mmp 2 Santa Cruz Biotechnology Search Results


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  • 88
    Santa Cruz Biotechnology mmp 2 santa cruz
    Immunostain for <t>MMP-2</t> antibody (DAB, ×200) of infected untreated liver sections of mice killed 10 (a) and 18 (b) weeks PI showing marked positively stained hepatocytes and granulomas (arrows) . Sections taken from livers of mice treated with PZQ (500 mg/kg/day for 2 days) showing moderate (a) and mild (b) positively stained hepatocytes, endothelial cells lining sinusoids and granuloma cells (arrows). Sections taken from livers of mice treated with silymarin (750 mg/kg/day, 5 days/week for 6 weeks) showing mild (a) and moderate (b) positively stained hepatocytes, endothelial cells lining sinusoids and granuloma cells (arrows). Sections taken from livers of mice treated with PZQ plus silymarin showing scattered positively stained hepatocytes, weak positively stained endothelial cells lining sinusoids and granuloma cells (a; arrows) and mild positively stained hepatocytes, weak positively stained endothelial cells lining sinusoids and granuloma cells (b; arrows).
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    Santa Cruz Biotechnology anti mmp 2
    Curcumin retards activation of β-catenin/Slug pathway in breast cancer stem cells, thereby restoring E-cadherin. (A) β-catenin-associated E-cadherin was assayed by co-immunoprecipitation from cell lysates of MCF-7-derived 2° mammospheres with or without curcumin treatment using specific antibodies (left panel) or with normal human immunoglobulin G (IgG) as a negative control (right panel). To ensure comparable protein loading, 20% of supernatant from immunoprecipitation (IP) sample was subjected to determination of α-actin by Western blotting. (B) Western blotting was conducted to study the levels of total β-catenin and nuclear β-catenin in 2° mammospheres in presence or absence of curcumin exposure. (C) The relative nuclear expression of β-catenin in 2° mammospheres with or without curcumin treatment was visualized by immunofluorescence. (D, E) Under similar conditions, Western blotting was performed to study the expression levels of β-catenin target genes Cyclin-D1, c-Myc, Slug, Snail, Vimentin, <t>MMP-2</t> and MMP-9 in curcumin treated/untreated 2° mammospheres. (F) Protein expression of E-cadherin in 2° mammospheres with or without curcumin or Slug-cDNA (or both) were determined by Western blotting (left panel). The efficiency of transfection was determined by Western blot analysis (right panel). (G) Graphical quantifications of cell adhesion, spreading, three-dimensional (3D) invasion, and migration assays of MCF-7-derived 2° mammospheres with or without curcumin and Slug-cDNA treatment/transfection. (H) Transwell migration assay was performed under similar experimental conditions in T47D-derived 2° mammospheres. α-Actin/histone H1/glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was used as an internal loading control. Data are presented as mean ± standard error of mean or representative of three independent experiments. Cont, control; Cur, curcumin.
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    92
    Santa Cruz Biotechnology matrix metalloproteinase mmp 2
    Left : Representative renal trichrome staining (left, ×20) and quantification in the outer and inner renal cortex. Right: protein expression and quantification of transforming growth factor (TGF)-β, <t>matrix-metalloproteinase</t> <t>(MMP)-2</t> and tissue-inhibitor of metalloproteinase (TIMP)-1 in normal, atherosclerotic renal artery stenosis (ARAS), and ARAS kidneys treated with endothelial progenitor cells (ARAS+EPC). EPC administration decreased renal TGF-β improved MMP-2, and attenuated renal fibrosis. *p
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    86
    Santa Cruz Biotechnology polyclonal mmp 2
    Left : Representative renal trichrome staining (left, ×20) and quantification in the outer and inner renal cortex. Right: protein expression and quantification of transforming growth factor (TGF)-β, <t>matrix-metalloproteinase</t> <t>(MMP)-2</t> and tissue-inhibitor of metalloproteinase (TIMP)-1 in normal, atherosclerotic renal artery stenosis (ARAS), and ARAS kidneys treated with endothelial progenitor cells (ARAS+EPC). EPC administration decreased renal TGF-β improved MMP-2, and attenuated renal fibrosis. *p
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    92
    Santa Cruz Biotechnology timp 2
    Expression and localisation of MMP-2 protein during follicular stage in normal and miniature pigs. Tissue sections of normal and miniature pig follicles were immunostained with the MMP-2 antibody and counterstained with H E. Black arrows indicate MMP-2-expressing cells. a MMP-2, b <t>TIMP-2,</t> c MMP-9, d TIMP-3. NPO normal pig ovary, MPO miniature pig ovary, TE theca externa cells, TI theca interna cells, GC granulosa cells, TL theca lutein cells, GL granulosa lutein cells. Original magnification ×400 (inset ×100)
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    Santa Cruz Biotechnology si mmp 2
    Sp1 is implicated in Bclw-induced invasion upstream of <t>MMP-2.</t> (A) The indicated U251 cell transfectants were incubated in a serum-free medium in the presence or absence of the Sp1 inhibitor mithramycin A (MMA; 10 μmol/L) for 1 or 24 h. Expression levels and activities of Sp1 and MMP-2 were compared using Western blotting and zymography assay using β-actin as the loading control or Ponceau S staining, respectively. The invasive potential of treated cells was compared. * p
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    Santa Cruz Biotechnology silencing mmp 2
    <t>MMP-2</t> is a direct target of miR-20b. A. The putative binding site of miR-20b and MMP-2 is shown. B. Luciferase assay of HEK293 cells co-transfected with firefly luciferase constructs containing the MMP-2 wild-type or mutated 3’-UTRs and miR-20b mimics, mimics NC, miR-20b inhibitor or inhibitor NC, as indicated (n = 3). C. The expressions of MMP-2 protein after transfection with miR-20b mimic or miR-20b inhibitor were measured by Western Blot. Data represent the mean ± SD of three independent experiments. ** P
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    Santa Cruz Biotechnology reagents antibody against mmp 2
    <t>MMP-2</t> is a direct target of miR-20b. A. The putative binding site of miR-20b and MMP-2 is shown. B. Luciferase assay of HEK293 cells co-transfected with firefly luciferase constructs containing the MMP-2 wild-type or mutated 3’-UTRs and miR-20b mimics, mimics NC, miR-20b inhibitor or inhibitor NC, as indicated (n = 3). C. The expressions of MMP-2 protein after transfection with miR-20b mimic or miR-20b inhibitor were measured by Western Blot. Data represent the mean ± SD of three independent experiments. ** P
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    Santa Cruz Biotechnology rabbit anti mmp 2
    Cardiac ischemia in rabbits reduces mature ERG protein expression and increases the expression of calpain, matriptase-2, and <t>MMP-2.</t> A and B , Western blots of ventricular tissue from control ( Ctrl ) or ischemic ( Isc ) rabbit hearts showing that 24-h ischemia
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    Santa Cruz Biotechnology polyclonal rabbit anti mmp 2
    Cardiac ischemia in rabbits reduces mature ERG protein expression and increases the expression of calpain, matriptase-2, and <t>MMP-2.</t> A and B , Western blots of ventricular tissue from control ( Ctrl ) or ischemic ( Isc ) rabbit hearts showing that 24-h ischemia
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    Santa Cruz Biotechnology human mmp 2
    Cardiac ischemia in rabbits reduces mature ERG protein expression and increases the expression of calpain, matriptase-2, and <t>MMP-2.</t> A and B , Western blots of ventricular tissue from control ( Ctrl ) or ischemic ( Isc ) rabbit hearts showing that 24-h ischemia
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    Santa Cruz Biotechnology rabbit mmp 2
    Cardiac ischemia in rabbits reduces mature ERG protein expression and increases the expression of calpain, matriptase-2, and <t>MMP-2.</t> A and B , Western blots of ventricular tissue from control ( Ctrl ) or ischemic ( Isc ) rabbit hearts showing that 24-h ischemia
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    91
    Santa Cruz Biotechnology antibodies against mmp 2
    GSP inhibits the migration and invasion of SCC12 cells by reducing <t>MMP-2/9</t> expression and activity. (A) The effect of GSP on the motility of SCC12 cells was assessed using wound-healing assays. Images were captured of migrating cells in the denuded zone (magnification, ×100). (B) The effect of GSP on the invasion of SCC12 cells. Cells were treated with various concentrations of GSP for 24 h and a cell invasion assay was performed. Images were captured of the invaded cells (magnification, ×200). (C) The effect of GSP on the activities and protein expression of MMP-2/9. (C-a) Supernatants of GSP-treated SCC12 cells were loaded into 10% gelatin-containing gel, resolved by electrophoresis and stained with Coomassie blue. (C-b) Total cell lysates were analyzed by SDS-PAGE, followed by probing with anti-human MMP-2 antibody. β-actin was used as a control for protein loading. MMP, matrix metalloproteinase; GSP, grape seed procyanidins; CTL, control.
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    Santa Cruz Biotechnology pabs against mmp 2
    GSP inhibits the migration and invasion of SCC12 cells by reducing <t>MMP-2/9</t> expression and activity. (A) The effect of GSP on the motility of SCC12 cells was assessed using wound-healing assays. Images were captured of migrating cells in the denuded zone (magnification, ×100). (B) The effect of GSP on the invasion of SCC12 cells. Cells were treated with various concentrations of GSP for 24 h and a cell invasion assay was performed. Images were captured of the invaded cells (magnification, ×200). (C) The effect of GSP on the activities and protein expression of MMP-2/9. (C-a) Supernatants of GSP-treated SCC12 cells were loaded into 10% gelatin-containing gel, resolved by electrophoresis and stained with Coomassie blue. (C-b) Total cell lysates were analyzed by SDS-PAGE, followed by probing with anti-human MMP-2 antibody. β-actin was used as a control for protein loading. MMP, matrix metalloproteinase; GSP, grape seed procyanidins; CTL, control.
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    Santa Cruz Biotechnology polyclonal anti mmp 2
    GSP inhibits the migration and invasion of SCC12 cells by reducing <t>MMP-2/9</t> expression and activity. (A) The effect of GSP on the motility of SCC12 cells was assessed using wound-healing assays. Images were captured of migrating cells in the denuded zone (magnification, ×100). (B) The effect of GSP on the invasion of SCC12 cells. Cells were treated with various concentrations of GSP for 24 h and a cell invasion assay was performed. Images were captured of the invaded cells (magnification, ×200). (C) The effect of GSP on the activities and protein expression of MMP-2/9. (C-a) Supernatants of GSP-treated SCC12 cells were loaded into 10% gelatin-containing gel, resolved by electrophoresis and stained with Coomassie blue. (C-b) Total cell lysates were analyzed by SDS-PAGE, followed by probing with anti-human MMP-2 antibody. β-actin was used as a control for protein loading. MMP, matrix metalloproteinase; GSP, grape seed procyanidins; CTL, control.
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    Santa Cruz Biotechnology rabbit monoclonal antibodies against mmp 2
    Expression of <t>MMP-2</t> and MMP-9 protein following treatment. MMP, matrix metalloproteinase; US, ultrasound group; US + MB, ultrasound in combination with microbubbles group.
    Rabbit Monoclonal Antibodies Against Mmp 2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology mouse monoclonal antibody against mmp 2
    Graphical representation of mRNA expression of a <t>MMP-2</t> b MMP-9 c HOXA-11 d HOXA-10 in the endometrium of women with endometriosis and controls. e Endometrial expression of MMP-2, MMP-9, HOXA-11, HOXA-10 and β-actin in women with endometriosis
    Mouse Monoclonal Antibody Against Mmp 2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 85/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Santa Cruz Biotechnology anti human mmp 2
    Graphical representation of mRNA expression of a <t>MMP-2</t> b MMP-9 c HOXA-11 d HOXA-10 in the endometrium of women with endometriosis and controls. e Endometrial expression of MMP-2, MMP-9, HOXA-11, HOXA-10 and β-actin in women with endometriosis
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    Image Search Results


    Immunostain for MMP-2 antibody (DAB, ×200) of infected untreated liver sections of mice killed 10 (a) and 18 (b) weeks PI showing marked positively stained hepatocytes and granulomas (arrows) . Sections taken from livers of mice treated with PZQ (500 mg/kg/day for 2 days) showing moderate (a) and mild (b) positively stained hepatocytes, endothelial cells lining sinusoids and granuloma cells (arrows). Sections taken from livers of mice treated with silymarin (750 mg/kg/day, 5 days/week for 6 weeks) showing mild (a) and moderate (b) positively stained hepatocytes, endothelial cells lining sinusoids and granuloma cells (arrows). Sections taken from livers of mice treated with PZQ plus silymarin showing scattered positively stained hepatocytes, weak positively stained endothelial cells lining sinusoids and granuloma cells (a; arrows) and mild positively stained hepatocytes, weak positively stained endothelial cells lining sinusoids and granuloma cells (b; arrows).

    Journal: Parasites & Vectors

    Article Title: Anti-inflammatory/anti-fibrotic effects of the hepatoprotective silymarin and the schistosomicide praziquantel against Schistosoma mansoni-induced liver fibrosis

    doi: 10.1186/1756-3305-5-9

    Figure Lengend Snippet: Immunostain for MMP-2 antibody (DAB, ×200) of infected untreated liver sections of mice killed 10 (a) and 18 (b) weeks PI showing marked positively stained hepatocytes and granulomas (arrows) . Sections taken from livers of mice treated with PZQ (500 mg/kg/day for 2 days) showing moderate (a) and mild (b) positively stained hepatocytes, endothelial cells lining sinusoids and granuloma cells (arrows). Sections taken from livers of mice treated with silymarin (750 mg/kg/day, 5 days/week for 6 weeks) showing mild (a) and moderate (b) positively stained hepatocytes, endothelial cells lining sinusoids and granuloma cells (arrows). Sections taken from livers of mice treated with PZQ plus silymarin showing scattered positively stained hepatocytes, weak positively stained endothelial cells lining sinusoids and granuloma cells (a; arrows) and mild positively stained hepatocytes, weak positively stained endothelial cells lining sinusoids and granuloma cells (b; arrows).

    Article Snippet: Liver fibrosis markers Infection of mice with S. mansoni caused pronounced elevations in both serum TGF-β1 (P < 0.001) and MMP-2 (P < 0.01, P < 0.001) levels, 10 and 18 weeks PI respectively, when compared to their corresponding uninfected untreated groups.

    Techniques: Infection, Mouse Assay, Staining

    Expression profiles of OPN and other oncogenic molecules in the human breast tumour specimens of different grades. (A) typical photographs (haematoxylin and eosin stained) of human breast tumour specimens of different grades (panel I). Breast tumour specimens were stained with rabbit anti-OPN antibody followed by Cy-3-conjugated anti-rabbit IgG (red). Note that the expression of OPN is shown by arrows (panel II). Status of total tyrosine and serine phosphorylations were determined by immunohistochemistry by using anti-mouse phosphotyrosine or phosphoserine antibody followed by FITC-conjugated anti-mouse IgG (green) (panels III and IV). Nuclear localization of NF-κβ, p65 were visualized in grade II and III specimens and indicated by white arrows whereas cytoplasmic localization of p65 was observed in normal and grade I specimens and indicated by red arrows (panel V). The levels of uPA (panel VI), MT1-MMP (panel VII), MMP-9 (panel VIII) and MMP-2 (panel IX) in different grades of breast tumour specimens were detected by immunohistochemical studies using their specific antibodies. The neovascularization was visualized by using anti-vWF antibody (panel X). NF-κβ, p65, MT1-MMP and MMP-2 were stained with FITC-conjugated anti-mouse IgG (green), whereas uPA, MMP-9 and vWF were stained with Cy3-conjugated anti-rabbit IgG (red). Nuclei were stained with DAPI (blue). Note that the expression of all these molecules and neovascularization are significantly higher in grade II and grade III specimens. (B) The expression profiles of OPN, uPA, MMP-2, MMP-9 and vWF in various grades of breast tumour specimens were quantified using Image Pro Plus software (Nikon) and represented graphically (n = 10/grade). The expression profile of these molecules were normalized with respect to DAPI. (C and D) The NF-κβ and AP-1 DNA-binding in different grades were analysed by EMSA. Note that significantly enhanced DNA-binding was observed in higher grades of tumour specimens.

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Down-regulation of osteopontin attenuates breast tumour progression in vivo

    doi: 10.1111/j.1582-4934.2008.00263.x

    Figure Lengend Snippet: Expression profiles of OPN and other oncogenic molecules in the human breast tumour specimens of different grades. (A) typical photographs (haematoxylin and eosin stained) of human breast tumour specimens of different grades (panel I). Breast tumour specimens were stained with rabbit anti-OPN antibody followed by Cy-3-conjugated anti-rabbit IgG (red). Note that the expression of OPN is shown by arrows (panel II). Status of total tyrosine and serine phosphorylations were determined by immunohistochemistry by using anti-mouse phosphotyrosine or phosphoserine antibody followed by FITC-conjugated anti-mouse IgG (green) (panels III and IV). Nuclear localization of NF-κβ, p65 were visualized in grade II and III specimens and indicated by white arrows whereas cytoplasmic localization of p65 was observed in normal and grade I specimens and indicated by red arrows (panel V). The levels of uPA (panel VI), MT1-MMP (panel VII), MMP-9 (panel VIII) and MMP-2 (panel IX) in different grades of breast tumour specimens were detected by immunohistochemical studies using their specific antibodies. The neovascularization was visualized by using anti-vWF antibody (panel X). NF-κβ, p65, MT1-MMP and MMP-2 were stained with FITC-conjugated anti-mouse IgG (green), whereas uPA, MMP-9 and vWF were stained with Cy3-conjugated anti-rabbit IgG (red). Nuclei were stained with DAPI (blue). Note that the expression of all these molecules and neovascularization are significantly higher in grade II and grade III specimens. (B) The expression profiles of OPN, uPA, MMP-2, MMP-9 and vWF in various grades of breast tumour specimens were quantified using Image Pro Plus software (Nikon) and represented graphically (n = 10/grade). The expression profile of these molecules were normalized with respect to DAPI. (C and D) The NF-κβ and AP-1 DNA-binding in different grades were analysed by EMSA. Note that significantly enhanced DNA-binding was observed in higher grades of tumour specimens.

    Article Snippet: Rabbit anti-p65 (NF-κβ), anti-uPA, anti-MMP-9 antibodies and mouse anti-MMP-2, anti-p-Akt (Ser-473), anti-p-ERK (Tyr-204) antibodies, goat anti-actin antibody and siRNA transfection reagent were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Expressing, Staining, Immunohistochemistry, Software, Binding Assay

    Silencing of OPN significantly down-regulates pristane-induced mammary carcinogenesis in nude mice. (A) Haematoxylin and eosin staining showed the mammary carcinogenesis induced by pristane. Photographs were taken under 10x and 60x magnifications. Normal mouse mammary fat pad (MFP) is shown as control (panels I and II). Vascularization is indicated by arrows (panel II). Expression profile of OPN was detected by immunoflu-orescence. Significantly higher level of OPN was observed in pristane-induced tumours whereas silencing of OPN down-regulates tumour-derived OPN expression (panel III). Expressions of MMP-9 (IV), MMP-2 (V) and MT1-MMP (VI) were determined by immunohistochemical analyses using their specific antibodies. (B) Expression of uPA, cellular localization of NF-κβ and total phosphorylations of serine and tyrosine were analysed by immunohistochemical studies (panels I—IV). Enhanced phosphorylations of ERK and Akt were observed in pristane-induced tumours but not in OPNi-injected tumours and normal tissues (panels V and VI). Tumour sections were stained with anti-vWF antibody to visualize the angiogenesis in these tumours (panel VII). vWF positive areas are indicated by arrows. (C) NF-κβ (upper panel) and AP-1 (lower panel)-DNA binding in tumour tissues were performed by EMSA. Six mice were used in each set of experiments.

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Down-regulation of osteopontin attenuates breast tumour progression in vivo

    doi: 10.1111/j.1582-4934.2008.00263.x

    Figure Lengend Snippet: Silencing of OPN significantly down-regulates pristane-induced mammary carcinogenesis in nude mice. (A) Haematoxylin and eosin staining showed the mammary carcinogenesis induced by pristane. Photographs were taken under 10x and 60x magnifications. Normal mouse mammary fat pad (MFP) is shown as control (panels I and II). Vascularization is indicated by arrows (panel II). Expression profile of OPN was detected by immunoflu-orescence. Significantly higher level of OPN was observed in pristane-induced tumours whereas silencing of OPN down-regulates tumour-derived OPN expression (panel III). Expressions of MMP-9 (IV), MMP-2 (V) and MT1-MMP (VI) were determined by immunohistochemical analyses using their specific antibodies. (B) Expression of uPA, cellular localization of NF-κβ and total phosphorylations of serine and tyrosine were analysed by immunohistochemical studies (panels I—IV). Enhanced phosphorylations of ERK and Akt were observed in pristane-induced tumours but not in OPNi-injected tumours and normal tissues (panels V and VI). Tumour sections were stained with anti-vWF antibody to visualize the angiogenesis in these tumours (panel VII). vWF positive areas are indicated by arrows. (C) NF-κβ (upper panel) and AP-1 (lower panel)-DNA binding in tumour tissues were performed by EMSA. Six mice were used in each set of experiments.

    Article Snippet: Rabbit anti-p65 (NF-κβ), anti-uPA, anti-MMP-9 antibodies and mouse anti-MMP-2, anti-p-Akt (Ser-473), anti-p-ERK (Tyr-204) antibodies, goat anti-actin antibody and siRNA transfection reagent were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Mouse Assay, Staining, Expressing, Derivative Assay, Immunohistochemistry, Injection, Binding Assay

    (A and B) MDA-MB-231 cells were transfected with various OPN-specific siRNA (OPNi, see Table 1 ) and OPN expression was detected by Western blot. Actin was used as loading control. (C) Cells were transfected with OPNi (OPNM). The levels of pERK, pAkt, uPA, MMP-9 and MMP-2 in cell lysates were analysed using their specific antibodies. Non-phospho ERK, Akt and actin were used as loading controls. Fold changes were calculated. (D) DNA binding of NF-κβ (panel I) and AP-1 (panel II) were performed from the nuclear extract obtained from control or OPNi transfected MDA-MB-231 cells. (E) Cells were transfected with OPNi or Coni. Wounds of constant diameter were made and wound assay was performed. Photographs were taken at 0 and at 12 hrs under Nikon microscope. The data represent three experiments exhibiting similar results.

    Journal: Journal of Cellular and Molecular Medicine

    Article Title: Down-regulation of osteopontin attenuates breast tumour progression in vivo

    doi: 10.1111/j.1582-4934.2008.00263.x

    Figure Lengend Snippet: (A and B) MDA-MB-231 cells were transfected with various OPN-specific siRNA (OPNi, see Table 1 ) and OPN expression was detected by Western blot. Actin was used as loading control. (C) Cells were transfected with OPNi (OPNM). The levels of pERK, pAkt, uPA, MMP-9 and MMP-2 in cell lysates were analysed using their specific antibodies. Non-phospho ERK, Akt and actin were used as loading controls. Fold changes were calculated. (D) DNA binding of NF-κβ (panel I) and AP-1 (panel II) were performed from the nuclear extract obtained from control or OPNi transfected MDA-MB-231 cells. (E) Cells were transfected with OPNi or Coni. Wounds of constant diameter were made and wound assay was performed. Photographs were taken at 0 and at 12 hrs under Nikon microscope. The data represent three experiments exhibiting similar results.

    Article Snippet: Rabbit anti-p65 (NF-κβ), anti-uPA, anti-MMP-9 antibodies and mouse anti-MMP-2, anti-p-Akt (Ser-473), anti-p-ERK (Tyr-204) antibodies, goat anti-actin antibody and siRNA transfection reagent were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Multiple Displacement Amplification, Transfection, Expressing, Western Blot, Binding Assay, Microscopy

    Curcumin retards activation of β-catenin/Slug pathway in breast cancer stem cells, thereby restoring E-cadherin. (A) β-catenin-associated E-cadherin was assayed by co-immunoprecipitation from cell lysates of MCF-7-derived 2° mammospheres with or without curcumin treatment using specific antibodies (left panel) or with normal human immunoglobulin G (IgG) as a negative control (right panel). To ensure comparable protein loading, 20% of supernatant from immunoprecipitation (IP) sample was subjected to determination of α-actin by Western blotting. (B) Western blotting was conducted to study the levels of total β-catenin and nuclear β-catenin in 2° mammospheres in presence or absence of curcumin exposure. (C) The relative nuclear expression of β-catenin in 2° mammospheres with or without curcumin treatment was visualized by immunofluorescence. (D, E) Under similar conditions, Western blotting was performed to study the expression levels of β-catenin target genes Cyclin-D1, c-Myc, Slug, Snail, Vimentin, MMP-2 and MMP-9 in curcumin treated/untreated 2° mammospheres. (F) Protein expression of E-cadherin in 2° mammospheres with or without curcumin or Slug-cDNA (or both) were determined by Western blotting (left panel). The efficiency of transfection was determined by Western blot analysis (right panel). (G) Graphical quantifications of cell adhesion, spreading, three-dimensional (3D) invasion, and migration assays of MCF-7-derived 2° mammospheres with or without curcumin and Slug-cDNA treatment/transfection. (H) Transwell migration assay was performed under similar experimental conditions in T47D-derived 2° mammospheres. α-Actin/histone H1/glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was used as an internal loading control. Data are presented as mean ± standard error of mean or representative of three independent experiments. Cont, control; Cur, curcumin.

    Journal: Stem Cell Research & Therapy

    Article Title: Curcumin inhibits breast cancer stem cell migration by amplifying the E-cadherin/β-catenin negative feedback loop

    doi: 10.1186/scrt506

    Figure Lengend Snippet: Curcumin retards activation of β-catenin/Slug pathway in breast cancer stem cells, thereby restoring E-cadherin. (A) β-catenin-associated E-cadherin was assayed by co-immunoprecipitation from cell lysates of MCF-7-derived 2° mammospheres with or without curcumin treatment using specific antibodies (left panel) or with normal human immunoglobulin G (IgG) as a negative control (right panel). To ensure comparable protein loading, 20% of supernatant from immunoprecipitation (IP) sample was subjected to determination of α-actin by Western blotting. (B) Western blotting was conducted to study the levels of total β-catenin and nuclear β-catenin in 2° mammospheres in presence or absence of curcumin exposure. (C) The relative nuclear expression of β-catenin in 2° mammospheres with or without curcumin treatment was visualized by immunofluorescence. (D, E) Under similar conditions, Western blotting was performed to study the expression levels of β-catenin target genes Cyclin-D1, c-Myc, Slug, Snail, Vimentin, MMP-2 and MMP-9 in curcumin treated/untreated 2° mammospheres. (F) Protein expression of E-cadherin in 2° mammospheres with or without curcumin or Slug-cDNA (or both) were determined by Western blotting (left panel). The efficiency of transfection was determined by Western blot analysis (right panel). (G) Graphical quantifications of cell adhesion, spreading, three-dimensional (3D) invasion, and migration assays of MCF-7-derived 2° mammospheres with or without curcumin and Slug-cDNA treatment/transfection. (H) Transwell migration assay was performed under similar experimental conditions in T47D-derived 2° mammospheres. α-Actin/histone H1/glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was used as an internal loading control. Data are presented as mean ± standard error of mean or representative of three independent experiments. Cont, control; Cur, curcumin.

    Article Snippet: For direct Western blot analysis, the cell lysates or the particular fractions were separated by SDS-PAGE, transferred to polyvinylidene difluoride membrane (Millipore, Darmstadt, Germany), and probed with specific antibodies like anti-E-cadherin, anti-β-catenin, anti-histone H1, anti-cyclin-D1, anti-c-myc, anti-slug, anti-vimentin, anti-MMP-2, anti-MMP-9, anti-twist, anti-Snail, and anti-α-Actin (Santa Cruz Biotechnology, Inc.).

    Techniques: Activation Assay, Immunoprecipitation, Derivative Assay, Negative Control, Western Blot, Expressing, Immunofluorescence, Transfection, Migration, Transwell Migration Assay

    Left : Representative renal trichrome staining (left, ×20) and quantification in the outer and inner renal cortex. Right: protein expression and quantification of transforming growth factor (TGF)-β, matrix-metalloproteinase (MMP)-2 and tissue-inhibitor of metalloproteinase (TIMP)-1 in normal, atherosclerotic renal artery stenosis (ARAS), and ARAS kidneys treated with endothelial progenitor cells (ARAS+EPC). EPC administration decreased renal TGF-β improved MMP-2, and attenuated renal fibrosis. *p

    Journal: Stem cells (Dayton, Ohio)

    Article Title: ENDOTHELIAL PROGENITOR CELLS HOMING AND RENAL REPAIR IN EXPERIMENTAL RENOVASCULAR DISEASE

    doi: 10.1002/stem.426

    Figure Lengend Snippet: Left : Representative renal trichrome staining (left, ×20) and quantification in the outer and inner renal cortex. Right: protein expression and quantification of transforming growth factor (TGF)-β, matrix-metalloproteinase (MMP)-2 and tissue-inhibitor of metalloproteinase (TIMP)-1 in normal, atherosclerotic renal artery stenosis (ARAS), and ARAS kidneys treated with endothelial progenitor cells (ARAS+EPC). EPC administration decreased renal TGF-β improved MMP-2, and attenuated renal fibrosis. *p

    Article Snippet: Western blotting: standard blotting protocols were followed, as previously described , using specific antibodies against vascular endothelial growth factor (VEGF), angiopoietin-1, transforming growth factor (TGF)-β, matrix-metalloproteinase (MMP)-2, tissue-inhibitor of MMP (TIMP)-1, the NAD(P)H oxidase subunit p47phox, the VEGF receptor KDR (Santa Cruz, CA, 1:200 for all), xanthine oxidase (1:10000, non-reducing, no-milk condition, Chemicon International), SDF-1, angiopoietin-1 (1:1000, Abcam), EPO and EPO-R (Santa Cruz, CA, 1:200).

    Techniques: Staining, Expressing

    Expression and localisation of MMP-2 protein during follicular stage in normal and miniature pigs. Tissue sections of normal and miniature pig follicles were immunostained with the MMP-2 antibody and counterstained with H E. Black arrows indicate MMP-2-expressing cells. a MMP-2, b TIMP-2, c MMP-9, d TIMP-3. NPO normal pig ovary, MPO miniature pig ovary, TE theca externa cells, TI theca interna cells, GC granulosa cells, TL theca lutein cells, GL granulosa lutein cells. Original magnification ×400 (inset ×100)

    Journal: Biotechnology Letters

    Article Title: Matrix metalloproteinases are important for follicular development in normal and miniature pigs

    doi: 10.1007/s10529-014-1474-9

    Figure Lengend Snippet: Expression and localisation of MMP-2 protein during follicular stage in normal and miniature pigs. Tissue sections of normal and miniature pig follicles were immunostained with the MMP-2 antibody and counterstained with H E. Black arrows indicate MMP-2-expressing cells. a MMP-2, b TIMP-2, c MMP-9, d TIMP-3. NPO normal pig ovary, MPO miniature pig ovary, TE theca externa cells, TI theca interna cells, GC granulosa cells, TL theca lutein cells, GL granulosa lutein cells. Original magnification ×400 (inset ×100)

    Article Snippet: Decreased expression of TIMP-2 (MMP-2 inhibitor) and increased expression of TIMP-3 (MMP-9 inhibitor) observed in miniature pigs lead to the inhibition of MMP-9 and enhancement of MMP-2 activity and have been shown to correlate with induction of ovulation and transformation of follicular cells into luteal cells (Ray and Stetler-Stevenson ), thus supporting our hypothesis.

    Techniques: Expressing

    MMP activity and TIMP expression in the ovaries of normal and miniature pigs. Zymography analysis of the MMP activity in the ovaries ( a ). TIMP-2 and TIMP-3 protein expression by western blot ( b ). Bar graphs ( right ) show quantification of the detected bands by densitometry ( c ). Data are presented as the mean ± SEM of three independent experiments; values normalised to those of β-actin (a house-keeping gene)

    Journal: Biotechnology Letters

    Article Title: Matrix metalloproteinases are important for follicular development in normal and miniature pigs

    doi: 10.1007/s10529-014-1474-9

    Figure Lengend Snippet: MMP activity and TIMP expression in the ovaries of normal and miniature pigs. Zymography analysis of the MMP activity in the ovaries ( a ). TIMP-2 and TIMP-3 protein expression by western blot ( b ). Bar graphs ( right ) show quantification of the detected bands by densitometry ( c ). Data are presented as the mean ± SEM of three independent experiments; values normalised to those of β-actin (a house-keeping gene)

    Article Snippet: Decreased expression of TIMP-2 (MMP-2 inhibitor) and increased expression of TIMP-3 (MMP-9 inhibitor) observed in miniature pigs lead to the inhibition of MMP-9 and enhancement of MMP-2 activity and have been shown to correlate with induction of ovulation and transformation of follicular cells into luteal cells (Ray and Stetler-Stevenson ), thus supporting our hypothesis.

    Techniques: Activity Assay, Expressing, Zymography, Western Blot

    mRNA expression of MMP-2, MMP-9, TIMP-2, and TIMP-3 in the ovaries of normal and miniature pigs. mRNA levels were assessed by real time RT-PCR. The data are presented as average fold changes (mean ± SD) of three independent experiments. * P

    Journal: Biotechnology Letters

    Article Title: Matrix metalloproteinases are important for follicular development in normal and miniature pigs

    doi: 10.1007/s10529-014-1474-9

    Figure Lengend Snippet: mRNA expression of MMP-2, MMP-9, TIMP-2, and TIMP-3 in the ovaries of normal and miniature pigs. mRNA levels were assessed by real time RT-PCR. The data are presented as average fold changes (mean ± SD) of three independent experiments. * P

    Article Snippet: Decreased expression of TIMP-2 (MMP-2 inhibitor) and increased expression of TIMP-3 (MMP-9 inhibitor) observed in miniature pigs lead to the inhibition of MMP-9 and enhancement of MMP-2 activity and have been shown to correlate with induction of ovulation and transformation of follicular cells into luteal cells (Ray and Stetler-Stevenson ), thus supporting our hypothesis.

    Techniques: Expressing, Quantitative RT-PCR

    Sp1 is implicated in Bclw-induced invasion upstream of MMP-2. (A) The indicated U251 cell transfectants were incubated in a serum-free medium in the presence or absence of the Sp1 inhibitor mithramycin A (MMA; 10 μmol/L) for 1 or 24 h. Expression levels and activities of Sp1 and MMP-2 were compared using Western blotting and zymography assay using β-actin as the loading control or Ponceau S staining, respectively. The invasive potential of treated cells was compared. * p

    Journal: Molecules and Cells

    Article Title: Specificity Protein 1 Expression Contributes to Bcl-w-Induced Aggressiveness in Glioblastoma Multiforme

    doi: 10.14348/molcells.2014.2161

    Figure Lengend Snippet: Sp1 is implicated in Bclw-induced invasion upstream of MMP-2. (A) The indicated U251 cell transfectants were incubated in a serum-free medium in the presence or absence of the Sp1 inhibitor mithramycin A (MMA; 10 μmol/L) for 1 or 24 h. Expression levels and activities of Sp1 and MMP-2 were compared using Western blotting and zymography assay using β-actin as the loading control or Ponceau S staining, respectively. The invasive potential of treated cells was compared. * p

    Article Snippet: Small interfering RNAs were purchased from as the following; silencer negative control siRNA, si-Bcl-w (Ambion, USA), si-Sp1 and si-MMP-2 (Santa Cruz Biotechnology, USA).

    Techniques: Incubation, Expressing, Western Blot, Zymography, Staining

    Activation of MMP-2 mediates Bcl-w-induced invasion. (A) The indicated U251 cell transfectants were incubated in serum-free medium in the presence or absence of aMMP-2 inhibitor (OA-Hy; 10 μmol/L) for 1 or 24 h. Expression levels of MMP-2 were compared using Western blotting. Invasion assays were performed using MMP-2 inhibitor-treated and untreated cells. ** p

    Journal: Molecules and Cells

    Article Title: Specificity Protein 1 Expression Contributes to Bcl-w-Induced Aggressiveness in Glioblastoma Multiforme

    doi: 10.14348/molcells.2014.2161

    Figure Lengend Snippet: Activation of MMP-2 mediates Bcl-w-induced invasion. (A) The indicated U251 cell transfectants were incubated in serum-free medium in the presence or absence of aMMP-2 inhibitor (OA-Hy; 10 μmol/L) for 1 or 24 h. Expression levels of MMP-2 were compared using Western blotting. Invasion assays were performed using MMP-2 inhibitor-treated and untreated cells. ** p

    Article Snippet: Small interfering RNAs were purchased from as the following; silencer negative control siRNA, si-Bcl-w (Ambion, USA), si-Sp1 and si-MMP-2 (Santa Cruz Biotechnology, USA).

    Techniques: Activation Assay, Incubation, Expressing, Western Blot

    Schematic diagram of the Bcl-w-induced signaling pathway by the activation of Sp1. Bcl-w enhanced the invasive potential of glioblastoma U251 cells by stimulating MMP-2 via increasing expression of the transcription factor Sp1 in the nucleus, and promoted neurosphere formation and glioma stem-like cell markers expression, Musashi, Nanog, Oct4 and Sox2. In conclusion, Bcl-w promotes the properties of GBM aggressiveness by activating Sp1.

    Journal: Molecules and Cells

    Article Title: Specificity Protein 1 Expression Contributes to Bcl-w-Induced Aggressiveness in Glioblastoma Multiforme

    doi: 10.14348/molcells.2014.2161

    Figure Lengend Snippet: Schematic diagram of the Bcl-w-induced signaling pathway by the activation of Sp1. Bcl-w enhanced the invasive potential of glioblastoma U251 cells by stimulating MMP-2 via increasing expression of the transcription factor Sp1 in the nucleus, and promoted neurosphere formation and glioma stem-like cell markers expression, Musashi, Nanog, Oct4 and Sox2. In conclusion, Bcl-w promotes the properties of GBM aggressiveness by activating Sp1.

    Article Snippet: Small interfering RNAs were purchased from as the following; silencer negative control siRNA, si-Bcl-w (Ambion, USA), si-Sp1 and si-MMP-2 (Santa Cruz Biotechnology, USA).

    Techniques: Activation Assay, Expressing

    MMP-2 is a direct target of miR-20b. A. The putative binding site of miR-20b and MMP-2 is shown. B. Luciferase assay of HEK293 cells co-transfected with firefly luciferase constructs containing the MMP-2 wild-type or mutated 3’-UTRs and miR-20b mimics, mimics NC, miR-20b inhibitor or inhibitor NC, as indicated (n = 3). C. The expressions of MMP-2 protein after transfection with miR-20b mimic or miR-20b inhibitor were measured by Western Blot. Data represent the mean ± SD of three independent experiments. ** P

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: MicroRNA-20b inhibits trophoblast cell migration and invasion by targeting MMP-2

    doi:

    Figure Lengend Snippet: MMP-2 is a direct target of miR-20b. A. The putative binding site of miR-20b and MMP-2 is shown. B. Luciferase assay of HEK293 cells co-transfected with firefly luciferase constructs containing the MMP-2 wild-type or mutated 3’-UTRs and miR-20b mimics, mimics NC, miR-20b inhibitor or inhibitor NC, as indicated (n = 3). C. The expressions of MMP-2 protein after transfection with miR-20b mimic or miR-20b inhibitor were measured by Western Blot. Data represent the mean ± SD of three independent experiments. ** P

    Article Snippet: MMP-2 overexpression plasmid (pcDNA-MMP-2) and MMP-2 siRNA for silencing MMP-2 were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Binding Assay, Luciferase, Transfection, Construct, Western Blot

    MMP-2 reversed the effect of miR-20b on cell invasion in HTR8/SVneo cells. HTR8/SVneo cells were co-transfected with si-MMP-2 and miR-20b inhibitor. A. Wound healing assay was performed to monitor cell migration after transfection with si-MMP-2 or miR-20b inhibitor. B. Transwell assay was performed to monitor cell invasiveness after transfection with si-MMP-2 or miR-20b inhibitor. C. Wound healing assay was performed to monitor cell migration after transfection with pcDNA-MMP-2 or miR-20b mimics. D. Transwell assay was performed to monitor cell invasiveness after transfection with pcDNA-MMP-2 or miR-20b mimics. Data represent the mean ± SD of three independent experiments. ** P

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: MicroRNA-20b inhibits trophoblast cell migration and invasion by targeting MMP-2

    doi:

    Figure Lengend Snippet: MMP-2 reversed the effect of miR-20b on cell invasion in HTR8/SVneo cells. HTR8/SVneo cells were co-transfected with si-MMP-2 and miR-20b inhibitor. A. Wound healing assay was performed to monitor cell migration after transfection with si-MMP-2 or miR-20b inhibitor. B. Transwell assay was performed to monitor cell invasiveness after transfection with si-MMP-2 or miR-20b inhibitor. C. Wound healing assay was performed to monitor cell migration after transfection with pcDNA-MMP-2 or miR-20b mimics. D. Transwell assay was performed to monitor cell invasiveness after transfection with pcDNA-MMP-2 or miR-20b mimics. Data represent the mean ± SD of three independent experiments. ** P

    Article Snippet: MMP-2 overexpression plasmid (pcDNA-MMP-2) and MMP-2 siRNA for silencing MMP-2 were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Transfection, Wound Healing Assay, Migration, Transwell Assay

    miR-20b negatively regulated the expression of MMP-2. A. The mRNA expression of MMP-2 was measured using qRT-PCR in placentas samples from fifteen patients with PE and fifteen women with normal pregnancies. Data represent the mean ± SD of three independent experiments. P

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: MicroRNA-20b inhibits trophoblast cell migration and invasion by targeting MMP-2

    doi:

    Figure Lengend Snippet: miR-20b negatively regulated the expression of MMP-2. A. The mRNA expression of MMP-2 was measured using qRT-PCR in placentas samples from fifteen patients with PE and fifteen women with normal pregnancies. Data represent the mean ± SD of three independent experiments. P

    Article Snippet: MMP-2 overexpression plasmid (pcDNA-MMP-2) and MMP-2 siRNA for silencing MMP-2 were purchased from Santa Cruz Biotechnology (Santa Cruz, CA, USA).

    Techniques: Expressing, Quantitative RT-PCR

    Cardiac ischemia in rabbits reduces mature ERG protein expression and increases the expression of calpain, matriptase-2, and MMP-2. A and B , Western blots of ventricular tissue from control ( Ctrl ) or ischemic ( Isc ) rabbit hearts showing that 24-h ischemia

    Journal: The Journal of Biological Chemistry

    Article Title: The Human Ether-a-go-go-related Gene (hERG) Potassium Channel Represents an Unusual Target for Protease-mediated Damage *

    doi: 10.1074/jbc.M116.743138

    Figure Lengend Snippet: Cardiac ischemia in rabbits reduces mature ERG protein expression and increases the expression of calpain, matriptase-2, and MMP-2. A and B , Western blots of ventricular tissue from control ( Ctrl ) or ischemic ( Isc ) rabbit hearts showing that 24-h ischemia

    Article Snippet: Goat anti-hERG (C-20 (sc-15968, C-terminal) and N-20 (sc-15966, N-terminal)), goat anti-matriptase-2 (sc-54240), goat anti-KCNE1 (sc-16796), rabbit anti-MMP-2 (sc-10736), and rabbit anti-calpain (sc-30064) primary antibodies and goat anti-rabbit (sc-2004), goat anti-mouse (sc-2005), and mouse anti-goat (sc-2354) IgG-HRP secondary antibodies were purchased from Santa Cruz Biotechnology.

    Techniques: Expressing, Western Blot

    GSP inhibits the migration and invasion of SCC12 cells by reducing MMP-2/9 expression and activity. (A) The effect of GSP on the motility of SCC12 cells was assessed using wound-healing assays. Images were captured of migrating cells in the denuded zone (magnification, ×100). (B) The effect of GSP on the invasion of SCC12 cells. Cells were treated with various concentrations of GSP for 24 h and a cell invasion assay was performed. Images were captured of the invaded cells (magnification, ×200). (C) The effect of GSP on the activities and protein expression of MMP-2/9. (C-a) Supernatants of GSP-treated SCC12 cells were loaded into 10% gelatin-containing gel, resolved by electrophoresis and stained with Coomassie blue. (C-b) Total cell lysates were analyzed by SDS-PAGE, followed by probing with anti-human MMP-2 antibody. β-actin was used as a control for protein loading. MMP, matrix metalloproteinase; GSP, grape seed procyanidins; CTL, control.

    Journal: Oncology Letters

    Article Title: Procyanidins from Vitis vinifera seeds induce apoptotic and autophagic cell death via generation of reactive oxygen species in squamous cell carcinoma cells

    doi: 10.3892/ol.2017.6422

    Figure Lengend Snippet: GSP inhibits the migration and invasion of SCC12 cells by reducing MMP-2/9 expression and activity. (A) The effect of GSP on the motility of SCC12 cells was assessed using wound-healing assays. Images were captured of migrating cells in the denuded zone (magnification, ×100). (B) The effect of GSP on the invasion of SCC12 cells. Cells were treated with various concentrations of GSP for 24 h and a cell invasion assay was performed. Images were captured of the invaded cells (magnification, ×200). (C) The effect of GSP on the activities and protein expression of MMP-2/9. (C-a) Supernatants of GSP-treated SCC12 cells were loaded into 10% gelatin-containing gel, resolved by electrophoresis and stained with Coomassie blue. (C-b) Total cell lysates were analyzed by SDS-PAGE, followed by probing with anti-human MMP-2 antibody. β-actin was used as a control for protein loading. MMP, matrix metalloproteinase; GSP, grape seed procyanidins; CTL, control.

    Article Snippet: Total proteins (30 µg) were separated by 10% SDS-PAGE and transferred onto a nitrocellulose membrane using semidry transfer apparatus (Trans-Blot SD Semi-Dry Transfer Cell; Bio-Rad Laboratories, Inc., Hercules, CA, USA) at 15 V for 30 min. Membranes were blocked with 5% skimmed milk and incubated with specific antibodies against MMP-2 (1:1,000 dilution; sc-10736; Santa Cruz Biotechnology, Inc., Dallas, TX, USA) and microtubule-associated protein 1 light chain 3 (LC3) (1:1,000 dilution; AP1801a; Abgent, Inc., San Diego, CA, USA) at 4°C overnight.

    Techniques: Migration, Expressing, Activity Assay, Invasion Assay, Electrophoresis, Staining, SDS Page, CTL Assay

    Expression of MMP-2 and MMP-9 protein following treatment. MMP, matrix metalloproteinase; US, ultrasound group; US + MB, ultrasound in combination with microbubbles group.

    Journal: Oncology Letters

    Article Title: Combined treatment of PC-3 cells with ultrasound and microbubbles suppresses invasion and migration

    doi: 10.3892/ol.2014.2310

    Figure Lengend Snippet: Expression of MMP-2 and MMP-9 protein following treatment. MMP, matrix metalloproteinase; US, ultrasound group; US + MB, ultrasound in combination with microbubbles group.

    Article Snippet: The membranes were then probed with primary rabbit monoclonal antibodies against MMP-2 and -9 (Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA) at 4°C overnight.

    Techniques: Expressing

    Graphical representation of mRNA expression of a MMP-2 b MMP-9 c HOXA-11 d HOXA-10 in the endometrium of women with endometriosis and controls. e Endometrial expression of MMP-2, MMP-9, HOXA-11, HOXA-10 and β-actin in women with endometriosis

    Journal: Journal of Assisted Reproduction and Genetics

    Article Title: HOXA-11 mediated dysregulation of matrix remodeling during implantation window in women with endometriosis

    doi: 10.1007/s10815-013-0088-9

    Figure Lengend Snippet: Graphical representation of mRNA expression of a MMP-2 b MMP-9 c HOXA-11 d HOXA-10 in the endometrium of women with endometriosis and controls. e Endometrial expression of MMP-2, MMP-9, HOXA-11, HOXA-10 and β-actin in women with endometriosis

    Article Snippet: 30 μg of homogenate protein was separated by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and the separated proteins electroblotted onto a Hybond nitrocellulose membrane (GE Healthcare) at 30 V for 13 h. After blocking the non-specific binding sites with non-fat dry milk in TBST buffer for 1 h at room temperature, the blots were incubated overnight at 4 °C with mouse monoclonal antibody against MMP-2, -9 (Santa Cruz Biotechnology Inc, Santa Cruz, CA, USA) and rabbit polyclonal antibody against HOXA-10 and −11 (Santa Cruz Biotechnology Inc, Santa Cruz, CA, USA).

    Techniques: Expressing