Structured Review

Santa Cruz Biotechnology mmp 2
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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Images

1) Product Images from "Anti-inflammatory/anti-fibrotic effects of the hepatoprotective silymarin and the schistosomicide praziquantel against Schistosoma mansoni-induced liver fibrosis"

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

Journal: Parasites & Vectors

doi: 10.1186/1756-3305-5-9

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).
Figure Legend 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).

Techniques Used: Infection, Mouse Assay, Staining

2) Product Images from "Anti-inflammatory/anti-fibrotic effects of the hepatoprotective silymarin and the schistosomicide praziquantel against Schistosoma mansoni-induced liver fibrosis"

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

Journal: Parasites & Vectors

doi: 10.1186/1756-3305-5-9

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).
Figure Legend 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).

Techniques Used: Infection, Mouse Assay, Staining

3) Product Images from "Anti-inflammatory/anti-fibrotic effects of the hepatoprotective silymarin and the schistosomicide praziquantel against Schistosoma mansoni-induced liver fibrosis"

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

Journal: Parasites & Vectors

doi: 10.1186/1756-3305-5-9

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).
Figure Legend 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).

Techniques Used: Infection, Mouse Assay, Staining

4) Product Images from "Chromodomain Helicase/ATPase DNA-Binding Protein 1-Like Gene (CHD1L) Expression and Implications for Invasion and Metastasis of Breast Cancer"

Article Title: Chromodomain Helicase/ATPase DNA-Binding Protein 1-Like Gene (CHD1L) Expression and Implications for Invasion and Metastasis of Breast Cancer

Journal: PLoS ONE

doi: 10.1371/journal.pone.0143030

CHD1L promotes lung colonization of human breast cancer in vivo . (A) Comparison of tumor cell colonies in mouse lungs between groups. (B) Tumor foci in mouse lungs were visualized using H E staining. Scale bar: 50 μm. (C) Lung metastatic nodules were counted ( n = 10). (D) Expression of CHD1L, MMP-2, and MMP-9 was detected in mice xenograft tumors by Western blot analysis. β-Actin was used as a loading control. Quantification of relative protein levels on three different Western blot analyses is shown below the blots.
Figure Legend Snippet: CHD1L promotes lung colonization of human breast cancer in vivo . (A) Comparison of tumor cell colonies in mouse lungs between groups. (B) Tumor foci in mouse lungs were visualized using H E staining. Scale bar: 50 μm. (C) Lung metastatic nodules were counted ( n = 10). (D) Expression of CHD1L, MMP-2, and MMP-9 was detected in mice xenograft tumors by Western blot analysis. β-Actin was used as a loading control. Quantification of relative protein levels on three different Western blot analyses is shown below the blots.

Techniques Used: In Vivo, Staining, Expressing, Mouse Assay, Western Blot

CHD1L is specifically upregulated in human breast cancer cell lines and tissues. (A) Left, Expression of CHD1L protein in cultured human normal mammary epithelial cell line (MCF10A) and various breast cancer cell lines (MDA-MB-231, T-47D, SK-BR-3, and MCF-7). Right, Expression of CHD1L protein in paired breast cancer tissues (T) and adjacent non-tumor tissues (ANT), with each pair obtained from the same patient. β-Actin was used as a loading control. Quantification of relative protein levels is shown below the blots. Results are representative of at least three repeated experiments. (B) Positive expression of CHD1L protein in normal mammary glands (a), negative expression of CHD1L protein in normal mammary glands (b), positive expression of CHD1L protein in carcinoma with lymph node metastasis (c), positive expression of MMP-2 protein in carcinoma with positive expression of CHD1L (d), positive expression of MMP-9 protein in carcinoma with positive expression of CHD1L (e), negative expression of CHD1L protein in carcinoma without lymph node metastasis (f), negative expression of MMP-2 protein in carcinoma with negative expression of CHD1L (g), and negative expression of MMP-9 protein in carcinoma with negative expression of CHD1L (h) were examined using immunohistochemical staining. Scale bar: 20 μm. (C) Kaplan–Meier analysis was performed between the CHD1L level and overall survival of breast cancer patients with positive (n = 112) and low (n = 156) CHD1L expression.
Figure Legend Snippet: CHD1L is specifically upregulated in human breast cancer cell lines and tissues. (A) Left, Expression of CHD1L protein in cultured human normal mammary epithelial cell line (MCF10A) and various breast cancer cell lines (MDA-MB-231, T-47D, SK-BR-3, and MCF-7). Right, Expression of CHD1L protein in paired breast cancer tissues (T) and adjacent non-tumor tissues (ANT), with each pair obtained from the same patient. β-Actin was used as a loading control. Quantification of relative protein levels is shown below the blots. Results are representative of at least three repeated experiments. (B) Positive expression of CHD1L protein in normal mammary glands (a), negative expression of CHD1L protein in normal mammary glands (b), positive expression of CHD1L protein in carcinoma with lymph node metastasis (c), positive expression of MMP-2 protein in carcinoma with positive expression of CHD1L (d), positive expression of MMP-9 protein in carcinoma with positive expression of CHD1L (e), negative expression of CHD1L protein in carcinoma without lymph node metastasis (f), negative expression of MMP-2 protein in carcinoma with negative expression of CHD1L (g), and negative expression of MMP-9 protein in carcinoma with negative expression of CHD1L (h) were examined using immunohistochemical staining. Scale bar: 20 μm. (C) Kaplan–Meier analysis was performed between the CHD1L level and overall survival of breast cancer patients with positive (n = 112) and low (n = 156) CHD1L expression.

Techniques Used: Expressing, Cell Culture, Multiple Displacement Amplification, Immunohistochemistry, Staining

5) Product Images from "Chromodomain Helicase/ATPase DNA-Binding Protein 1-Like Gene (CHD1L) Expression and Implications for Invasion and Metastasis of Breast Cancer"

Article Title: Chromodomain Helicase/ATPase DNA-Binding Protein 1-Like Gene (CHD1L) Expression and Implications for Invasion and Metastasis of Breast Cancer

Journal: PLoS ONE

doi: 10.1371/journal.pone.0143030

CHD1L promotes lung colonization of human breast cancer in vivo . (A) Comparison of tumor cell colonies in mouse lungs between groups. (B) Tumor foci in mouse lungs were visualized using H E staining. Scale bar: 50 μm. (C) Lung metastatic nodules were counted ( n = 10). (D) Expression of CHD1L, MMP-2, and MMP-9 was detected in mice xenograft tumors by Western blot analysis. β-Actin was used as a loading control. Quantification of relative protein levels on three different Western blot analyses is shown below the blots.
Figure Legend Snippet: CHD1L promotes lung colonization of human breast cancer in vivo . (A) Comparison of tumor cell colonies in mouse lungs between groups. (B) Tumor foci in mouse lungs were visualized using H E staining. Scale bar: 50 μm. (C) Lung metastatic nodules were counted ( n = 10). (D) Expression of CHD1L, MMP-2, and MMP-9 was detected in mice xenograft tumors by Western blot analysis. β-Actin was used as a loading control. Quantification of relative protein levels on three different Western blot analyses is shown below the blots.

Techniques Used: In Vivo, Staining, Expressing, Mouse Assay, Western Blot

CHD1L is specifically upregulated in human breast cancer cell lines and tissues. (A) Left, Expression of CHD1L protein in cultured human normal mammary epithelial cell line (MCF10A) and various breast cancer cell lines (MDA-MB-231, T-47D, SK-BR-3, and MCF-7). Right, Expression of CHD1L protein in paired breast cancer tissues (T) and adjacent non-tumor tissues (ANT), with each pair obtained from the same patient. β-Actin was used as a loading control. Quantification of relative protein levels is shown below the blots. Results are representative of at least three repeated experiments. (B) Positive expression of CHD1L protein in normal mammary glands (a), negative expression of CHD1L protein in normal mammary glands (b), positive expression of CHD1L protein in carcinoma with lymph node metastasis (c), positive expression of MMP-2 protein in carcinoma with positive expression of CHD1L (d), positive expression of MMP-9 protein in carcinoma with positive expression of CHD1L (e), negative expression of CHD1L protein in carcinoma without lymph node metastasis (f), negative expression of MMP-2 protein in carcinoma with negative expression of CHD1L (g), and negative expression of MMP-9 protein in carcinoma with negative expression of CHD1L (h) were examined using immunohistochemical staining. Scale bar: 20 μm. (C) Kaplan–Meier analysis was performed between the CHD1L level and overall survival of breast cancer patients with positive (n = 112) and low (n = 156) CHD1L expression.
Figure Legend Snippet: CHD1L is specifically upregulated in human breast cancer cell lines and tissues. (A) Left, Expression of CHD1L protein in cultured human normal mammary epithelial cell line (MCF10A) and various breast cancer cell lines (MDA-MB-231, T-47D, SK-BR-3, and MCF-7). Right, Expression of CHD1L protein in paired breast cancer tissues (T) and adjacent non-tumor tissues (ANT), with each pair obtained from the same patient. β-Actin was used as a loading control. Quantification of relative protein levels is shown below the blots. Results are representative of at least three repeated experiments. (B) Positive expression of CHD1L protein in normal mammary glands (a), negative expression of CHD1L protein in normal mammary glands (b), positive expression of CHD1L protein in carcinoma with lymph node metastasis (c), positive expression of MMP-2 protein in carcinoma with positive expression of CHD1L (d), positive expression of MMP-9 protein in carcinoma with positive expression of CHD1L (e), negative expression of CHD1L protein in carcinoma without lymph node metastasis (f), negative expression of MMP-2 protein in carcinoma with negative expression of CHD1L (g), and negative expression of MMP-9 protein in carcinoma with negative expression of CHD1L (h) were examined using immunohistochemical staining. Scale bar: 20 μm. (C) Kaplan–Meier analysis was performed between the CHD1L level and overall survival of breast cancer patients with positive (n = 112) and low (n = 156) CHD1L expression.

Techniques Used: Expressing, Cell Culture, Multiple Displacement Amplification, Immunohistochemistry, Staining

6) Product Images from "Chromodomain Helicase/ATPase DNA-Binding Protein 1-Like Gene (CHD1L) Expression and Implications for Invasion and Metastasis of Breast Cancer"

Article Title: Chromodomain Helicase/ATPase DNA-Binding Protein 1-Like Gene (CHD1L) Expression and Implications for Invasion and Metastasis of Breast Cancer

Journal: PLoS ONE

doi: 10.1371/journal.pone.0143030

CHD1L promotes lung colonization of human breast cancer in vivo . (A) Comparison of tumor cell colonies in mouse lungs between groups. (B) Tumor foci in mouse lungs were visualized using H E staining. Scale bar: 50 μm. (C) Lung metastatic nodules were counted ( n = 10). (D) Expression of CHD1L, MMP-2, and MMP-9 was detected in mice xenograft tumors by Western blot analysis. β-Actin was used as a loading control. Quantification of relative protein levels on three different Western blot analyses is shown below the blots.
Figure Legend Snippet: CHD1L promotes lung colonization of human breast cancer in vivo . (A) Comparison of tumor cell colonies in mouse lungs between groups. (B) Tumor foci in mouse lungs were visualized using H E staining. Scale bar: 50 μm. (C) Lung metastatic nodules were counted ( n = 10). (D) Expression of CHD1L, MMP-2, and MMP-9 was detected in mice xenograft tumors by Western blot analysis. β-Actin was used as a loading control. Quantification of relative protein levels on three different Western blot analyses is shown below the blots.

Techniques Used: In Vivo, Staining, Expressing, Mouse Assay, Western Blot

CHD1L is specifically upregulated in human breast cancer cell lines and tissues. (A) Left, Expression of CHD1L protein in cultured human normal mammary epithelial cell line (MCF10A) and various breast cancer cell lines (MDA-MB-231, T-47D, SK-BR-3, and MCF-7). Right, Expression of CHD1L protein in paired breast cancer tissues (T) and adjacent non-tumor tissues (ANT), with each pair obtained from the same patient. β-Actin was used as a loading control. Quantification of relative protein levels is shown below the blots. Results are representative of at least three repeated experiments. (B) Positive expression of CHD1L protein in normal mammary glands (a), negative expression of CHD1L protein in normal mammary glands (b), positive expression of CHD1L protein in carcinoma with lymph node metastasis (c), positive expression of MMP-2 protein in carcinoma with positive expression of CHD1L (d), positive expression of MMP-9 protein in carcinoma with positive expression of CHD1L (e), negative expression of CHD1L protein in carcinoma without lymph node metastasis (f), negative expression of MMP-2 protein in carcinoma with negative expression of CHD1L (g), and negative expression of MMP-9 protein in carcinoma with negative expression of CHD1L (h) were examined using immunohistochemical staining. Scale bar: 20 μm. (C) Kaplan–Meier analysis was performed between the CHD1L level and overall survival of breast cancer patients with positive (n = 112) and low (n = 156) CHD1L expression.
Figure Legend Snippet: CHD1L is specifically upregulated in human breast cancer cell lines and tissues. (A) Left, Expression of CHD1L protein in cultured human normal mammary epithelial cell line (MCF10A) and various breast cancer cell lines (MDA-MB-231, T-47D, SK-BR-3, and MCF-7). Right, Expression of CHD1L protein in paired breast cancer tissues (T) and adjacent non-tumor tissues (ANT), with each pair obtained from the same patient. β-Actin was used as a loading control. Quantification of relative protein levels is shown below the blots. Results are representative of at least three repeated experiments. (B) Positive expression of CHD1L protein in normal mammary glands (a), negative expression of CHD1L protein in normal mammary glands (b), positive expression of CHD1L protein in carcinoma with lymph node metastasis (c), positive expression of MMP-2 protein in carcinoma with positive expression of CHD1L (d), positive expression of MMP-9 protein in carcinoma with positive expression of CHD1L (e), negative expression of CHD1L protein in carcinoma without lymph node metastasis (f), negative expression of MMP-2 protein in carcinoma with negative expression of CHD1L (g), and negative expression of MMP-9 protein in carcinoma with negative expression of CHD1L (h) were examined using immunohistochemical staining. Scale bar: 20 μm. (C) Kaplan–Meier analysis was performed between the CHD1L level and overall survival of breast cancer patients with positive (n = 112) and low (n = 156) CHD1L expression.

Techniques Used: Expressing, Cell Culture, Multiple Displacement Amplification, Immunohistochemistry, Staining

7) Product Images from "Plaque Rupture is a Determinant of Vascular Events in Carotid Artery Atherosclerotic Disease: Involvement of Matrix Metalloproteinases 2 and 9"

Article Title: Plaque Rupture is a Determinant of Vascular Events in Carotid Artery Atherosclerotic Disease: Involvement of Matrix Metalloproteinases 2 and 9

Journal: Journal of Clinical Neurology (Seoul, Korea)

doi: 10.3988/jcn.2011.7.2.69

Immunofluorescence staining illustrating the expressions of MMP-2 and MMP-9 produced by macrophages in carotid plaques. A and D: MMP-2 and MMP-9 were visualized with secondary antibodies conjugated to Texas Red (red). B and E: The nuclei were stained with DAPI (blue). C and F: MMPs colocalized with the cytoplasm in the macrophages. The white boxes in each image are magnified. Scale bar=100 µm. MMP: matrix metalloproteinase.
Figure Legend Snippet: Immunofluorescence staining illustrating the expressions of MMP-2 and MMP-9 produced by macrophages in carotid plaques. A and D: MMP-2 and MMP-9 were visualized with secondary antibodies conjugated to Texas Red (red). B and E: The nuclei were stained with DAPI (blue). C and F: MMPs colocalized with the cytoplasm in the macrophages. The white boxes in each image are magnified. Scale bar=100 µm. MMP: matrix metalloproteinase.

Techniques Used: Immunofluorescence, Staining, Produced

Carotid specimens that were immunohistochemically positive for MMP-2 (A) and MMP-9 (B) were also strongly positive for CD68 (C) but negative for SMA (D). MMP: matrix metalloproteinase, SMA: smooth-muscle actin.
Figure Legend Snippet: Carotid specimens that were immunohistochemically positive for MMP-2 (A) and MMP-9 (B) were also strongly positive for CD68 (C) but negative for SMA (D). MMP: matrix metalloproteinase, SMA: smooth-muscle actin.

Techniques Used:

8) Product Images from "MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer"

Article Title: MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.13283

MMP ‐13 and  MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS  double‐staining in H460 xenografts showed decreased  VM  but increased  EDV  numbers (Bar = 100 μm). The black arrow shows  VM  formation. The red arrow shows the  EDV s. ( C ) The expression levels of  MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the  MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm).  WB  showed  MMP ‐13 gradually increasing, but Ln‐5 and  EGFR  showed a decreasing trend with tumour growth.  MMP ‐2 expression was observed at different tumour growth stages.
Figure Legend Snippet: MMP ‐13 and MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS double‐staining in H460 xenografts showed decreased VM but increased EDV numbers (Bar = 100 μm). The black arrow shows VM formation. The red arrow shows the EDV s. ( C ) The expression levels of MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm). WB showed MMP ‐13 gradually increasing, but Ln‐5 and EGFR showed a decreasing trend with tumour growth. MMP ‐2 expression was observed at different tumour growth stages.

Techniques Used: Expressing, Double Staining, Western Blot

Cleavage of Ln‐5 by  MMP ‐13 was detected with a silver staining kit and  LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by  MMP ‐2 and  MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12%  SDS ‐ PAGE  gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain.  MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment.  MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B )  LC ‐ MS / MS  detection showed that the 20 kD fragment generated by  MMP ‐13 was part of the Ln‐5γ2 chain. ( C )  MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain  III  and IV domain.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐13 was detected with a silver staining kit and LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by MMP ‐2 and MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12% SDS ‐ PAGE gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain. MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment. MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B ) LC ‐ MS / MS detection showed that the 20 kD fragment generated by MMP ‐13 was part of the Ln‐5γ2 chain. ( C ) MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain III and IV domain.

Techniques Used: Silver Staining, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, SDS Page, Generated, Molecular Weight

Cleavage of Ln‐5 by  MMP ‐2 or  MMP ‐13 affected  EGFR  and F‐actin expression. ( A ) The  WB  results show that treatment with  MMP ‐2 Ln‐5 cleavage fragments enhanced the  EGFR , F‐actin and  EGFR  downstream targets Raf,  ERK  and  AKT  protein levels in cells, but the levels were reduced in the  MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of  EGFR  and F‐actin filaments was observed in the  MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the  MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐2 or MMP ‐13 affected EGFR and F‐actin expression. ( A ) The WB results show that treatment with MMP ‐2 Ln‐5 cleavage fragments enhanced the EGFR , F‐actin and EGFR downstream targets Raf, ERK and AKT protein levels in cells, but the levels were reduced in the MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of EGFR and F‐actin filaments was observed in the MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.

Techniques Used: Expressing, Western Blot, Immunofluorescence, Staining

VM  and the expression of  MMP ‐13,  MMP ‐2, Ln‐5 and  EGFR  in  LCLC  tissues. ( A ) Representative images of the presence of  VM  in human  LCLC  tissues ( CD 34/ PAS  double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both  CD 34 and  PAS . The black arrows show  VM  channels in which  PAS ‐positive materials and red blood cells (red arrow) are observed. ( B )  VM ‐positive tissues exhibited significantly reduced  MMP ‐13 expression, and  VM ‐negative tissues exhibited significantly increased  MMP ‐13 expression ( P  = 0.005). In contrast,  VM ‐positive tissues exhibited significantly reduced  MMP ‐2 expression, and  VM ‐negative tissue exhibited significantly increased  MMP ‐2 expression. There was no significant correlation between  MMP ‐13 and  MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and  EGFR  can be observed in the  LCLC  samples with  MMP ‐13‐positive tissues compared with expression in  VM ‐negative tissues ( P
Figure Legend Snippet: VM and the expression of MMP ‐13, MMP ‐2, Ln‐5 and EGFR in LCLC tissues. ( A ) Representative images of the presence of VM in human LCLC tissues ( CD 34/ PAS double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both CD 34 and PAS . The black arrows show VM channels in which PAS ‐positive materials and red blood cells (red arrow) are observed. ( B ) VM ‐positive tissues exhibited significantly reduced MMP ‐13 expression, and VM ‐negative tissues exhibited significantly increased MMP ‐13 expression ( P  = 0.005). In contrast, VM ‐positive tissues exhibited significantly reduced MMP ‐2 expression, and VM ‐negative tissue exhibited significantly increased MMP ‐2 expression. There was no significant correlation between MMP ‐13 and MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and EGFR can be observed in the LCLC samples with MMP ‐13‐positive tissues compared with expression in VM ‐negative tissues ( P

Techniques Used: Expressing, Double Staining

9) Product Images from "MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer"

Article Title: MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.13283

MMP ‐13 and  MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS  double‐staining in H460 xenografts showed decreased  VM  but increased  EDV  numbers (Bar = 100 μm). The black arrow shows  VM  formation. The red arrow shows the  EDV s. ( C ) The expression levels of  MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the  MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm).  WB  showed  MMP ‐13 gradually increasing, but Ln‐5 and  EGFR  showed a decreasing trend with tumour growth.  MMP ‐2 expression was observed at different tumour growth stages.
Figure Legend Snippet: MMP ‐13 and MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS double‐staining in H460 xenografts showed decreased VM but increased EDV numbers (Bar = 100 μm). The black arrow shows VM formation. The red arrow shows the EDV s. ( C ) The expression levels of MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm). WB showed MMP ‐13 gradually increasing, but Ln‐5 and EGFR showed a decreasing trend with tumour growth. MMP ‐2 expression was observed at different tumour growth stages.

Techniques Used: Expressing, Double Staining, Western Blot

Cleavage of Ln‐5 by  MMP ‐13 was detected with a silver staining kit and  LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by  MMP ‐2 and  MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12%  SDS ‐ PAGE  gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain.  MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment.  MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B )  LC ‐ MS / MS  detection showed that the 20 kD fragment generated by  MMP ‐13 was part of the Ln‐5γ2 chain. ( C )  MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain  III  and IV domain.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐13 was detected with a silver staining kit and LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by MMP ‐2 and MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12% SDS ‐ PAGE gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain. MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment. MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B ) LC ‐ MS / MS detection showed that the 20 kD fragment generated by MMP ‐13 was part of the Ln‐5γ2 chain. ( C ) MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain III and IV domain.

Techniques Used: Silver Staining, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, SDS Page, Generated, Molecular Weight

Cleavage of Ln‐5 by  MMP ‐2 or  MMP ‐13 affected  EGFR  and F‐actin expression. ( A ) The  WB  results show that treatment with  MMP ‐2 Ln‐5 cleavage fragments enhanced the  EGFR , F‐actin and  EGFR  downstream targets Raf,  ERK  and  AKT  protein levels in cells, but the levels were reduced in the  MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of  EGFR  and F‐actin filaments was observed in the  MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the  MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐2 or MMP ‐13 affected EGFR and F‐actin expression. ( A ) The WB results show that treatment with MMP ‐2 Ln‐5 cleavage fragments enhanced the EGFR , F‐actin and EGFR downstream targets Raf, ERK and AKT protein levels in cells, but the levels were reduced in the MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of EGFR and F‐actin filaments was observed in the MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.

Techniques Used: Expressing, Western Blot, Immunofluorescence, Staining

VM  and the expression of  MMP ‐13,  MMP ‐2, Ln‐5 and  EGFR  in  LCLC  tissues. ( A ) Representative images of the presence of  VM  in human  LCLC  tissues ( CD 34/ PAS  double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both  CD 34 and  PAS . The black arrows show  VM  channels in which  PAS ‐positive materials and red blood cells (red arrow) are observed. ( B )  VM ‐positive tissues exhibited significantly reduced  MMP ‐13 expression, and  VM ‐negative tissues exhibited significantly increased  MMP ‐13 expression ( P  = 0.005). In contrast,  VM ‐positive tissues exhibited significantly reduced  MMP ‐2 expression, and  VM ‐negative tissue exhibited significantly increased  MMP ‐2 expression. There was no significant correlation between  MMP ‐13 and  MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and  EGFR  can be observed in the  LCLC  samples with  MMP ‐13‐positive tissues compared with expression in  VM ‐negative tissues ( P
Figure Legend Snippet: VM and the expression of MMP ‐13, MMP ‐2, Ln‐5 and EGFR in LCLC tissues. ( A ) Representative images of the presence of VM in human LCLC tissues ( CD 34/ PAS double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both CD 34 and PAS . The black arrows show VM channels in which PAS ‐positive materials and red blood cells (red arrow) are observed. ( B ) VM ‐positive tissues exhibited significantly reduced MMP ‐13 expression, and VM ‐negative tissues exhibited significantly increased MMP ‐13 expression ( P  = 0.005). In contrast, VM ‐positive tissues exhibited significantly reduced MMP ‐2 expression, and VM ‐negative tissue exhibited significantly increased MMP ‐2 expression. There was no significant correlation between MMP ‐13 and MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and EGFR can be observed in the LCLC samples with MMP ‐13‐positive tissues compared with expression in VM ‐negative tissues ( P

Techniques Used: Expressing, Double Staining

10) Product Images from "MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer"

Article Title: MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.13283

MMP ‐13 and  MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS  double‐staining in H460 xenografts showed decreased  VM  but increased  EDV  numbers (Bar = 100 μm). The black arrow shows  VM  formation. The red arrow shows the  EDV s. ( C ) The expression levels of  MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the  MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm).  WB  showed  MMP ‐13 gradually increasing, but Ln‐5 and  EGFR  showed a decreasing trend with tumour growth.  MMP ‐2 expression was observed at different tumour growth stages.
Figure Legend Snippet: MMP ‐13 and MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS double‐staining in H460 xenografts showed decreased VM but increased EDV numbers (Bar = 100 μm). The black arrow shows VM formation. The red arrow shows the EDV s. ( C ) The expression levels of MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm). WB showed MMP ‐13 gradually increasing, but Ln‐5 and EGFR showed a decreasing trend with tumour growth. MMP ‐2 expression was observed at different tumour growth stages.

Techniques Used: Expressing, Double Staining, Western Blot

Cleavage of Ln‐5 by  MMP ‐13 was detected with a silver staining kit and  LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by  MMP ‐2 and  MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12%  SDS ‐ PAGE  gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain.  MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment.  MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B )  LC ‐ MS / MS  detection showed that the 20 kD fragment generated by  MMP ‐13 was part of the Ln‐5γ2 chain. ( C )  MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain  III  and IV domain.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐13 was detected with a silver staining kit and LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by MMP ‐2 and MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12% SDS ‐ PAGE gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain. MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment. MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B ) LC ‐ MS / MS detection showed that the 20 kD fragment generated by MMP ‐13 was part of the Ln‐5γ2 chain. ( C ) MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain III and IV domain.

Techniques Used: Silver Staining, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, SDS Page, Generated, Molecular Weight

Cleavage of Ln‐5 by  MMP ‐2 or  MMP ‐13 affected  EGFR  and F‐actin expression. ( A ) The  WB  results show that treatment with  MMP ‐2 Ln‐5 cleavage fragments enhanced the  EGFR , F‐actin and  EGFR  downstream targets Raf,  ERK  and  AKT  protein levels in cells, but the levels were reduced in the  MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of  EGFR  and F‐actin filaments was observed in the  MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the  MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐2 or MMP ‐13 affected EGFR and F‐actin expression. ( A ) The WB results show that treatment with MMP ‐2 Ln‐5 cleavage fragments enhanced the EGFR , F‐actin and EGFR downstream targets Raf, ERK and AKT protein levels in cells, but the levels were reduced in the MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of EGFR and F‐actin filaments was observed in the MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.

Techniques Used: Expressing, Western Blot, Immunofluorescence, Staining

VM  and the expression of  MMP ‐13,  MMP ‐2, Ln‐5 and  EGFR  in  LCLC  tissues. ( A ) Representative images of the presence of  VM  in human  LCLC  tissues ( CD 34/ PAS  double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both  CD 34 and  PAS . The black arrows show  VM  channels in which  PAS ‐positive materials and red blood cells (red arrow) are observed. ( B )  VM ‐positive tissues exhibited significantly reduced  MMP ‐13 expression, and  VM ‐negative tissues exhibited significantly increased  MMP ‐13 expression ( P  = 0.005). In contrast,  VM ‐positive tissues exhibited significantly reduced  MMP ‐2 expression, and  VM ‐negative tissue exhibited significantly increased  MMP ‐2 expression. There was no significant correlation between  MMP ‐13 and  MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and  EGFR  can be observed in the  LCLC  samples with  MMP ‐13‐positive tissues compared with expression in  VM ‐negative tissues ( P
Figure Legend Snippet: VM and the expression of MMP ‐13, MMP ‐2, Ln‐5 and EGFR in LCLC tissues. ( A ) Representative images of the presence of VM in human LCLC tissues ( CD 34/ PAS double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both CD 34 and PAS . The black arrows show VM channels in which PAS ‐positive materials and red blood cells (red arrow) are observed. ( B ) VM ‐positive tissues exhibited significantly reduced MMP ‐13 expression, and VM ‐negative tissues exhibited significantly increased MMP ‐13 expression ( P  = 0.005). In contrast, VM ‐positive tissues exhibited significantly reduced MMP ‐2 expression, and VM ‐negative tissue exhibited significantly increased MMP ‐2 expression. There was no significant correlation between MMP ‐13 and MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and EGFR can be observed in the LCLC samples with MMP ‐13‐positive tissues compared with expression in VM ‐negative tissues ( P

Techniques Used: Expressing, Double Staining

11) Product Images from "MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer"

Article Title: MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.13283

MMP ‐13 and  MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS  double‐staining in H460 xenografts showed decreased  VM  but increased  EDV  numbers (Bar = 100 μm). The black arrow shows  VM  formation. The red arrow shows the  EDV s. ( C ) The expression levels of  MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the  MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm).  WB  showed  MMP ‐13 gradually increasing, but Ln‐5 and  EGFR  showed a decreasing trend with tumour growth.  MMP ‐2 expression was observed at different tumour growth stages.
Figure Legend Snippet: MMP ‐13 and MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS double‐staining in H460 xenografts showed decreased VM but increased EDV numbers (Bar = 100 μm). The black arrow shows VM formation. The red arrow shows the EDV s. ( C ) The expression levels of MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm). WB showed MMP ‐13 gradually increasing, but Ln‐5 and EGFR showed a decreasing trend with tumour growth. MMP ‐2 expression was observed at different tumour growth stages.

Techniques Used: Expressing, Double Staining, Western Blot

Cleavage of Ln‐5 by  MMP ‐13 was detected with a silver staining kit and  LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by  MMP ‐2 and  MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12%  SDS ‐ PAGE  gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain.  MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment.  MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B )  LC ‐ MS / MS  detection showed that the 20 kD fragment generated by  MMP ‐13 was part of the Ln‐5γ2 chain. ( C )  MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain  III  and IV domain.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐13 was detected with a silver staining kit and LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by MMP ‐2 and MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12% SDS ‐ PAGE gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain. MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment. MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B ) LC ‐ MS / MS detection showed that the 20 kD fragment generated by MMP ‐13 was part of the Ln‐5γ2 chain. ( C ) MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain III and IV domain.

Techniques Used: Silver Staining, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, SDS Page, Generated, Molecular Weight

Cleavage of Ln‐5 by  MMP ‐2 or  MMP ‐13 affected  EGFR  and F‐actin expression. ( A ) The  WB  results show that treatment with  MMP ‐2 Ln‐5 cleavage fragments enhanced the  EGFR , F‐actin and  EGFR  downstream targets Raf,  ERK  and  AKT  protein levels in cells, but the levels were reduced in the  MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of  EGFR  and F‐actin filaments was observed in the  MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the  MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐2 or MMP ‐13 affected EGFR and F‐actin expression. ( A ) The WB results show that treatment with MMP ‐2 Ln‐5 cleavage fragments enhanced the EGFR , F‐actin and EGFR downstream targets Raf, ERK and AKT protein levels in cells, but the levels were reduced in the MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of EGFR and F‐actin filaments was observed in the MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.

Techniques Used: Expressing, Western Blot, Immunofluorescence, Staining

VM  and the expression of  MMP ‐13,  MMP ‐2, Ln‐5 and  EGFR  in  LCLC  tissues. ( A ) Representative images of the presence of  VM  in human  LCLC  tissues ( CD 34/ PAS  double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both  CD 34 and  PAS . The black arrows show  VM  channels in which  PAS ‐positive materials and red blood cells (red arrow) are observed. ( B )  VM ‐positive tissues exhibited significantly reduced  MMP ‐13 expression, and  VM ‐negative tissues exhibited significantly increased  MMP ‐13 expression ( P  = 0.005). In contrast,  VM ‐positive tissues exhibited significantly reduced  MMP ‐2 expression, and  VM ‐negative tissue exhibited significantly increased  MMP ‐2 expression. There was no significant correlation between  MMP ‐13 and  MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and  EGFR  can be observed in the  LCLC  samples with  MMP ‐13‐positive tissues compared with expression in  VM ‐negative tissues ( P
Figure Legend Snippet: VM and the expression of MMP ‐13, MMP ‐2, Ln‐5 and EGFR in LCLC tissues. ( A ) Representative images of the presence of VM in human LCLC tissues ( CD 34/ PAS double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both CD 34 and PAS . The black arrows show VM channels in which PAS ‐positive materials and red blood cells (red arrow) are observed. ( B ) VM ‐positive tissues exhibited significantly reduced MMP ‐13 expression, and VM ‐negative tissues exhibited significantly increased MMP ‐13 expression ( P  = 0.005). In contrast, VM ‐positive tissues exhibited significantly reduced MMP ‐2 expression, and VM ‐negative tissue exhibited significantly increased MMP ‐2 expression. There was no significant correlation between MMP ‐13 and MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and EGFR can be observed in the LCLC samples with MMP ‐13‐positive tissues compared with expression in VM ‐negative tissues ( P

Techniques Used: Expressing, Double Staining

12) Product Images from "MicroRNA-195 inhibits growth and invasion of laryngeal carcinoma cells by directly targeting DCUN1D1"

Article Title: MicroRNA-195 inhibits growth and invasion of laryngeal carcinoma cells by directly targeting DCUN1D1

Journal: Oncology Reports

doi: 10.3892/or.2017.5875

Western blot analysis was performed to confirm the re-expression of DCUN1D1 and other related proteins. (A and B) Western blot was used to evaluate the expression levels of DCUN1D1, MMP-9 and MMP-2 proteins transfected with miR-195, DCUN1D1 siRNA or co-transfected with miR-195 and pcDNA3.1-DCUN1D1 in TU-177 cells. Data are expressed as the mean value ± SD. *P
Figure Legend Snippet: Western blot analysis was performed to confirm the re-expression of DCUN1D1 and other related proteins. (A and B) Western blot was used to evaluate the expression levels of DCUN1D1, MMP-9 and MMP-2 proteins transfected with miR-195, DCUN1D1 siRNA or co-transfected with miR-195 and pcDNA3.1-DCUN1D1 in TU-177 cells. Data are expressed as the mean value ± SD. *P

Techniques Used: Western Blot, Expressing, Transfection

13) Product Images from "MicroRNA-195 inhibits growth and invasion of laryngeal carcinoma cells by directly targeting DCUN1D1"

Article Title: MicroRNA-195 inhibits growth and invasion of laryngeal carcinoma cells by directly targeting DCUN1D1

Journal: Oncology Reports

doi: 10.3892/or.2017.5875

Western blot analysis was performed to confirm the re-expression of DCUN1D1 and other related proteins. (A and B) Western blot was used to evaluate the expression levels of DCUN1D1, MMP-9 and MMP-2 proteins transfected with miR-195, DCUN1D1 siRNA or co-transfected with miR-195 and pcDNA3.1-DCUN1D1 in TU-177 cells. Data are expressed as the mean value ± SD. *P
Figure Legend Snippet: Western blot analysis was performed to confirm the re-expression of DCUN1D1 and other related proteins. (A and B) Western blot was used to evaluate the expression levels of DCUN1D1, MMP-9 and MMP-2 proteins transfected with miR-195, DCUN1D1 siRNA or co-transfected with miR-195 and pcDNA3.1-DCUN1D1 in TU-177 cells. Data are expressed as the mean value ± SD. *P

Techniques Used: Western Blot, Expressing, Transfection

14) Product Images from "Anti-metastatic activity of fangchinoline in human gastric cancer AGS cells"

Article Title: Anti-metastatic activity of fangchinoline in human gastric cancer AGS cells

Journal: Oncology Letters

doi: 10.3892/ol.2016.5457

Effects of FCL on the expression of MMP-2/MMP-9 and phosphorylation of AKT in gastric cancer cells. (A) Cells were treated with or without FCL (0–8 µM) for 24 h. Total protein was extracted, and western blotting was performed to assess the expression of MMP-2 and MMP-9 proteins. (B) Western blotting was performed to assess the expression of p-AKT and AKT proteins. (C and D) The densitometry of the bands was normalized to the expression of GAPDH and analyzed. *P
Figure Legend Snippet: Effects of FCL on the expression of MMP-2/MMP-9 and phosphorylation of AKT in gastric cancer cells. (A) Cells were treated with or without FCL (0–8 µM) for 24 h. Total protein was extracted, and western blotting was performed to assess the expression of MMP-2 and MMP-9 proteins. (B) Western blotting was performed to assess the expression of p-AKT and AKT proteins. (C and D) The densitometry of the bands was normalized to the expression of GAPDH and analyzed. *P

Techniques Used: Expressing, Western Blot

Effects of FCL on the expression of MMP-2, MMP-9, TIMP1 and TIMP2 mRNAs. (A) Gastric cancer cells were treated with or without FCL (2–8 µM) for 24 h. Total RNA was isolated, and reverse transcription-polymerase chain reaction was performed to detect the expression of MMP-2, MMP-9, TIMP1 and TIMP2 mRNAs. (B) The densitometry of the bands was normalized to the expression of GAPDH and analyzed. *P
Figure Legend Snippet: Effects of FCL on the expression of MMP-2, MMP-9, TIMP1 and TIMP2 mRNAs. (A) Gastric cancer cells were treated with or without FCL (2–8 µM) for 24 h. Total RNA was isolated, and reverse transcription-polymerase chain reaction was performed to detect the expression of MMP-2, MMP-9, TIMP1 and TIMP2 mRNAs. (B) The densitometry of the bands was normalized to the expression of GAPDH and analyzed. *P

Techniques Used: Expressing, Isolation, Reverse Transcription Polymerase Chain Reaction

15) Product Images from "The Treponema denticola Chymotrypsin-Like Protease Dentilisin Induces Matrix Metalloproteinase-2-Dependent Fibronectin Fragmentation in Periodontal Ligament Cells ▿"

Article Title: The Treponema denticola Chymotrypsin-Like Protease Dentilisin Induces Matrix Metalloproteinase-2-Dependent Fibronectin Fragmentation in Periodontal Ligament Cells ▿

Journal: Infection and Immunity

doi: 10.1128/IAI.01001-10

FN degradation is blocked in supernatants of MMP-2 siRNA-transfected PDL cell cultures. Cell-free supernatants from PDL cultures transfected with MMP-2-specific siRNA or scrambled siRNA control were challenged or not challenged with T. denticola 35405
Figure Legend Snippet: FN degradation is blocked in supernatants of MMP-2 siRNA-transfected PDL cell cultures. Cell-free supernatants from PDL cultures transfected with MMP-2-specific siRNA or scrambled siRNA control were challenged or not challenged with T. denticola 35405

Techniques Used: Transfection

MMP-2 activity in 24-h supernatants of PDL cell cultures (PDL) following a 2-h challenge with T. denticola . Gelatin zymogram (top) and Western immunoblot (bottom) probed with an anti-MMP-2 catalytic domain antibody. Lanes: C, PDL no-challenge control;
Figure Legend Snippet: MMP-2 activity in 24-h supernatants of PDL cell cultures (PDL) following a 2-h challenge with T. denticola . Gelatin zymogram (top) and Western immunoblot (bottom) probed with an anti-MMP-2 catalytic domain antibody. Lanes: C, PDL no-challenge control;

Techniques Used: Activity Assay, Western Blot

MMP-2-specific inhibitor blocks MMP-2 activation and inhibits FN fragmentation. Lanes contain PDL culture supernatant alone (PDL) or after 2 h of treatment with T. denticola 35405, washing, and addition of fresh medium (PDL + Td ). ARP101 was added
Figure Legend Snippet: MMP-2-specific inhibitor blocks MMP-2 activation and inhibits FN fragmentation. Lanes contain PDL culture supernatant alone (PDL) or after 2 h of treatment with T. denticola 35405, washing, and addition of fresh medium (PDL + Td ). ARP101 was added

Techniques Used: Activation Assay

16) Product Images from "The Treponema denticola Chymotrypsin-Like Protease Dentilisin Induces Matrix Metalloproteinase-2-Dependent Fibronectin Fragmentation in Periodontal Ligament Cells ▿"

Article Title: The Treponema denticola Chymotrypsin-Like Protease Dentilisin Induces Matrix Metalloproteinase-2-Dependent Fibronectin Fragmentation in Periodontal Ligament Cells ▿

Journal: Infection and Immunity

doi: 10.1128/IAI.01001-10

FN degradation is blocked in supernatants of MMP-2 siRNA-transfected PDL cell cultures. Cell-free supernatants from PDL cultures transfected with MMP-2-specific siRNA or scrambled siRNA control were challenged or not challenged with T. denticola 35405
Figure Legend Snippet: FN degradation is blocked in supernatants of MMP-2 siRNA-transfected PDL cell cultures. Cell-free supernatants from PDL cultures transfected with MMP-2-specific siRNA or scrambled siRNA control were challenged or not challenged with T. denticola 35405

Techniques Used: Transfection

MMP-2 activity in 24-h supernatants of PDL cell cultures (PDL) following a 2-h challenge with T. denticola . Gelatin zymogram (top) and Western immunoblot (bottom) probed with an anti-MMP-2 catalytic domain antibody. Lanes: C, PDL no-challenge control;
Figure Legend Snippet: MMP-2 activity in 24-h supernatants of PDL cell cultures (PDL) following a 2-h challenge with T. denticola . Gelatin zymogram (top) and Western immunoblot (bottom) probed with an anti-MMP-2 catalytic domain antibody. Lanes: C, PDL no-challenge control;

Techniques Used: Activity Assay, Western Blot

MMP-2-specific inhibitor blocks MMP-2 activation and inhibits FN fragmentation. Lanes contain PDL culture supernatant alone (PDL) or after 2 h of treatment with T. denticola 35405, washing, and addition of fresh medium (PDL + Td ). ARP101 was added
Figure Legend Snippet: MMP-2-specific inhibitor blocks MMP-2 activation and inhibits FN fragmentation. Lanes contain PDL culture supernatant alone (PDL) or after 2 h of treatment with T. denticola 35405, washing, and addition of fresh medium (PDL + Td ). ARP101 was added

Techniques Used: Activation Assay

17) Product Images from "The Treponema denticola Chymotrypsin-Like Protease Dentilisin Induces Matrix Metalloproteinase-2-Dependent Fibronectin Fragmentation in Periodontal Ligament Cells ▿"

Article Title: The Treponema denticola Chymotrypsin-Like Protease Dentilisin Induces Matrix Metalloproteinase-2-Dependent Fibronectin Fragmentation in Periodontal Ligament Cells ▿

Journal: Infection and Immunity

doi: 10.1128/IAI.01001-10

FN degradation is blocked in supernatants of MMP-2 siRNA-transfected PDL cell cultures. Cell-free supernatants from PDL cultures transfected with MMP-2-specific siRNA or scrambled siRNA control were challenged or not challenged with T. denticola 35405
Figure Legend Snippet: FN degradation is blocked in supernatants of MMP-2 siRNA-transfected PDL cell cultures. Cell-free supernatants from PDL cultures transfected with MMP-2-specific siRNA or scrambled siRNA control were challenged or not challenged with T. denticola 35405

Techniques Used: Transfection

MMP-2 activity in 24-h supernatants of PDL cell cultures (PDL) following a 2-h challenge with T. denticola . Gelatin zymogram (top) and Western immunoblot (bottom) probed with an anti-MMP-2 catalytic domain antibody. Lanes: C, PDL no-challenge control;
Figure Legend Snippet: MMP-2 activity in 24-h supernatants of PDL cell cultures (PDL) following a 2-h challenge with T. denticola . Gelatin zymogram (top) and Western immunoblot (bottom) probed with an anti-MMP-2 catalytic domain antibody. Lanes: C, PDL no-challenge control;

Techniques Used: Activity Assay, Western Blot

MMP-2-specific inhibitor blocks MMP-2 activation and inhibits FN fragmentation. Lanes contain PDL culture supernatant alone (PDL) or after 2 h of treatment with T. denticola 35405, washing, and addition of fresh medium (PDL + Td ). ARP101 was added
Figure Legend Snippet: MMP-2-specific inhibitor blocks MMP-2 activation and inhibits FN fragmentation. Lanes contain PDL culture supernatant alone (PDL) or after 2 h of treatment with T. denticola 35405, washing, and addition of fresh medium (PDL + Td ). ARP101 was added

Techniques Used: Activation Assay

18) Product Images from "Deficiency of cathepsin S attenuates angiotensin II-induced abdominal aortic aneurysm formation in apolipoprotein E-deficient mice"

Article Title: Deficiency of cathepsin S attenuates angiotensin II-induced abdominal aortic aneurysm formation in apolipoprotein E-deficient mice

Journal: Cardiovascular Research

doi: 10.1093/cvr/cvs263

AAA lesion ECM degradation and protease expression. ( A ) Medial elastin fragmentation grades between Apoe –/– Ctss +/+ and Apoe –/– Ctss –/– mice. Grading keys are shown on the left. ( B ). Sirius red staining showed adventitial collagen contents in AAA lesions. Representative photographs are shown on the right. ( C ) AAA lesion extract JPM labelling to detect active cathepsins. Coomassie staining was used for protein loading control. ( D ) Gelatin gel zymograph. Both active MMP-2 and MMP-9 and their molecular weights are indicated. ( E ). AAA lesion Cat K-positive areas. ( F ) AAA lesion MMP-2-positive areas. Representative graphs of ( E ) and ( F ) are shown on the left. Data represent the mean ± SEM ( n = 10 per group). P
Figure Legend Snippet: AAA lesion ECM degradation and protease expression. ( A ) Medial elastin fragmentation grades between Apoe –/– Ctss +/+ and Apoe –/– Ctss –/– mice. Grading keys are shown on the left. ( B ). Sirius red staining showed adventitial collagen contents in AAA lesions. Representative photographs are shown on the right. ( C ) AAA lesion extract JPM labelling to detect active cathepsins. Coomassie staining was used for protein loading control. ( D ) Gelatin gel zymograph. Both active MMP-2 and MMP-9 and their molecular weights are indicated. ( E ). AAA lesion Cat K-positive areas. ( F ) AAA lesion MMP-2-positive areas. Representative graphs of ( E ) and ( F ) are shown on the left. Data represent the mean ± SEM ( n = 10 per group). P

Techniques Used: Expressing, Mouse Assay, Staining

19) Product Images from "Exercise training reduces fibrosis and matrix metalloproteinase dysregulation in the aging rat heart"

Article Title: Exercise training reduces fibrosis and matrix metalloproteinase dysregulation in the aging rat heart

Journal: The FASEB Journal

doi: 10.1096/fj.10-172924

Protein expression for MMPs pro-MMP-1 ( A ), active MMP-1 ( B ), pro-MMP-2 ( C ), and active MMP-2 ( D ) using Western immunoblotting in LV samples from YS, YE, OS, and OE FBNF1 rats. C, control. Data are expressed as means ± se . Matched controls or GAPDH
Figure Legend Snippet: Protein expression for MMPs pro-MMP-1 ( A ), active MMP-1 ( B ), pro-MMP-2 ( C ), and active MMP-2 ( D ) using Western immunoblotting in LV samples from YS, YE, OS, and OE FBNF1 rats. C, control. Data are expressed as means ± se . Matched controls or GAPDH

Techniques Used: Expressing, Western Blot

20) Product Images from "Exercise training reduces fibrosis and matrix metalloproteinase dysregulation in the aging rat heart"

Article Title: Exercise training reduces fibrosis and matrix metalloproteinase dysregulation in the aging rat heart

Journal: The FASEB Journal

doi: 10.1096/fj.10-172924

Protein expression for MMPs pro-MMP-1 ( A ), active MMP-1 ( B ), pro-MMP-2 ( C ), and active MMP-2 ( D ) using Western immunoblotting in LV samples from YS, YE, OS, and OE FBNF1 rats. C, control. Data are expressed as means ± se . Matched controls or GAPDH
Figure Legend Snippet: Protein expression for MMPs pro-MMP-1 ( A ), active MMP-1 ( B ), pro-MMP-2 ( C ), and active MMP-2 ( D ) using Western immunoblotting in LV samples from YS, YE, OS, and OE FBNF1 rats. C, control. Data are expressed as means ± se . Matched controls or GAPDH

Techniques Used: Expressing, Western Blot

21) Product Images from "CXCR3 activation by lentivirus infection suppresses neuronal autophagy: neuroprotective effects of antiretroviral therapy"

Article Title: CXCR3 activation by lentivirus infection suppresses neuronal autophagy: neuroprotective effects of antiretroviral therapy

Journal: The FASEB Journal

doi: 10.1096/fj.08-128819

Brain expression of CXCL12, MMP-2, and CXCR3 in FIV infection. A ) Immunoblotting showed increased full-length (1-67) and cleaved (5-67) CXCL12 in brains of FIV − compared with mock-infected animals. B ) CXCL12, CXCL12(5-67), MMP-2, and CXCR3 immunoreactivities were increased in brains of FIV + animals but were suppressed by concurrent ddI treatment. C ) MMP-2 immunoreactivity (IR) showed minimal induction in FIV + animals with and without ddI treatment. D , E ) CXCL12(1-67) ( D ) and CXCL12(5-67) ( E ) were induced by FIV infection, but these changes were reversed by ddI treatment. F ) CXCR3 showed minimal induction of both immunoreactive bands in FIV infection and was not affected by ddI treatment. * P
Figure Legend Snippet: Brain expression of CXCL12, MMP-2, and CXCR3 in FIV infection. A ) Immunoblotting showed increased full-length (1-67) and cleaved (5-67) CXCL12 in brains of FIV − compared with mock-infected animals. B ) CXCL12, CXCL12(5-67), MMP-2, and CXCR3 immunoreactivities were increased in brains of FIV + animals but were suppressed by concurrent ddI treatment. C ) MMP-2 immunoreactivity (IR) showed minimal induction in FIV + animals with and without ddI treatment. D , E ) CXCL12(1-67) ( D ) and CXCL12(5-67) ( E ) were induced by FIV infection, but these changes were reversed by ddI treatment. F ) CXCR3 showed minimal induction of both immunoreactive bands in FIV infection and was not affected by ddI treatment. * P

Techniques Used: Expressing, Infection

Neurobehavioral performance, viral burden, and neuroinflammation in FIV infection. A ) FIV-infected animals (FIV+) exhibit greater neurobehavioral deficits than mock-infected controls (FIV−), while ddI treatment reversed neurobehavioral deficits in FIV-infected animals (FIV+/ddI) and had no effects on mock-infected animals. B ) ddI treatment suppressed viral load in plasma of FIV-infected animals. C ) Glycoprotein, F4/80 , expressed in activated myeloid cells showed increased transcript abundance in FIV-infected animals, which was reversed by ddI treatment. D ) CXCL12 transcript levels were higher in FIV-infected animals but were not reduced by ddI treatment. E ) MMP-2 transcripts were unregulated in FIV-infected animals but were suppressed with ddI treatment. F ) GFAP transcriptional activity was not affected by FIV infection or ddI treatment. * P
Figure Legend Snippet: Neurobehavioral performance, viral burden, and neuroinflammation in FIV infection. A ) FIV-infected animals (FIV+) exhibit greater neurobehavioral deficits than mock-infected controls (FIV−), while ddI treatment reversed neurobehavioral deficits in FIV-infected animals (FIV+/ddI) and had no effects on mock-infected animals. B ) ddI treatment suppressed viral load in plasma of FIV-infected animals. C ) Glycoprotein, F4/80 , expressed in activated myeloid cells showed increased transcript abundance in FIV-infected animals, which was reversed by ddI treatment. D ) CXCL12 transcript levels were higher in FIV-infected animals but were not reduced by ddI treatment. E ) MMP-2 transcripts were unregulated in FIV-infected animals but were suppressed with ddI treatment. F ) GFAP transcriptional activity was not affected by FIV infection or ddI treatment. * P

Techniques Used: Infection, Activity Assay

Suppression of neuronal autophagy and its regulation by antiretroviral therapy. ddI suppressed viral burden in the peripheral circulation, diminishing leukocyte activation and CNS entry with an ensuing reduction in MMP-2 production and its actions, thereby preventing the induction of CXCL12(5-12) with its adverse effects on neuronal autophagy and survival.
Figure Legend Snippet: Suppression of neuronal autophagy and its regulation by antiretroviral therapy. ddI suppressed viral burden in the peripheral circulation, diminishing leukocyte activation and CNS entry with an ensuing reduction in MMP-2 production and its actions, thereby preventing the induction of CXCL12(5-12) with its adverse effects on neuronal autophagy and survival.

Techniques Used: Activation Assay

22) Product Images from "MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer"

Article Title: MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.13283

MMP ‐13 and  MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS  double‐staining in H460 xenografts showed decreased  VM  but increased  EDV  numbers (Bar = 100 μm). The black arrow shows  VM  formation. The red arrow shows the  EDV s. ( C ) The expression levels of  MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the  MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm).  WB  showed  MMP ‐13 gradually increasing, but Ln‐5 and  EGFR  showed a decreasing trend with tumour growth.  MMP ‐2 expression was observed at different tumour growth stages.
Figure Legend Snippet: MMP ‐13 and MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS double‐staining in H460 xenografts showed decreased VM but increased EDV numbers (Bar = 100 μm). The black arrow shows VM formation. The red arrow shows the EDV s. ( C ) The expression levels of MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm). WB showed MMP ‐13 gradually increasing, but Ln‐5 and EGFR showed a decreasing trend with tumour growth. MMP ‐2 expression was observed at different tumour growth stages.

Techniques Used: Expressing, Double Staining, Western Blot

Cleavage of Ln‐5 by  MMP ‐13 was detected with a silver staining kit and  LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by  MMP ‐2 and  MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12%  SDS ‐ PAGE  gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain.  MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment.  MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B )  LC ‐ MS / MS  detection showed that the 20 kD fragment generated by  MMP ‐13 was part of the Ln‐5γ2 chain. ( C )  MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain  III  and IV domain.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐13 was detected with a silver staining kit and LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by MMP ‐2 and MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12% SDS ‐ PAGE gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain. MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment. MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B ) LC ‐ MS / MS detection showed that the 20 kD fragment generated by MMP ‐13 was part of the Ln‐5γ2 chain. ( C ) MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain III and IV domain.

Techniques Used: Silver Staining, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, SDS Page, Generated, Molecular Weight

Cleavage of Ln‐5 by  MMP ‐2 or  MMP ‐13 affected  EGFR  and F‐actin expression. ( A ) The  WB  results show that treatment with  MMP ‐2 Ln‐5 cleavage fragments enhanced the  EGFR , F‐actin and  EGFR  downstream targets Raf,  ERK  and  AKT  protein levels in cells, but the levels were reduced in the  MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of  EGFR  and F‐actin filaments was observed in the  MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the  MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐2 or MMP ‐13 affected EGFR and F‐actin expression. ( A ) The WB results show that treatment with MMP ‐2 Ln‐5 cleavage fragments enhanced the EGFR , F‐actin and EGFR downstream targets Raf, ERK and AKT protein levels in cells, but the levels were reduced in the MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of EGFR and F‐actin filaments was observed in the MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.

Techniques Used: Expressing, Western Blot, Immunofluorescence, Staining

VM  and the expression of  MMP ‐13,  MMP ‐2, Ln‐5 and  EGFR  in  LCLC  tissues. ( A ) Representative images of the presence of  VM  in human  LCLC  tissues ( CD 34/ PAS  double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both  CD 34 and  PAS . The black arrows show  VM  channels in which  PAS ‐positive materials and red blood cells (red arrow) are observed. ( B )  VM ‐positive tissues exhibited significantly reduced  MMP ‐13 expression, and  VM ‐negative tissues exhibited significantly increased  MMP ‐13 expression ( P  = 0.005). In contrast,  VM ‐positive tissues exhibited significantly reduced  MMP ‐2 expression, and  VM ‐negative tissue exhibited significantly increased  MMP ‐2 expression. There was no significant correlation between  MMP ‐13 and  MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and  EGFR  can be observed in the  LCLC  samples with  MMP ‐13‐positive tissues compared with expression in  VM ‐negative tissues ( P
Figure Legend Snippet: VM and the expression of MMP ‐13, MMP ‐2, Ln‐5 and EGFR in LCLC tissues. ( A ) Representative images of the presence of VM in human LCLC tissues ( CD 34/ PAS double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both CD 34 and PAS . The black arrows show VM channels in which PAS ‐positive materials and red blood cells (red arrow) are observed. ( B ) VM ‐positive tissues exhibited significantly reduced MMP ‐13 expression, and VM ‐negative tissues exhibited significantly increased MMP ‐13 expression ( P  = 0.005). In contrast, VM ‐positive tissues exhibited significantly reduced MMP ‐2 expression, and VM ‐negative tissue exhibited significantly increased MMP ‐2 expression. There was no significant correlation between MMP ‐13 and MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and EGFR can be observed in the LCLC samples with MMP ‐13‐positive tissues compared with expression in VM ‐negative tissues ( P

Techniques Used: Expressing, Double Staining

23) Product Images from "MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer"

Article Title: MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.13283

MMP ‐13 and  MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS  double‐staining in H460 xenografts showed decreased  VM  but increased  EDV  numbers (Bar = 100 μm). The black arrow shows  VM  formation. The red arrow shows the  EDV s. ( C ) The expression levels of  MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the  MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm).  WB  showed  MMP ‐13 gradually increasing, but Ln‐5 and  EGFR  showed a decreasing trend with tumour growth.  MMP ‐2 expression was observed at different tumour growth stages.
Figure Legend Snippet: MMP ‐13 and MMP ‐2 expression in different tumour stages. ( A ) Tumour volume at different weeks. ( B ) Endomucin/ PAS double‐staining in H460 xenografts showed decreased VM but increased EDV numbers (Bar = 100 μm). The black arrow shows VM formation. The red arrow shows the EDV s. ( C ) The expression levels of MMP ‐13 showed a gradually increasing trend with tumour growth. Meanwhile, no significant difference in the MMP ‐2 expression was observed at different tumour growth stages (Bar = 100 μm). WB showed MMP ‐13 gradually increasing, but Ln‐5 and EGFR showed a decreasing trend with tumour growth. MMP ‐2 expression was observed at different tumour growth stages.

Techniques Used: Expressing, Double Staining, Western Blot

Cleavage of Ln‐5 by  MMP ‐13 was detected with a silver staining kit and  LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by  MMP ‐2 and  MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12%  SDS ‐ PAGE  gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain.  MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment.  MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B )  LC ‐ MS / MS  detection showed that the 20 kD fragment generated by  MMP ‐13 was part of the Ln‐5γ2 chain. ( C )  MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain  III  and IV domain.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐13 was detected with a silver staining kit and LC ‐ MS / MS . ( A ) Human Ln‐5 was cleaved by MMP ‐2 and MMP ‐13 at 37°C for 6 hrs, and the cleavage fragments were separated on a 12% SDS ‐ PAGE gel and detected with a silver staining kit. The left lane shows the 140‐ and 100‐ kD a forms of the intact Ln‐5γ2 chain. MMP ‐2 generated an 80 kD Ln‐5γ2x fragment and a very faint 66 kD fragment. MMP ‐13 further generated low molecular weight fragments that were approximately 20 kD. ( B ) LC ‐ MS / MS detection showed that the 20 kD fragment generated by MMP ‐13 was part of the Ln‐5γ2 chain. ( C ) MMP ‐13 cleaved the Ln‐5γ2 chain at Lys‐Cys (540–541) and Arg‐Leu (694–695). This fragment belongs to the Ln‐5γ2 chain III and IV domain.

Techniques Used: Silver Staining, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, SDS Page, Generated, Molecular Weight

Cleavage of Ln‐5 by  MMP ‐2 or  MMP ‐13 affected  EGFR  and F‐actin expression. ( A ) The  WB  results show that treatment with  MMP ‐2 Ln‐5 cleavage fragments enhanced the  EGFR , F‐actin and  EGFR  downstream targets Raf,  ERK  and  AKT  protein levels in cells, but the levels were reduced in the  MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of  EGFR  and F‐actin filaments was observed in the  MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the  MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.
Figure Legend Snippet: Cleavage of Ln‐5 by MMP ‐2 or MMP ‐13 affected EGFR and F‐actin expression. ( A ) The WB results show that treatment with MMP ‐2 Ln‐5 cleavage fragments enhanced the EGFR , F‐actin and EGFR downstream targets Raf, ERK and AKT protein levels in cells, but the levels were reduced in the MMP ‐13‐Ln‐5 group. Vimentin and α‐tubulin levels were not obviously changed in either group. ( B ) Immunofluorescence staining was performed, and higher co‐expression of EGFR and F‐actin filaments was observed in the MMP ‐2 + Ln‐5 group, and the arrangement of the F‐actin cytoskeleton was dramatically changed compared with that of the MMP ‐13 + Ln‐5 group. The expression of vimentin and α‐tubulin was not different between these two treatment groups in both H460 and H661 cells.

Techniques Used: Expressing, Western Blot, Immunofluorescence, Staining

VM  and the expression of  MMP ‐13,  MMP ‐2, Ln‐5 and  EGFR  in  LCLC  tissues. ( A ) Representative images of the presence of  VM  in human  LCLC  tissues ( CD 34/ PAS  double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both  CD 34 and  PAS . The black arrows show  VM  channels in which  PAS ‐positive materials and red blood cells (red arrow) are observed. ( B )  VM ‐positive tissues exhibited significantly reduced  MMP ‐13 expression, and  VM ‐negative tissues exhibited significantly increased  MMP ‐13 expression ( P  = 0.005). In contrast,  VM ‐positive tissues exhibited significantly reduced  MMP ‐2 expression, and  VM ‐negative tissue exhibited significantly increased  MMP ‐2 expression. There was no significant correlation between  MMP ‐13 and  MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and  EGFR  can be observed in the  LCLC  samples with  MMP ‐13‐positive tissues compared with expression in  VM ‐negative tissues ( P
Figure Legend Snippet: VM and the expression of MMP ‐13, MMP ‐2, Ln‐5 and EGFR in LCLC tissues. ( A ) Representative images of the presence of VM in human LCLC tissues ( CD 34/ PAS double‐staining). The yellow arrow shows that the endothelial‐dependent vessel was positive for both CD 34 and PAS . The black arrows show VM channels in which PAS ‐positive materials and red blood cells (red arrow) are observed. ( B ) VM ‐positive tissues exhibited significantly reduced MMP ‐13 expression, and VM ‐negative tissues exhibited significantly increased MMP ‐13 expression ( P  = 0.005). In contrast, VM ‐positive tissues exhibited significantly reduced MMP ‐2 expression, and VM ‐negative tissue exhibited significantly increased MMP ‐2 expression. There was no significant correlation between MMP ‐13 and MMP ‐2 ( P  = 0.301). ( C ). Significantly reduced expression of Ln‐5 and EGFR can be observed in the LCLC samples with MMP ‐13‐positive tissues compared with expression in VM ‐negative tissues ( P

Techniques Used: Expressing, Double Staining

24) Product Images from "Propofol suppresses proliferation and invasion of glioma cells by upregulating microRNA-218 expression"

Article Title: Propofol suppresses proliferation and invasion of glioma cells by upregulating microRNA-218 expression

Journal: Molecular Medicine Reports

doi: 10.3892/mmr.2015.4014

Western blot analysis showed that propofol treatment downregulated matrix metalloproteinase-2 (MMP-2) expression. (A) The protein levels of MMP-2 in U373 cells were markedly decreased following propofol treatment. (B) Statistical analysis of MMP-2 protein levels. *P
Figure Legend Snippet: Western blot analysis showed that propofol treatment downregulated matrix metalloproteinase-2 (MMP-2) expression. (A) The protein levels of MMP-2 in U373 cells were markedly decreased following propofol treatment. (B) Statistical analysis of MMP-2 protein levels. *P

Techniques Used: Western Blot, Expressing

Overexpression of microRNA (miR)-218 can suppress matrix metalloproteinase (MMP)-2 expression. (A) Transfection of U373 human glioma cells with miR-218 precursor significantly elevated the expression levels of miR-218. (B) Western blot analysis indicated that transfection with miR-218 precursor decreased MMP-2 protein expression levels. *P
Figure Legend Snippet: Overexpression of microRNA (miR)-218 can suppress matrix metalloproteinase (MMP)-2 expression. (A) Transfection of U373 human glioma cells with miR-218 precursor significantly elevated the expression levels of miR-218. (B) Western blot analysis indicated that transfection with miR-218 precursor decreased MMP-2 protein expression levels. *P

Techniques Used: Over Expression, Expressing, Transfection, Western Blot

25) Product Images from "Nanoparticle analysis sheds budding insights into genetic drivers of extracellular vesicle biogenesis"

Article Title: Nanoparticle analysis sheds budding insights into genetic drivers of extracellular vesicle biogenesis

Journal: Journal of Extracellular Vesicles

doi: 10.3402/jev.v5.31295

Biochemical analyses of extracellular vesicles (EVs) demonstrate relative secretion levels across cancer cells. Quantity of particles per cell from SF268 and MCF7 cells following (a) PEG precipitation and (b) iodixanol gradient purification. (c) HEK293 cell lysate (CL) and representative EV lysates from cancer cells in the NCI-60 panel loaded by equal volume. EV lysates are enriched for exosomal markers Alix, TSG101, CD63 and CD81; microvesicle marker MMP-2; and positive for EV marker HSC70. Calnexin is found predominately in CL while minimal to undetectable levels are found in EV samples. (d) Quantification of relative EV levels from MCF7, SK-MEL-5 and OVCAR-5 cells by esterase activity.
Figure Legend Snippet: Biochemical analyses of extracellular vesicles (EVs) demonstrate relative secretion levels across cancer cells. Quantity of particles per cell from SF268 and MCF7 cells following (a) PEG precipitation and (b) iodixanol gradient purification. (c) HEK293 cell lysate (CL) and representative EV lysates from cancer cells in the NCI-60 panel loaded by equal volume. EV lysates are enriched for exosomal markers Alix, TSG101, CD63 and CD81; microvesicle marker MMP-2; and positive for EV marker HSC70. Calnexin is found predominately in CL while minimal to undetectable levels are found in EV samples. (d) Quantification of relative EV levels from MCF7, SK-MEL-5 and OVCAR-5 cells by esterase activity.

Techniques Used: Purification, Marker, Activity Assay

26) Product Images from "Maternal hypoxia alters matrix metalloproteinase expression patterns and causes cardiac remodeling in fetal and neonatal rats"

Article Title: Maternal hypoxia alters matrix metalloproteinase expression patterns and causes cardiac remodeling in fetal and neonatal rats

Journal: American Journal of Physiology - Heart and Circulatory Physiology

doi: 10.1152/ajpheart.00356.2011

The effect of maternal hypoxia on the activity of MMP-2 and MMP-9. Hearts were isolated from E21 and PD7 rats in the control and hypoxic groups. The activities of MMP-2 and MMP-9 were determined by gelatin zymography. Clear bands indicate positive MMP
Figure Legend Snippet: The effect of maternal hypoxia on the activity of MMP-2 and MMP-9. Hearts were isolated from E21 and PD7 rats in the control and hypoxic groups. The activities of MMP-2 and MMP-9 were determined by gelatin zymography. Clear bands indicate positive MMP

Techniques Used: Activity Assay, Isolation, Zymography

27) Product Images from "CXCR3 activation by lentivirus infection suppresses neuronal autophagy: neuroprotective effects of antiretroviral therapy"

Article Title: CXCR3 activation by lentivirus infection suppresses neuronal autophagy: neuroprotective effects of antiretroviral therapy

Journal: The FASEB Journal

doi: 10.1096/fj.08-128819

Brain expression of CXCL12, MMP-2, and CXCR3 in FIV infection. A ) Immunoblotting showed increased full-length (1-67) and cleaved (5-67) CXCL12 in brains of FIV − compared with mock-infected animals. B ) CXCL12, CXCL12(5-67), MMP-2, and CXCR3 immunoreactivities were increased in brains of FIV + animals but were suppressed by concurrent ddI treatment. C ) MMP-2 immunoreactivity (IR) showed minimal induction in FIV + animals with and without ddI treatment. D , E ) CXCL12(1-67) ( D ) and CXCL12(5-67) ( E ) were induced by FIV infection, but these changes were reversed by ddI treatment. F ) CXCR3 showed minimal induction of both immunoreactive bands in FIV infection and was not affected by ddI treatment. * P
Figure Legend Snippet: Brain expression of CXCL12, MMP-2, and CXCR3 in FIV infection. A ) Immunoblotting showed increased full-length (1-67) and cleaved (5-67) CXCL12 in brains of FIV − compared with mock-infected animals. B ) CXCL12, CXCL12(5-67), MMP-2, and CXCR3 immunoreactivities were increased in brains of FIV + animals but were suppressed by concurrent ddI treatment. C ) MMP-2 immunoreactivity (IR) showed minimal induction in FIV + animals with and without ddI treatment. D , E ) CXCL12(1-67) ( D ) and CXCL12(5-67) ( E ) were induced by FIV infection, but these changes were reversed by ddI treatment. F ) CXCR3 showed minimal induction of both immunoreactive bands in FIV infection and was not affected by ddI treatment. * P

Techniques Used: Expressing, Infection

Neurobehavioral performance, viral burden, and neuroinflammation in FIV infection. A ) FIV-infected animals (FIV+) exhibit greater neurobehavioral deficits than mock-infected controls (FIV−), while ddI treatment reversed neurobehavioral deficits in FIV-infected animals (FIV+/ddI) and had no effects on mock-infected animals. B ) ddI treatment suppressed viral load in plasma of FIV-infected animals. C ) Glycoprotein, F4/80 , expressed in activated myeloid cells showed increased transcript abundance in FIV-infected animals, which was reversed by ddI treatment. D ) CXCL12 transcript levels were higher in FIV-infected animals but were not reduced by ddI treatment. E ) MMP-2 transcripts were unregulated in FIV-infected animals but were suppressed with ddI treatment. F ) GFAP transcriptional activity was not affected by FIV infection or ddI treatment. * P
Figure Legend Snippet: Neurobehavioral performance, viral burden, and neuroinflammation in FIV infection. A ) FIV-infected animals (FIV+) exhibit greater neurobehavioral deficits than mock-infected controls (FIV−), while ddI treatment reversed neurobehavioral deficits in FIV-infected animals (FIV+/ddI) and had no effects on mock-infected animals. B ) ddI treatment suppressed viral load in plasma of FIV-infected animals. C ) Glycoprotein, F4/80 , expressed in activated myeloid cells showed increased transcript abundance in FIV-infected animals, which was reversed by ddI treatment. D ) CXCL12 transcript levels were higher in FIV-infected animals but were not reduced by ddI treatment. E ) MMP-2 transcripts were unregulated in FIV-infected animals but were suppressed with ddI treatment. F ) GFAP transcriptional activity was not affected by FIV infection or ddI treatment. * P

Techniques Used: Infection, Activity Assay

Suppression of neuronal autophagy and its regulation by antiretroviral therapy. ddI suppressed viral burden in the peripheral circulation, diminishing leukocyte activation and CNS entry with an ensuing reduction in MMP-2 production and its actions, thereby preventing the induction of CXCL12(5-12) with its adverse effects on neuronal autophagy and survival.
Figure Legend Snippet: Suppression of neuronal autophagy and its regulation by antiretroviral therapy. ddI suppressed viral burden in the peripheral circulation, diminishing leukocyte activation and CNS entry with an ensuing reduction in MMP-2 production and its actions, thereby preventing the induction of CXCL12(5-12) with its adverse effects on neuronal autophagy and survival.

Techniques Used: Activation Assay

28) Product Images from "Lipid-Soluble Ginseng Extract Inhibits Invasion and Metastasis of B16F10 Melanoma Cells"

Article Title: Lipid-Soluble Ginseng Extract Inhibits Invasion and Metastasis of B16F10 Melanoma Cells

Journal: Journal of Medicinal Food

doi: 10.1089/jmf.2013.3138

Effects of LSGE on the activity and expression of MMP-2 in B16F10 melanoma cells. The cells were treated either with LSGE at the concentration of 3 μg/mL or with the V.C. The band images are representative of three independent experiments.
Figure Legend Snippet: Effects of LSGE on the activity and expression of MMP-2 in B16F10 melanoma cells. The cells were treated either with LSGE at the concentration of 3 μg/mL or with the V.C. The band images are representative of three independent experiments.

Techniques Used: Activity Assay, Expressing, Concentration Assay

29) Product Images from "Lipid-Soluble Ginseng Extract Inhibits Invasion and Metastasis of B16F10 Melanoma Cells"

Article Title: Lipid-Soluble Ginseng Extract Inhibits Invasion and Metastasis of B16F10 Melanoma Cells

Journal: Journal of Medicinal Food

doi: 10.1089/jmf.2013.3138

Effects of LSGE on the activity and expression of MMP-2 in B16F10 melanoma cells. The cells were treated either with LSGE at the concentration of 3 μg/mL or with the V.C. The band images are representative of three independent experiments.
Figure Legend Snippet: Effects of LSGE on the activity and expression of MMP-2 in B16F10 melanoma cells. The cells were treated either with LSGE at the concentration of 3 μg/mL or with the V.C. The band images are representative of three independent experiments.

Techniques Used: Activity Assay, Expressing, Concentration Assay

30) Product Images from "Aurora-A modulates MMP-2 expression via AKT/NF-κB pathway in esophageal squamous cell carcinoma cells"

Article Title: Aurora-A modulates MMP-2 expression via AKT/NF-κB pathway in esophageal squamous cell carcinoma cells

Journal: Acta Biochimica et Biophysica Sinica

doi: 10.1093/abbs/gmw030

ESCC cell invasion is promoted by Aurora-A overexpression and attenuated by the MMP-2 inhibitor I (A) The levels of fusion protein GFP-Aurora-A and MMP-2 were detected by western blot analysis after stable transfection of GFP-Aurora-A expression
Figure Legend Snippet: ESCC cell invasion is promoted by Aurora-A overexpression and attenuated by the MMP-2 inhibitor I (A) The levels of fusion protein GFP-Aurora-A and MMP-2 were detected by western blot analysis after stable transfection of GFP-Aurora-A expression

Techniques Used: Over Expression, Western Blot, Stable Transfection, Expressing

Expression of Aurora-A is positively correlated with expression of MMP - 2 in ESCC
Figure Legend Snippet: Expression of Aurora-A is positively correlated with expression of MMP - 2 in ESCC

Techniques Used: Expressing

Representative immunohistochemical stainings of MMP-2 in ESCC and normal adjacent tissues on TMA (A) In normal adjacent esophageal tissues, MMP-2 showed negative cytoplasmic and weak nuclear staining. In ESCC tissues, MMP-2 staining was weakly
Figure Legend Snippet: Representative immunohistochemical stainings of MMP-2 in ESCC and normal adjacent tissues on TMA (A) In normal adjacent esophageal tissues, MMP-2 showed negative cytoplasmic and weak nuclear staining. In ESCC tissues, MMP-2 staining was weakly

Techniques Used: Immunohistochemistry, Staining

Aurora-A overexpression upregulates MMP-2 expression via AKT/NF-κB activation in ESCC cells (A) The nuclear protein level of NF-κB p65 was detected by western blot analysis in Aurora-A-overexpressing and control cells. (B) Cells
Figure Legend Snippet: Aurora-A overexpression upregulates MMP-2 expression via AKT/NF-κB activation in ESCC cells (A) The nuclear protein level of NF-κB p65 was detected by western blot analysis in Aurora-A-overexpressing and control cells. (B) Cells

Techniques Used: Over Expression, Expressing, Activation Assay, Western Blot

Expressions of Aurora-A and MMP-2 proteins in ESCC tissue
Figure Legend Snippet: Expressions of Aurora-A and MMP-2 proteins in ESCC tissue

Techniques Used:

Expressions of Aurora-A and MMP-2 proteins as well as cell invasion capability in ESCC cell lines (A) The expression levels of Aurora-A and MMP-2 were detected by western blot analysis in KYSE150 and EC9706 cells. (B) The relative Aurora-A and
Figure Legend Snippet: Expressions of Aurora-A and MMP-2 proteins as well as cell invasion capability in ESCC cell lines (A) The expression levels of Aurora-A and MMP-2 were detected by western blot analysis in KYSE150 and EC9706 cells. (B) The relative Aurora-A and

Techniques Used: Expressing, Western Blot

31) Product Images from "Expression of tissue inhibitor of matrix metalloproteinases-1 during aging in rat liver"

Article Title: Expression of tissue inhibitor of matrix metalloproteinases-1 during aging in rat liver

Journal: World Journal of Gastroenterology : WJG

doi: 10.3748/wjg.v11.i24.3696

Protein expressions of TIMP-1 and MMP-2, MMP-9 in rat livers (Western blot).
Figure Legend Snippet: Protein expressions of TIMP-1 and MMP-2, MMP-9 in rat livers (Western blot).

Techniques Used: Western Blot

32) Product Images from "Original Research: ACE2 activator associated with physical exercise potentiates the reduction of pulmonary fibrosis"

Article Title: Original Research: ACE2 activator associated with physical exercise potentiates the reduction of pulmonary fibrosis

Journal: Experimental Biology and Medicine

doi: 10.1177/1535370216665174

Correlation between the fibrous connective tissue and the other results obtained in this study. (a) Strong negative correlation between pulmonary fibrosis tissue area (µm 2 ) and functional capacity (minutes); (b) Strong positive correlation between pulmonary fibrosis tissue area (µm 2 ) and TGF-β 1 area (µm 2 ); (c) Strong positive correlation between pulmonary fibrosis tissue area (µm 2 ) and the expression of beta-prolyl-4-hydroxylase (µm 2 ); (d) Strong negative correlation between pulmonary fibrosis tissue area (µm 2 ) and MMP-2 area (µm 2 ). Pearson’s r or Spearman r was used to correlate the different variables
Figure Legend Snippet: Correlation between the fibrous connective tissue and the other results obtained in this study. (a) Strong negative correlation between pulmonary fibrosis tissue area (µm 2 ) and functional capacity (minutes); (b) Strong positive correlation between pulmonary fibrosis tissue area (µm 2 ) and TGF-β 1 area (µm 2 ); (c) Strong positive correlation between pulmonary fibrosis tissue area (µm 2 ) and the expression of beta-prolyl-4-hydroxylase (µm 2 ); (d) Strong negative correlation between pulmonary fibrosis tissue area (µm 2 ) and MMP-2 area (µm 2 ). Pearson’s r or Spearman r was used to correlate the different variables

Techniques Used: Functional Assay, Expressing

33) Product Images from "Isorhapontigenin (ISO) inhibits invasive bladder cancer (BC) formation in vivo and human BC invasion in vitro by targeting STAT1/FOXO1 Axis"

Article Title: Isorhapontigenin (ISO) inhibits invasive bladder cancer (BC) formation in vivo and human BC invasion in vitro by targeting STAT1/FOXO1 Axis

Journal: Cancer prevention research (Philadelphia, Pa.)

doi: 10.1158/1940-6207.CAPR-15-0338

ISO reversed the BBN-induced down-regulation of FOXO1 and up-regulation of MMP-2 in mice Mice were divided into vehicle-treated control group (n=12), BBN-treated group (n=12), and BBN combined with ISO-treated group (n=12). (A) IHC-P staining by antibodies specific against FOXO1 and MMP-2 were performed. FOXO1 (B) and MMP-2 (C) protein expression levels were analyzed by calculating the integrated optical density per stained area (IOD/area) using Image-Pro Plus version 6.0. Results are the means ± SD of 12 mice in each group. Symbol “*” indicates a significant difference between vehicle control group and BBN-treated group ( P
Figure Legend Snippet: ISO reversed the BBN-induced down-regulation of FOXO1 and up-regulation of MMP-2 in mice Mice were divided into vehicle-treated control group (n=12), BBN-treated group (n=12), and BBN combined with ISO-treated group (n=12). (A) IHC-P staining by antibodies specific against FOXO1 and MMP-2 were performed. FOXO1 (B) and MMP-2 (C) protein expression levels were analyzed by calculating the integrated optical density per stained area (IOD/area) using Image-Pro Plus version 6.0. Results are the means ± SD of 12 mice in each group. Symbol “*” indicates a significant difference between vehicle control group and BBN-treated group ( P

Techniques Used: Mouse Assay, Immunohistochemistry, Staining, Expressing

ISO inhibited BC cell invasion through down-regulation of MMP-2 in a FOXO1-denpendent manner UMUC3 (A) and T24T (B) cells were treated with either vehicle or ISO as the indicated concentrations for 18 hours. The protein level of MMP-2 was determined by Western blotting, and GAPDH was used as protein loading control. (C) T24T cells were treated with either vehicle or the indicated concentrations of ISO for 18 hours. The mmp-2 and mmp-9 mRNA levels were evaluated by RT-PCR, and gapdh mRNA was used as the internal loading control. (D) T24T cells were stably transfected with MMP-2 promoter-driven luciferase reporter and the stable transfectants were treated with 20 μM of ISO for the indicated times. Dual-Luciferase Reporter Assay System was used to detect the Luciferase activity. Results are the means ± SD of triplicates. Symbol “*” indicates a significant difference between vehicle control and ISO-treated groups ( P
Figure Legend Snippet: ISO inhibited BC cell invasion through down-regulation of MMP-2 in a FOXO1-denpendent manner UMUC3 (A) and T24T (B) cells were treated with either vehicle or ISO as the indicated concentrations for 18 hours. The protein level of MMP-2 was determined by Western blotting, and GAPDH was used as protein loading control. (C) T24T cells were treated with either vehicle or the indicated concentrations of ISO for 18 hours. The mmp-2 and mmp-9 mRNA levels were evaluated by RT-PCR, and gapdh mRNA was used as the internal loading control. (D) T24T cells were stably transfected with MMP-2 promoter-driven luciferase reporter and the stable transfectants were treated with 20 μM of ISO for the indicated times. Dual-Luciferase Reporter Assay System was used to detect the Luciferase activity. Results are the means ± SD of triplicates. Symbol “*” indicates a significant difference between vehicle control and ISO-treated groups ( P

Techniques Used: Western Blot, Reverse Transcription Polymerase Chain Reaction, Stable Transfection, Transfection, Luciferase, Reporter Assay, Activity Assay

34) Product Images from "Anti-proliferative effect of olmesartan on Tenon's capsule fibroblasts"

Article Title: Anti-proliferative effect of olmesartan on Tenon's capsule fibroblasts

Journal: International Journal of Ophthalmology

doi: 10.18240/ijo.2016.05.05

Olmesartan treated-eye presents with lower MMP-2 expression by means of mean density in each group comparing with the controlled eye.
Figure Legend Snippet: Olmesartan treated-eye presents with lower MMP-2 expression by means of mean density in each group comparing with the controlled eye.

Techniques Used: Expressing

The immunohistochemical pictures show the expression of MMP-2 in conjunctiva and subconjunctival tissue of 10×40 magnification
Figure Legend Snippet: The immunohistochemical pictures show the expression of MMP-2 in conjunctiva and subconjunctival tissue of 10×40 magnification

Techniques Used: Immunohistochemistry, Expressing

35) Product Images from "Chalcone flavokawain A attenuates TGF‐β1‐induced fibrotic pathology via inhibition of ROS/Smad3 signaling pathways and induction of Nrf2/ ARE‐mediated antioxidant genes in vascular smooth muscle cells, et al. Chalcone flavokawain A attenuates TGF‐β1‐induced fibrotic pathology via inhibition of ROS/Smad3 signaling pathways and induction of Nrf2/ARE‐mediated antioxidant genes in vascular smooth muscle cells"

Article Title: Chalcone flavokawain A attenuates TGF‐β1‐induced fibrotic pathology via inhibition of ROS/Smad3 signaling pathways and induction of Nrf2/ ARE‐mediated antioxidant genes in vascular smooth muscle cells, et al. Chalcone flavokawain A attenuates TGF‐β1‐induced fibrotic pathology via inhibition of ROS/Smad3 signaling pathways and induction of Nrf2/ARE‐mediated antioxidant genes in vascular smooth muscle cells

Journal: Journal of Cellular and Molecular Medicine

doi: 10.1111/jcmm.13973

FKA  down‐regulates  MMP ‐9/‐2 and up‐regulates  TIMP ‐1 expressions in  TGF ‐β1‐activated A7r5 cells. A‐C, Cells were preincubated with  FKA  (2‐30 μM) for 2 h and then stimulated with or without  TGF ‐β1 (10 ng/ mL ) for 24 h. Western blotting was performed to analyse (A)  MMP ‐9, (B)  MMP ‐2 and (C)  TIMP ‐1 protein levels. Relative changes in protein intensities were quantified using AlphaEaseFc 4.0 software and presented as histograms, with controls set as onefold. The results are presented as the mean ±  SD  of three assays. Significant at *** p 
Figure Legend Snippet: FKA down‐regulates MMP ‐9/‐2 and up‐regulates TIMP ‐1 expressions in TGF ‐β1‐activated A7r5 cells. A‐C, Cells were preincubated with FKA (2‐30 μM) for 2 h and then stimulated with or without TGF ‐β1 (10 ng/ mL ) for 24 h. Western blotting was performed to analyse (A) MMP ‐9, (B) MMP ‐2 and (C) TIMP ‐1 protein levels. Relative changes in protein intensities were quantified using AlphaEaseFc 4.0 software and presented as histograms, with controls set as onefold. The results are presented as the mean ±  SD of three assays. Significant at *** p 

Techniques Used: Western Blot, Software

36) Product Images from "Plaque Rupture is a Determinant of Vascular Events in Carotid Artery Atherosclerotic Disease: Involvement of Matrix Metalloproteinases 2 and 9"

Article Title: Plaque Rupture is a Determinant of Vascular Events in Carotid Artery Atherosclerotic Disease: Involvement of Matrix Metalloproteinases 2 and 9

Journal: Journal of Clinical Neurology (Seoul, Korea)

doi: 10.3988/jcn.2011.7.2.69

Immunofluorescence staining illustrating the expressions of MMP-2 and MMP-9 produced by macrophages in carotid plaques. A and D: MMP-2 and MMP-9 were visualized with secondary antibodies conjugated to Texas Red (red). B and E: The nuclei were stained with DAPI (blue). C and F: MMPs colocalized with the cytoplasm in the macrophages. The white boxes in each image are magnified. Scale bar=100 µm. MMP: matrix metalloproteinase.
Figure Legend Snippet: Immunofluorescence staining illustrating the expressions of MMP-2 and MMP-9 produced by macrophages in carotid plaques. A and D: MMP-2 and MMP-9 were visualized with secondary antibodies conjugated to Texas Red (red). B and E: The nuclei were stained with DAPI (blue). C and F: MMPs colocalized with the cytoplasm in the macrophages. The white boxes in each image are magnified. Scale bar=100 µm. MMP: matrix metalloproteinase.

Techniques Used: Immunofluorescence, Staining, Produced

Carotid specimens that were immunohistochemically positive for MMP-2 (A) and MMP-9 (B) were also strongly positive for CD68 (C) but negative for SMA (D). MMP: matrix metalloproteinase, SMA: smooth-muscle actin.
Figure Legend Snippet: Carotid specimens that were immunohistochemically positive for MMP-2 (A) and MMP-9 (B) were also strongly positive for CD68 (C) but negative for SMA (D). MMP: matrix metalloproteinase, SMA: smooth-muscle actin.

Techniques Used:

37) Product Images from "Aurora-A modulates MMP-2 expression via AKT/NF-κB pathway in esophageal squamous cell carcinoma cells"

Article Title: Aurora-A modulates MMP-2 expression via AKT/NF-κB pathway in esophageal squamous cell carcinoma cells

Journal: Acta Biochimica et Biophysica Sinica

doi: 10.1093/abbs/gmw030

ESCC cell invasion is promoted by Aurora-A overexpression and attenuated by the MMP-2 inhibitor I (A) The levels of fusion protein GFP-Aurora-A and MMP-2 were detected by western blot analysis after stable transfection of GFP-Aurora-A expression
Figure Legend Snippet: ESCC cell invasion is promoted by Aurora-A overexpression and attenuated by the MMP-2 inhibitor I (A) The levels of fusion protein GFP-Aurora-A and MMP-2 were detected by western blot analysis after stable transfection of GFP-Aurora-A expression

Techniques Used: Over Expression, Western Blot, Stable Transfection, Expressing

Expression of Aurora-A is positively correlated with expression of MMP - 2 in ESCC
Figure Legend Snippet: Expression of Aurora-A is positively correlated with expression of MMP - 2 in ESCC

Techniques Used: Expressing

Representative immunohistochemical stainings of MMP-2 in ESCC and normal adjacent tissues on TMA (A) In normal adjacent esophageal tissues, MMP-2 showed negative cytoplasmic and weak nuclear staining. In ESCC tissues, MMP-2 staining was weakly
Figure Legend Snippet: Representative immunohistochemical stainings of MMP-2 in ESCC and normal adjacent tissues on TMA (A) In normal adjacent esophageal tissues, MMP-2 showed negative cytoplasmic and weak nuclear staining. In ESCC tissues, MMP-2 staining was weakly

Techniques Used: Immunohistochemistry, Staining

Aurora-A overexpression upregulates MMP-2 expression via AKT/NF-κB activation in ESCC cells (A) The nuclear protein level of NF-κB p65 was detected by western blot analysis in Aurora-A-overexpressing and control cells. (B) Cells
Figure Legend Snippet: Aurora-A overexpression upregulates MMP-2 expression via AKT/NF-κB activation in ESCC cells (A) The nuclear protein level of NF-κB p65 was detected by western blot analysis in Aurora-A-overexpressing and control cells. (B) Cells

Techniques Used: Over Expression, Expressing, Activation Assay, Western Blot

Expressions of Aurora-A and MMP-2 proteins in ESCC tissue
Figure Legend Snippet: Expressions of Aurora-A and MMP-2 proteins in ESCC tissue

Techniques Used:

Expressions of Aurora-A and MMP-2 proteins as well as cell invasion capability in ESCC cell lines (A) The expression levels of Aurora-A and MMP-2 were detected by western blot analysis in KYSE150 and EC9706 cells. (B) The relative Aurora-A and
Figure Legend Snippet: Expressions of Aurora-A and MMP-2 proteins as well as cell invasion capability in ESCC cell lines (A) The expression levels of Aurora-A and MMP-2 were detected by western blot analysis in KYSE150 and EC9706 cells. (B) The relative Aurora-A and

Techniques Used: Expressing, Western Blot

38) Product Images from "Hyperthermia-Induced NDRG2 Upregulation Inhibits the Invasion of Human Hepatocellular Carcinoma via Suppressing ERK1/2 Signaling Pathway"

Article Title: Hyperthermia-Induced NDRG2 Upregulation Inhibits the Invasion of Human Hepatocellular Carcinoma via Suppressing ERK1/2 Signaling Pathway

Journal: PLoS ONE

doi: 10.1371/journal.pone.0061079

Down-regulation of NDRG2 affects the invasiveness of heat-treated HCC cells in vivo. (A) Expression level of NDRG2 in Scramble-HepG2 (transfected with silencing expression control plasmid) and shNDRG2-HepG2 (transfected with NDRG2 silencing plasmid) cells. HepG2 cells were transfected separately with the Scramble or shNDRG2 and then individually injected into the hind legs of the mice. After two weeks of implantation, mice in the heat-treated groups were subjected to a 45°C water bath for 30 min. Each experimental group contained 5 mice. Four weeks later, mice were sacrificed, and primary tumors were removed for histological examination. (B) Representative H E staining of histological sections revealed histological destruction in each group. Arrows point to invasion areas. Stars mark the locations of muscle. (C) Immunohistochemistry showed expression levels of NDRG2, MMP-2 and MMP-9 in the tumor tissues of each group. Bar = 30 µm (magnification 400×).
Figure Legend Snippet: Down-regulation of NDRG2 affects the invasiveness of heat-treated HCC cells in vivo. (A) Expression level of NDRG2 in Scramble-HepG2 (transfected with silencing expression control plasmid) and shNDRG2-HepG2 (transfected with NDRG2 silencing plasmid) cells. HepG2 cells were transfected separately with the Scramble or shNDRG2 and then individually injected into the hind legs of the mice. After two weeks of implantation, mice in the heat-treated groups were subjected to a 45°C water bath for 30 min. Each experimental group contained 5 mice. Four weeks later, mice were sacrificed, and primary tumors were removed for histological examination. (B) Representative H E staining of histological sections revealed histological destruction in each group. Arrows point to invasion areas. Stars mark the locations of muscle. (C) Immunohistochemistry showed expression levels of NDRG2, MMP-2 and MMP-9 in the tumor tissues of each group. Bar = 30 µm (magnification 400×).

Techniques Used: In Vivo, Expressing, Transfection, Plasmid Preparation, Injection, Mouse Assay, Staining, Immunohistochemistry

39) Product Images from "Suppressions of Migration and Invasion by Cantharidin in TSGH-8301 Human Bladder Carcinoma Cells through the Inhibitions of Matrix Metalloproteinase-2/-9 Signaling"

Article Title: Suppressions of Migration and Invasion by Cantharidin in TSGH-8301 Human Bladder Carcinoma Cells through the Inhibitions of Matrix Metalloproteinase-2/-9 Signaling

Journal: Evidence-based Complementary and Alternative Medicine : eCAM

doi: 10.1155/2013/190281

Cantharidin affects the levels of associated proteins and gene levels in migration and invasion of TSGH-8301 cells. Cells were treated with cantharidin (0, 1, and 2.5 μ M) for 24 h, and then cells were collected. The total protein extract was quantified and determined as described in Section 2 . The levels of p-p38, p-JNK1/2, p-ERK1/2, MMP-2, and MMP-9 protein expressions (a) were estimated by Western blotting as described in Section 2 . (b) The total RNA was extracted from cantharidin-treated cells, and the RNA samples were reverse-transcribed to cDNA for real-time PCR as described in Section 2 . The ratios between MMP-2, MMP-9, and GAPDH mRNA are used and data represents mean ± SD in duplicate of at least three independent experiments. * P
Figure Legend Snippet: Cantharidin affects the levels of associated proteins and gene levels in migration and invasion of TSGH-8301 cells. Cells were treated with cantharidin (0, 1, and 2.5 μ M) for 24 h, and then cells were collected. The total protein extract was quantified and determined as described in Section 2 . The levels of p-p38, p-JNK1/2, p-ERK1/2, MMP-2, and MMP-9 protein expressions (a) were estimated by Western blotting as described in Section 2 . (b) The total RNA was extracted from cantharidin-treated cells, and the RNA samples were reverse-transcribed to cDNA for real-time PCR as described in Section 2 . The ratios between MMP-2, MMP-9, and GAPDH mRNA are used and data represents mean ± SD in duplicate of at least three independent experiments. * P

Techniques Used: Migration, Western Blot, Real-time Polymerase Chain Reaction

Cantharidin suppresses the activities of matrix metalloproteinases (MMPs) in TSGH-8301 cells. Gelatin zymography was used to evaluate the activities of MMP-2 and MMP-9 as described in Section 2 . The different activity of MMP-2 and -9 was determined by densitometry analysis, and results are expressed as % of control. Similar results were obtained from three independent experiments.
Figure Legend Snippet: Cantharidin suppresses the activities of matrix metalloproteinases (MMPs) in TSGH-8301 cells. Gelatin zymography was used to evaluate the activities of MMP-2 and MMP-9 as described in Section 2 . The different activity of MMP-2 and -9 was determined by densitometry analysis, and results are expressed as % of control. Similar results were obtained from three independent experiments.

Techniques Used: Zymography, Activity Assay

40) Product Images from "LY294002 induces differentiation and inhibits invasion of glioblastoma cells by targeting GSK-3beta and MMP"

Article Title: LY294002 induces differentiation and inhibits invasion of glioblastoma cells by targeting GSK-3beta and MMP

Journal: EXCLI Journal

doi:

AG3340 impaired invasion of C6 glioblastoma cells. (A) Immunoblots of the MMP-2 and MMP-9 protein levels of cells treated with 20 μM LY294002 for 48 h. (B) Matrigel invasion assay of C6 cells pretreated with 100 μM AG3340 for 24 h (Scale bar = 50 μM). (C) Statistical analysis of three independent experiments in panel B. The data are mean ± SD (n=3). * p
Figure Legend Snippet: AG3340 impaired invasion of C6 glioblastoma cells. (A) Immunoblots of the MMP-2 and MMP-9 protein levels of cells treated with 20 μM LY294002 for 48 h. (B) Matrigel invasion assay of C6 cells pretreated with 100 μM AG3340 for 24 h (Scale bar = 50 μM). (C) Statistical analysis of three independent experiments in panel B. The data are mean ± SD (n=3). * p

Techniques Used: Western Blot, Invasion Assay

Related Articles

Enzyme-linked Immunosorbent Assay:

Article Title: Chromodomain Helicase/ATPase DNA-Binding Protein 1-Like Gene (CHD1L) Expression and Implications for Invasion and Metastasis of Breast Cancer
Article Snippet: .. Enzyme-linked immunosorbent assay (ELISA) An ELISA kit was used to detect the MMP-2 and MMP-9 expression levels in the culture medium of all cells with or without 10 ng/mL EGF. .. The medium was then harvested and filtered for the measurement of MMP-2 and MMP-9.

Article Title: Chromodomain Helicase/ATPase DNA-Binding Protein 1-Like Gene (CHD1L) Expression and Implications for Invasion and Metastasis of Breast Cancer
Article Snippet: .. MMP-2 and MMP-9 activities were assessed using ELISA with culture media of SiCHD1L/MDA231 and Scr/MDA231 cells. .. In the absence of EGF, significant changes in MMP-2 and MMP-9 levels were not observed in SiCHD1L/MDA231 cells.

other:

Article Title: Anti-inflammatory/anti-fibrotic effects of the hepatoprotective silymarin and the schistosomicide praziquantel against Schistosoma mansoni-induced liver fibrosis
Article Snippet: The highest reduction observed in TGF-β1, MMP-2 and mast cells was in the group treated with PZQ plus silymarin.

Article Title: Plaque Rupture is a Determinant of Vascular Events in Carotid Artery Atherosclerotic Disease: Involvement of Matrix Metalloproteinases 2 and 9
Article Snippet: The findings of our study show that both MMP-2 and MMP-9 are significantly associated with plaque rupture.

Article Title: MMP‐2 and MMP‐13 affect vasculogenic mimicry formation in large cell lung cancer
Article Snippet: Either exogenous Ln‐5 or Ln‐5 cleaved by MMP‐13 or MMP‐2 at 37°C for 6 hrs was added into the culture medium when seeding the cells (200 ng/ml).

Expressing:

Article Title: Chromodomain Helicase/ATPase DNA-Binding Protein 1-Like Gene (CHD1L) Expression and Implications for Invasion and Metastasis of Breast Cancer
Article Snippet: .. Enzyme-linked immunosorbent assay (ELISA) An ELISA kit was used to detect the MMP-2 and MMP-9 expression levels in the culture medium of all cells with or without 10 ng/mL EGF. .. The medium was then harvested and filtered for the measurement of MMP-2 and MMP-9.

Article Title: Chromodomain Helicase/ATPase DNA-Binding Protein 1-Like Gene (CHD1L) Expression and Implications for Invasion and Metastasis of Breast Cancer
Article Snippet: .. The results of the present study show that EGF stimulation resulted in reduced MMP-2 and MMP-9 expression in CHD1L-downregulated cells compared with MDA231/con cells. .. Activation of the PI3K/Akt/mTOR signaling pathway in breast cancer could be as frequent as 70%.

Article Title: Anti-inflammatory/anti-fibrotic effects of the hepatoprotective silymarin and the schistosomicide praziquantel against Schistosoma mansoni-induced liver fibrosis
Article Snippet: .. This was evident in diminishing hepatic content of HYP, serum levels and hepatic expression of TGF-β1 and MMP-2 and the number of mast cells. ..

Infection:

Article Title: Anti-inflammatory/anti-fibrotic effects of the hepatoprotective silymarin and the schistosomicide praziquantel against Schistosoma mansoni-induced liver fibrosis
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. .. Compared to the infected untreated group, treatment with PZQ caused a significant reduction in both serum TGF-β1 (P < 0.001) and MMP-2 (P < 0.05, P < 0.001) levels by (43.34%, 51.75%) and (20.73%, 39.35%), 10 and 18 weeks PI, respectively.

Mouse Assay:

Article Title: Anti-inflammatory/anti-fibrotic effects of the hepatoprotective silymarin and the schistosomicide praziquantel against Schistosoma mansoni-induced liver fibrosis
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. .. Compared to the infected untreated group, treatment with PZQ caused a significant reduction in both serum TGF-β1 (P < 0.001) and MMP-2 (P < 0.05, P < 0.001) levels by (43.34%, 51.75%) and (20.73%, 39.35%), 10 and 18 weeks PI, respectively.

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    Santa Cruz Biotechnology primary mouse anti human monoclonal antibody mmp 2
    Survival curves of positive and negative <t>MMP-2</t> expression groups. MMP-2, matrix metalloproteinase-2.
    Primary Mouse Anti Human Monoclonal Antibody Mmp 2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/primary mouse anti human monoclonal antibody mmp 2/product/Santa Cruz Biotechnology
    Average 92 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    primary mouse anti human monoclonal antibody mmp 2 - by Bioz Stars, 2020-09
    92/100 stars
      Buy from Supplier

    92
    Santa Cruz Biotechnology mmp 2
    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).
    Mmp 2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 92/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mmp 2/product/Santa Cruz Biotechnology
    Average 92 stars, based on 36 article reviews
    Price from $9.99 to $1999.99
    mmp 2 - by Bioz Stars, 2020-09
    92/100 stars
      Buy from Supplier

    Image Search Results


    Survival curves of positive and negative MMP-2 expression groups. MMP-2, matrix metalloproteinase-2.

    Journal: Oncology Letters

    Article Title: MMP-2 expression and correlation with pathology and MRI of glioma

    doi: 10.3892/ol.2018.9806

    Figure Lengend Snippet: Survival curves of positive and negative MMP-2 expression groups. MMP-2, matrix metalloproteinase-2.

    Article Snippet: Primary mouse anti-human monoclonal antibody MMP-2 (diluted at 1:100; cat. no. sc-13594, Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA) was added and incubated overnight in a wet box.

    Techniques: Expressing

    Detection of MMP-2 expression in glioma tissues and paired normal brain tissues via IHC (magnification, ×200). MMP-2, matrix metalloproteinase-2; IHC, immunohistochemistry.

    Journal: Oncology Letters

    Article Title: MMP-2 expression and correlation with pathology and MRI of glioma

    doi: 10.3892/ol.2018.9806

    Figure Lengend Snippet: Detection of MMP-2 expression in glioma tissues and paired normal brain tissues via IHC (magnification, ×200). MMP-2, matrix metalloproteinase-2; IHC, immunohistochemistry.

    Article Snippet: Primary mouse anti-human monoclonal antibody MMP-2 (diluted at 1:100; cat. no. sc-13594, Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA) was added and incubated overnight in a wet box.

    Techniques: Expressing, Immunohistochemistry

    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