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CNN3 promoted VSMCs proliferation <t>in</t> <t>β-catenin</t> dependent manner. (A) The VSMCs were transfected with siCNN3 or pcDNA3.1-CNN3. Immunofluorescence of β-catenin expression was detected by confocal laser-scanning microscopy. Then, the VSMCs were transfected with siCNN3 or pcDNA3.1-CNN3 with or without co-transfecting siβ-catenin. (B) CCK-8 assay was used to assess cell proliferation. (C) Cell proliferation was also evaluated using EdU staining. (D) Western blotting was performed to detect the expression levels of proteins (CDK4, CDK6, P16, P21 and P53) in VSMCs. Tubulin was used as a loading control. Data are given as the mean ± SD. All experiments were performed in triplicate. Scale bar = 100 μm ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.
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Image Search Results


CNN3 promoted VSMCs proliferation in β-catenin dependent manner. (A) The VSMCs were transfected with siCNN3 or pcDNA3.1-CNN3. Immunofluorescence of β-catenin expression was detected by confocal laser-scanning microscopy. Then, the VSMCs were transfected with siCNN3 or pcDNA3.1-CNN3 with or without co-transfecting siβ-catenin. (B) CCK-8 assay was used to assess cell proliferation. (C) Cell proliferation was also evaluated using EdU staining. (D) Western blotting was performed to detect the expression levels of proteins (CDK4, CDK6, P16, P21 and P53) in VSMCs. Tubulin was used as a loading control. Data are given as the mean ± SD. All experiments were performed in triplicate. Scale bar = 100 μm ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.

Journal: Atherosclerosis Plus

Article Title: CNN3 promotes vascular smooth muscle cells proliferation and migration to deteriorate atherosclerosis by β-catenin signaling pathway

doi: 10.1016/j.athplu.2026.100560

Figure Lengend Snippet: CNN3 promoted VSMCs proliferation in β-catenin dependent manner. (A) The VSMCs were transfected with siCNN3 or pcDNA3.1-CNN3. Immunofluorescence of β-catenin expression was detected by confocal laser-scanning microscopy. Then, the VSMCs were transfected with siCNN3 or pcDNA3.1-CNN3 with or without co-transfecting siβ-catenin. (B) CCK-8 assay was used to assess cell proliferation. (C) Cell proliferation was also evaluated using EdU staining. (D) Western blotting was performed to detect the expression levels of proteins (CDK4, CDK6, P16, P21 and P53) in VSMCs. Tubulin was used as a loading control. Data are given as the mean ± SD. All experiments were performed in triplicate. Scale bar = 100 μm ∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.

Article Snippet: The separated proteins were transferred to cellulose acetate membranes and then blocked with 5% BSA for 1 h at room temperature and incubated overnight at 4 °C with rabbit polyclonal anti-CNN3 antibodies (11509-1-AP; proteintech, Guangzhou, China), rabbit recombinant monoclonal anti-β-catenin antibody (A11932; ABclonal, Guangzhou, China), rabbit polyclonal anti-CNN3 (A1202; ABclonal, Guangzhou, China), anti-MMP7 (A0695; ABclonal, Guangzhou, China), anti-MMP10 (A3033; ABclonal, Guangzhou, China), anti-tubulin antibodies (ab6046; Abcam, Cambridge, UK), as a loading control.

Techniques: Transfection, Immunofluorescence, Expressing, Confocal Laser Scanning Microscopy, CCK-8 Assay, Staining, Western Blot, Control

CNN3 promoted VSMCs migration in β-catenin dependent manner. (A) Wound healing was performed to assess cells migration ability. (B) Cell invasiveness was determined using transwell assays. (C-D) Western blotting was performed to detect the expression levels of MMPs in VSMCs. Tubulin was used as a loading control. Data are given as the mean ± SD. All experiments were performed in triplicate. Scale bar = 100 μm∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.

Journal: Atherosclerosis Plus

Article Title: CNN3 promotes vascular smooth muscle cells proliferation and migration to deteriorate atherosclerosis by β-catenin signaling pathway

doi: 10.1016/j.athplu.2026.100560

Figure Lengend Snippet: CNN3 promoted VSMCs migration in β-catenin dependent manner. (A) Wound healing was performed to assess cells migration ability. (B) Cell invasiveness was determined using transwell assays. (C-D) Western blotting was performed to detect the expression levels of MMPs in VSMCs. Tubulin was used as a loading control. Data are given as the mean ± SD. All experiments were performed in triplicate. Scale bar = 100 μm∗ p < 0.05, ∗∗ p < 0.01, ∗∗∗ p < 0.001.

Article Snippet: The separated proteins were transferred to cellulose acetate membranes and then blocked with 5% BSA for 1 h at room temperature and incubated overnight at 4 °C with rabbit polyclonal anti-CNN3 antibodies (11509-1-AP; proteintech, Guangzhou, China), rabbit recombinant monoclonal anti-β-catenin antibody (A11932; ABclonal, Guangzhou, China), rabbit polyclonal anti-CNN3 (A1202; ABclonal, Guangzhou, China), anti-MMP7 (A0695; ABclonal, Guangzhou, China), anti-MMP10 (A3033; ABclonal, Guangzhou, China), anti-tubulin antibodies (ab6046; Abcam, Cambridge, UK), as a loading control.

Techniques: Migration, Western Blot, Expressing, Control

SPARC knockdown disrupts Wnt signaling and β-catenin nuclear translocation. ( A , B ) Western blot and RT-qPCR analysis showing reduced β-catenin and c-Myc protein and mRNA expression in HCECs following SPARC knockdown ( n = 5 independent experiments per group). ( C , D ) Western blot and RT-qPCR analysis of β-catenin protein and mRNA expression in corneal epithelial cells from WT and Sparc −/− mice at the indicated postinjury time points ( n = 3 independent pooled biological replicates per group). ( E , F ) Immunofluorescence staining of β-catenin ( red ) and DAPI ( blue ) in HCECs after SPARC knockdown ( n = 5 independent experiments per group). ( G ) Immunofluorescence images and quantification of β-catenin ( green ) in corneal sections from WT and Sparc −/− mice at different postinjury time points; nuclei were counterstained with DAPI ( blue ) ( n = 5 mice per group). ( H , I ) Scratch-wound assay and quantification of wound closure in HCECs after β-catenin knockdown with or without exogenous SPARC supplementation (the knockdown efficiency of β-catenin in HCECs is shown in B; n = 5 independent experiments per group). Scale bars are indicated in the images. Data are presented as mean ± SD. * P < 0.05, *** P < 0.001, **** P < 0.0001.

Journal: Investigative Ophthalmology & Visual Science

Article Title: SPARC Promotes Corneal Epithelial Wound Healing Through β-catenin Nuclear Translocation and c-Met Activation

doi: 10.1167/iovs.67.10.23

Figure Lengend Snippet: SPARC knockdown disrupts Wnt signaling and β-catenin nuclear translocation. ( A , B ) Western blot and RT-qPCR analysis showing reduced β-catenin and c-Myc protein and mRNA expression in HCECs following SPARC knockdown ( n = 5 independent experiments per group). ( C , D ) Western blot and RT-qPCR analysis of β-catenin protein and mRNA expression in corneal epithelial cells from WT and Sparc −/− mice at the indicated postinjury time points ( n = 3 independent pooled biological replicates per group). ( E , F ) Immunofluorescence staining of β-catenin ( red ) and DAPI ( blue ) in HCECs after SPARC knockdown ( n = 5 independent experiments per group). ( G ) Immunofluorescence images and quantification of β-catenin ( green ) in corneal sections from WT and Sparc −/− mice at different postinjury time points; nuclei were counterstained with DAPI ( blue ) ( n = 5 mice per group). ( H , I ) Scratch-wound assay and quantification of wound closure in HCECs after β-catenin knockdown with or without exogenous SPARC supplementation (the knockdown efficiency of β-catenin in HCECs is shown in B; n = 5 independent experiments per group). Scale bars are indicated in the images. Data are presented as mean ± SD. * P < 0.05, *** P < 0.001, **** P < 0.0001.

Article Snippet: Protein extracts from mouse corneal epithelial tissues were incubated with a β-catenin primary antibody (1:500, A19657; ABclonal) or normal rabbit IgG (1:100, ab172730; Abcam) overnight at 4°C.

Techniques: Knockdown, Translocation Assay, Western Blot, Quantitative RT-PCR, Expressing, Immunofluorescence, Staining, Scratch Wound Assay Assay

β-Catenin nuclear translocation blockade impairs Met transcription. ( A , B ) Western blot and RT-qPCR analysis showing reduced Met protein and mRNA expression in HCECs following β-catenin knockdown ( n = 5 independent experiments per group). ( C , D ) Immunofluorescence staining of p-Met ( green ) and DAPI ( blue ) in HCECs transfected with β-catenin siRNA ( n = 5 independent experiments per group). ( E ) Immunofluorescence staining of EdU ( green ) and DAPI ( blue ) in regenerating corneal epithelium from WT and β-catenin siRNA-treated mice at day 1 postinjury (the knockdown efficiency of β-catenin in C57BL/6 mice is shown in D; n = 5 mice per group). ( F ) Co-immunoprecipitation analysis showing β-catenin–c-Met interactions in HCECs from control and SPARC-knockdown groups ( n = 5 independent experiments per group). Scale bars are indicated in the images. Data are presented as mean ± SD. * P < 0.05, *** P < 0.001, **** P < 0.0001.

Journal: Investigative Ophthalmology & Visual Science

Article Title: SPARC Promotes Corneal Epithelial Wound Healing Through β-catenin Nuclear Translocation and c-Met Activation

doi: 10.1167/iovs.67.10.23

Figure Lengend Snippet: β-Catenin nuclear translocation blockade impairs Met transcription. ( A , B ) Western blot and RT-qPCR analysis showing reduced Met protein and mRNA expression in HCECs following β-catenin knockdown ( n = 5 independent experiments per group). ( C , D ) Immunofluorescence staining of p-Met ( green ) and DAPI ( blue ) in HCECs transfected with β-catenin siRNA ( n = 5 independent experiments per group). ( E ) Immunofluorescence staining of EdU ( green ) and DAPI ( blue ) in regenerating corneal epithelium from WT and β-catenin siRNA-treated mice at day 1 postinjury (the knockdown efficiency of β-catenin in C57BL/6 mice is shown in D; n = 5 mice per group). ( F ) Co-immunoprecipitation analysis showing β-catenin–c-Met interactions in HCECs from control and SPARC-knockdown groups ( n = 5 independent experiments per group). Scale bars are indicated in the images. Data are presented as mean ± SD. * P < 0.05, *** P < 0.001, **** P < 0.0001.

Article Snippet: Protein extracts from mouse corneal epithelial tissues were incubated with a β-catenin primary antibody (1:500, A19657; ABclonal) or normal rabbit IgG (1:100, ab172730; Abcam) overnight at 4°C.

Techniques: Translocation Assay, Western Blot, Quantitative RT-PCR, Expressing, Knockdown, Immunofluorescence, Staining, Transfection, Immunoprecipitation, Control