (5 μM) for 24 h or transfected with β-catenin siRNA, Sufu siRNA, or Sufu overexpression plasmids with or without Wnt3a (50 ngml−1) for 48 h. (a) Western blotting of nuclear Gli1. *P < .05, significantly different from vehicle control or control siRNA, #P < .05, significantly different from Wnt3a + control siRNA; n = 5. (b) Immunofluorescence of Gli1 nuclear translocation (400× magnification, scale bars: 5 μm). Pearson's correlation coefficients were calculated to confirm Gli1 co-localization with cell nuclei. *P < .05, significantly different from vehicle control or control siRNA, #P < .05, significantly different from Wnt3a + control siRNA; n = 3. (c, d) Western blotting of nuclear Gli1. *P < .05, significantly different from control siRNA, #P < .05, significantly different from Sufu siRNA; n = 5. (e) Collagen gel contraction. *P < .05, significantly different from vector, #P < .05, significantly different from Wnt3a + vector; n = 5. (f) Cytoskeleton immunofluorescence (400× magnification, scale bars: 10 μm); n = 3

Journal: British journal of pharmacology

Article Title: Regulation of hepatic stellate cell contraction and cirrhotic portal hypertension by Wnt/β-catenin signalling via interaction with Gli1.

doi: 10.1111/bph.15289

Figure Lengend Snippet: FIGURE 4 Sufu negatively mediates Wnt interaction with Gli1 and induction of HSC contraction. LX2 human HSCs were treated with Wnt3a (50 ngml−1), XAV (10 μM), IWR (5 μM), or C59 (5 μM) for 24 h or transfected with β-catenin siRNA, Sufu siRNA, or Sufu overexpression plasmids with or without Wnt3a (50 ngml−1) for 48 h. (a) Western blotting of nuclear Gli1. *P < .05, significantly different from vehicle control or control siRNA, #P < .05, significantly different from Wnt3a + control siRNA; n = 5. (b) Immunofluorescence of Gli1 nuclear translocation (400× magnification, scale bars: 5 μm). Pearson's correlation coefficients were calculated to confirm Gli1 co-localization with cell nuclei. *P < .05, significantly different from vehicle control or control siRNA, #P < .05, significantly different from Wnt3a + control siRNA; n = 3. (c, d) Western blotting of nuclear Gli1. *P < .05, significantly different from control siRNA, #P < .05, significantly different from Sufu siRNA; n = 5. (e) Collagen gel contraction. *P < .05, significantly different from vector, #P < .05, significantly different from Wnt3a + vector; n = 5. (f) Cytoskeleton immunofluorescence (400× magnification, scale bars: 10 μm); n = 3

Techniques: Transfection, Over Expression, Western Blot, Control, Immunofluorescence, Translocation Assay, Plasmid Preparation

FIGURE 5 Wnt/β-catenin signalling represses Sufu transcription via TCF4 in HSCs. LX2 human HSCs were treated with Wnt3a (50 ngml−1), XAV (10 μM), IWR (5 μM), or C59 (5 μM) for 24 h or transfected with β-catenin siRNA, TCF3 siRNA, or TCF4 siRNA for 48 h. (a, e) Luciferase activities of Sufu promoter; n = 5. (b) Real-time PCR for Sufu; n = 5. (c, d) Western blotting for Sufu; n = 5.*P < .05, significantly different from vehicle control or control siRNA, #P < .05, significantly different from Wnt3a + control siRNA. (f) Co-immunoprecipitation for β-catenin/TCF4 physical interaction; n = 3

Journal: British journal of pharmacology

Article Title: Regulation of hepatic stellate cell contraction and cirrhotic portal hypertension by Wnt/β-catenin signalling via interaction with Gli1.

doi: 10.1111/bph.15289

Figure Lengend Snippet: FIGURE 5 Wnt/β-catenin signalling represses Sufu transcription via TCF4 in HSCs. LX2 human HSCs were treated with Wnt3a (50 ngml−1), XAV (10 μM), IWR (5 μM), or C59 (5 μM) for 24 h or transfected with β-catenin siRNA, TCF3 siRNA, or TCF4 siRNA for 48 h. (a, e) Luciferase activities of Sufu promoter; n = 5. (b) Real-time PCR for Sufu; n = 5. (c, d) Western blotting for Sufu; n = 5.*P < .05, significantly different from vehicle control or control siRNA, #P < .05, significantly different from Wnt3a + control siRNA. (f) Co-immunoprecipitation for β-catenin/TCF4 physical interaction; n = 3

Techniques: Transfection, Luciferase, Real-time Polymerase Chain Reaction, Western Blot, Control, Immunoprecipitation

FIGURE 6 Wnt/β-catenin repression of Sufu transcription requires β-catenin/TCF4 interaction and TCF4 binding to Sufu promoter in HSCs. (a) Molecular simulation of β-catenin/TCF3 or β-catenin/TCF4 physical interactions. (b–d) LX2 human HSCs were treated with Wnt3a (50 ngml−1) and/or transfected with β-catenin WT plasmids or β-catenin site-directed mutant plasmids at Lys312 or Lys435 for 48 h. (b) Luciferase activities of Sufu promoter. *P < .05, significantly different from control, #P < .05, significantly different from Wnt3a + WT plasmids; n = 5. (c) Real-time PCR of Sufu. *P < .05, significantly different from control, #P < .05, significantly different fromWnt3a + WT plasmids; n = 5. (d) Collagen gel contraction. *P < .05, significantly different from control, #P < .05, significantly different from Wnt3a + WT plasmids; n = 5. (e) Chromatin immunoprecipitation-quantitative PCR of TCF4 binding to Sufu promoter using two pairs of primers of Sufu gene. *P < .05, significantly different from control; n = 5. (f) LX2 human HSCs were transfected with WT or mutant luciferase reporter plasmids of Sufu followed by transfection with TCF4 overexpression plasmids for 48 h. Luciferase activities of Sufu promoter. *P < .05, significantly different as indicated; n = 5

Journal: British journal of pharmacology

Article Title: Regulation of hepatic stellate cell contraction and cirrhotic portal hypertension by Wnt/β-catenin signalling via interaction with Gli1.

doi: 10.1111/bph.15289

Figure Lengend Snippet: FIGURE 6 Wnt/β-catenin repression of Sufu transcription requires β-catenin/TCF4 interaction and TCF4 binding to Sufu promoter in HSCs. (a) Molecular simulation of β-catenin/TCF3 or β-catenin/TCF4 physical interactions. (b–d) LX2 human HSCs were treated with Wnt3a (50 ngml−1) and/or transfected with β-catenin WT plasmids or β-catenin site-directed mutant plasmids at Lys312 or Lys435 for 48 h. (b) Luciferase activities of Sufu promoter. *P < .05, significantly different from control, #P < .05, significantly different from Wnt3a + WT plasmids; n = 5. (c) Real-time PCR of Sufu. *P < .05, significantly different from control, #P < .05, significantly different fromWnt3a + WT plasmids; n = 5. (d) Collagen gel contraction. *P < .05, significantly different from control, #P < .05, significantly different from Wnt3a + WT plasmids; n = 5. (e) Chromatin immunoprecipitation-quantitative PCR of TCF4 binding to Sufu promoter using two pairs of primers of Sufu gene. *P < .05, significantly different from control; n = 5. (f) LX2 human HSCs were transfected with WT or mutant luciferase reporter plasmids of Sufu followed by transfection with TCF4 overexpression plasmids for 48 h. Luciferase activities of Sufu promoter. *P < .05, significantly different as indicated; n = 5

Techniques: Binding Assay, Transfection, Mutagenesis, Luciferase, Control, Real-time Polymerase Chain Reaction, Chromatin Immunoprecipitation, Over Expression

FIGURE 7 Short-term liver-targeted deficiency of β-catenin inhibits cirrhotic portal hypertension via decreasing HSC contraction in mice. Mice with CCl4-induced cirrhosis were administrated with AAV8-β-catenin shRNA via caudal vein once for 1 or 4 weeks. (a) Measurements of portal pressure; n = 5. (b) Collagen gel contraction in mouse primary HSCs; n = 5. (c) Real-time PCR of Col 1α1 in mouse primary HSCs; n = 5. (d) Real-time PCR of Sufu in mouse primary HSCs; n = 5. (e) Western blotting of Sufu and nuclear Gli1 in mouse primary HSCs; n = 5. *P < .05, significantly different from olive oil + AAV8-control shRNA, #P < .05, significantly different from CCl4 + AAV8-control shRNA

Journal: British journal of pharmacology

Article Title: Regulation of hepatic stellate cell contraction and cirrhotic portal hypertension by Wnt/β-catenin signalling via interaction with Gli1.

doi: 10.1111/bph.15289

Figure Lengend Snippet: FIGURE 7 Short-term liver-targeted deficiency of β-catenin inhibits cirrhotic portal hypertension via decreasing HSC contraction in mice. Mice with CCl4-induced cirrhosis were administrated with AAV8-β-catenin shRNA via caudal vein once for 1 or 4 weeks. (a) Measurements of portal pressure; n = 5. (b) Collagen gel contraction in mouse primary HSCs; n = 5. (c) Real-time PCR of Col 1α1 in mouse primary HSCs; n = 5. (d) Real-time PCR of Sufu in mouse primary HSCs; n = 5. (e) Western blotting of Sufu and nuclear Gli1 in mouse primary HSCs; n = 5. *P < .05, significantly different from olive oil + AAV8-control shRNA, #P < .05, significantly different from CCl4 + AAV8-control shRNA

Techniques: shRNA, Real-time Polymerase Chain Reaction, Western Blot, Control

FIGURE 8 Acute pharmacological blockade of β-catenin reduces portal hypertension via decreasing HSC contraction, and long-term treatment ameliorates liver fibrosis in mice. Mice with CCl4-induced cirrhosis were orally treated with XAV (20 mgkg−1) or IWR (10 mgkg−1) daily for 1 or 4 weeks. (a, b) Measurements of portal pressure; n = 5. (c) Collagen gel contraction in mouse primary HSCs; n = 5. (d) Real-time PCR of Col 1α1 in mouse primary HSCs; n = 5. (e) Real-time PCR of Sufu in mouse primary HSCs; n = 5. (f) Western blotting of Sufu and nuclear Gli1 in mouse primary HSCs; n = 5. *P < .05, significantly different from control, #P < .05, significantly different from CCl4

Journal: British journal of pharmacology

Article Title: Regulation of hepatic stellate cell contraction and cirrhotic portal hypertension by Wnt/β-catenin signalling via interaction with Gli1.

doi: 10.1111/bph.15289

Figure Lengend Snippet: FIGURE 8 Acute pharmacological blockade of β-catenin reduces portal hypertension via decreasing HSC contraction, and long-term treatment ameliorates liver fibrosis in mice. Mice with CCl4-induced cirrhosis were orally treated with XAV (20 mgkg−1) or IWR (10 mgkg−1) daily for 1 or 4 weeks. (a, b) Measurements of portal pressure; n = 5. (c) Collagen gel contraction in mouse primary HSCs; n = 5. (d) Real-time PCR of Col 1α1 in mouse primary HSCs; n = 5. (e) Real-time PCR of Sufu in mouse primary HSCs; n = 5. (f) Western blotting of Sufu and nuclear Gli1 in mouse primary HSCs; n = 5. *P < .05, significantly different from control, #P < .05, significantly different from CCl4

Techniques: Real-time Polymerase Chain Reaction, Western Blot, Control

FIGURE 9 Scheme of the molecular mechanisms underlying HSC contraction. Activation of Wnt/β-catenin signalling represses transcription of Sufu in a TCF4-dependent manner. This stimulates Gli1 nuclear translocation, leading to LARG-associated RhoA activation and results in contraction of HSCs. β-Catenin inhibitors reduce HSC contraction by disrupting this cascade and thereby exhibit therapeutic effects in models of cirrhotic portal hypertension

Journal: British journal of pharmacology

Article Title: Regulation of hepatic stellate cell contraction and cirrhotic portal hypertension by Wnt/β-catenin signalling via interaction with Gli1.

doi: 10.1111/bph.15289

Figure Lengend Snippet: FIGURE 9 Scheme of the molecular mechanisms underlying HSC contraction. Activation of Wnt/β-catenin signalling represses transcription of Sufu in a TCF4-dependent manner. This stimulates Gli1 nuclear translocation, leading to LARG-associated RhoA activation and results in contraction of HSCs. β-Catenin inhibitors reduce HSC contraction by disrupting this cascade and thereby exhibit therapeutic effects in models of cirrhotic portal hypertension

Techniques: Activation Assay, Translocation Assay

Review

shrna lentiviral construct against sufu (Santa Cruz Biotechnology)

Structured Review

Images

1) Product Images from "Imperatorin Suppresses Aberrant Hedgehog Pathway and Overcomes Smoothened Antagonist Resistance via STAT3 Inhibition"

Related Articles

Construct:

shRNA:

Similar Products

Image Search Results