collagenase ii Search Results


94
MedChemExpress cartilage tissue
Cartilage Tissue, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Thermo Fisher s0015 trizol thermo fisher scientific 15596026 dnase i vwr ic19006210 collagenase ii life technologies 17101015 hoechst 33342 invitrogen h3570
S0015 Trizol Thermo Fisher Scientific 15596026 Dnase I Vwr Ic19006210 Collagenase Ii Life Technologies 17101015 Hoechst 33342 Invitrogen H3570, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology collagenase cls type ii
Collagenase Cls Type Ii, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Proteintech mmp2
CAFs secrete SRGN via autophagy to promote OSCC cell invasion and migration by facilitating ECM remodelling through interaction with <t>MMP2/9.</t> (A, B) WB analysis of SRGN protein expression levels and quantification in WT CAFs and SRGN KO CAFs. (C) qPCR analysis of SRGN gene expression in WT CAFs and SRGN KO CAFs. (D) UV image of the agarose gel. (E) The supernatant from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs was collected and co‐cultured with OSCC cells. Invasion ability was assessed by transwell assays. (F) Invasion cell numbers were quantified using ImageJ software. (* p < .05; ** p < .01; *** p < .001). (G) The supernatant from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs was collected and co‐cultured with SCC9 cells. Migration ability was assessed by scratch assays. (H) Prediction of SRGN‐binding proteins using the STRING database. (I) HEK293T cells were transfected with SRGN‐Flag and incubated for 48 h. Cell lysates were incubated with anti‐Flag beads, and immunoblotting (IB) was performed using anti‐Flag, anti‐MMP11, anti‐MMP9, and anti‐MMP2 antibodies. (J) WB analysis of changes in MMP9, MMP11, MMP2, and SRGN protein expression levels in WT CAFs and SRGN KO CAFs. (K) Gelatin degradation assays were performed to evaluate gelatin degradation after 24 h of co‐culture of CAL27 cells with the supernatants from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs. Scale bar = 20 µm.
Mmp2, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech anti matrix metalloproteinase
Figure 3. Epithelial‑mesenchymal transition of retinoblastoma cells is suppressed by shRNA‑FEZF1‑AS1. Western blotting was used to analyze the protein expression levels of (A) Vimentin, Snail, Slug and β‑catenin, (B) N‑cadherin, E‑cadherin, Claudin‑1 and (C) MMP2 and MMP9 in Y79 cells transfected with shRNA‑NC or shRNA‑FEZF1‑AS1. All data are expressed as the mean ± SEM. **P<0.01, ***P<0.001 vs. shRNA‑NC group. FEZF1‑AS1, FEZ family zinc finger 1 antisense RNA 1; shRNA, short hairpin RNA; NC, negative control; MMP, matrix <t>metalloproteinase.</t>
Anti Matrix Metalloproteinase, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Boster Bio pvdf membrane
Figure 3. Epithelial‑mesenchymal transition of retinoblastoma cells is suppressed by shRNA‑FEZF1‑AS1. Western blotting was used to analyze the protein expression levels of (A) Vimentin, Snail, Slug and β‑catenin, (B) N‑cadherin, E‑cadherin, Claudin‑1 and (C) MMP2 and MMP9 in Y79 cells transfected with shRNA‑NC or shRNA‑FEZF1‑AS1. All data are expressed as the mean ± SEM. **P<0.01, ***P<0.001 vs. shRNA‑NC group. FEZF1‑AS1, FEZ family zinc finger 1 antisense RNA 1; shRNA, short hairpin RNA; NC, negative control; MMP, matrix <t>metalloproteinase.</t>
Pvdf Membrane, supplied by Boster Bio, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Valiant Co Ltd collagenase type ii
Figure 3. Epithelial‑mesenchymal transition of retinoblastoma cells is suppressed by shRNA‑FEZF1‑AS1. Western blotting was used to analyze the protein expression levels of (A) Vimentin, Snail, Slug and β‑catenin, (B) N‑cadherin, E‑cadherin, Claudin‑1 and (C) MMP2 and MMP9 in Y79 cells transfected with shRNA‑NC or shRNA‑FEZF1‑AS1. All data are expressed as the mean ± SEM. **P<0.01, ***P<0.001 vs. shRNA‑NC group. FEZF1‑AS1, FEZ family zinc finger 1 antisense RNA 1; shRNA, short hairpin RNA; NC, negative control; MMP, matrix <t>metalloproteinase.</t>
Collagenase Type Ii, supplied by Valiant Co Ltd, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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96
Proteintech anti mmp9 rb
Downregulation of MMP2/9 by SB-3CT treatment reduced PD-L1 expression. a Spearman’s correlation of group4 score and PD-L1 mRNA expression across 33 cancer types. b – g Evaluation of PD-L1 expression derived from SK-MEL-28 melanoma cell lines and A549 lung cancer cell lines treated with DMSO, SB-3CT (25 μM), IFNγ (200 ng/mL), and IFNγ/SB-3CT in combination for 24 h. b , c PD-L1 expression by RT-PCR in b SK-MEL-28 melanoma cell lines and c A549 lung cancer cell lines. d , e Western blot (left panel: representative images, right panel: quantification) of PD-L1 protein levels in d SK-MEL-28 and e A549. f , g Flow cytometry of PD-L1 + membrane level in f SK-MEL-28 and g A549. h – m PD-L1 expression of SK-MEL-28 melanoma cell line transfected with shMMP2 ( h – j ) and shMMP9 ( k – m ) or the scrambled negative control shRNA (shNC). Western blot ( h , k ) quantification of MMP2, <t>MMP9,</t> and PD-L1 protein expression ( i , l ), and RT-PCR analysis of MMP2, MMP9, and PD-L1 mRNA expression ( j , m )
Anti Mmp9 Rb, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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92
Proteintech human mmp2
(A) DU145 cells with filamin C silencing were fluorescence-labeled and analyzed in a zebrafish cancer metastasis model. The selected pictures were shown from 0 to 3 days post injection. The areas indicated with arrows were enlarged for visualizing disseminated cancer cells. (B) Filamin C was silenced in DU145 cells and the proenzyme (Pro) and activated form of <t>MMP2</t> were analyzed. (C) Migration of DU145 cells with or without filamin C silencing were analyzed. The third group with filamin C silencing was further treated with the MMP2 inhibitor ARP100. The statistical analysis results were shown in Figure and the Western blot results were shown in Figure . FLNC, filamin C.
Human Mmp2, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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97
Proteintech mmp 2
(A) DU145 cells with filamin C silencing were fluorescence-labeled and analyzed in a zebrafish cancer metastasis model. The selected pictures were shown from 0 to 3 days post injection. The areas indicated with arrows were enlarged for visualizing disseminated cancer cells. (B) Filamin C was silenced in DU145 cells and the proenzyme (Pro) and activated form of <t>MMP2</t> were analyzed. (C) Migration of DU145 cells with or without filamin C silencing were analyzed. The third group with filamin C silencing was further treated with the MMP2 inhibitor ARP100. The statistical analysis results were shown in Figure and the Western blot results were shown in Figure . FLNC, filamin C.
Mmp 2, supplied by Proteintech, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech rabbit anti mmp2
TEM8 promoted invasion and migration in ovarian cancer cells. A-D. Transwell assay showed that TEM8 overexpression promoted invasion of ovarian cancer cells, however, TEM8 knockdown reversed this effect (n = 9; ×200, scale bar = 100 μm). E-H. Scratch assay showed that TEM8 overexpression promoted migration of ovarian cancer cells, however, TEM8 knockdown reversed this effect (n = 9; ×100, scale bar = 100 μm). I, J. Representative images and quantitation of the western blot showed that the protein expression of <t>MMP2,</t> MMP9, and VEGFA in the TEM8 overexpression/knockdown groups (n = 3). GAPDH was used as an internal control. Data are presented as mean ± SD. *, P < 0.05; **, P < 0.01; ***, P < 0.001.
Rabbit Anti Mmp2, supplied by Proteintech, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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90
Merck & Co collagenase ii
TEM8 promoted invasion and migration in ovarian cancer cells. A-D. Transwell assay showed that TEM8 overexpression promoted invasion of ovarian cancer cells, however, TEM8 knockdown reversed this effect (n = 9; ×200, scale bar = 100 μm). E-H. Scratch assay showed that TEM8 overexpression promoted migration of ovarian cancer cells, however, TEM8 knockdown reversed this effect (n = 9; ×100, scale bar = 100 μm). I, J. Representative images and quantitation of the western blot showed that the protein expression of <t>MMP2,</t> MMP9, and VEGFA in the TEM8 overexpression/knockdown groups (n = 3). GAPDH was used as an internal control. Data are presented as mean ± SD. *, P < 0.05; **, P < 0.01; ***, P < 0.001.
Collagenase Ii, supplied by Merck & Co, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


CAFs secrete SRGN via autophagy to promote OSCC cell invasion and migration by facilitating ECM remodelling through interaction with MMP2/9. (A, B) WB analysis of SRGN protein expression levels and quantification in WT CAFs and SRGN KO CAFs. (C) qPCR analysis of SRGN gene expression in WT CAFs and SRGN KO CAFs. (D) UV image of the agarose gel. (E) The supernatant from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs was collected and co‐cultured with OSCC cells. Invasion ability was assessed by transwell assays. (F) Invasion cell numbers were quantified using ImageJ software. (* p < .05; ** p < .01; *** p < .001). (G) The supernatant from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs was collected and co‐cultured with SCC9 cells. Migration ability was assessed by scratch assays. (H) Prediction of SRGN‐binding proteins using the STRING database. (I) HEK293T cells were transfected with SRGN‐Flag and incubated for 48 h. Cell lysates were incubated with anti‐Flag beads, and immunoblotting (IB) was performed using anti‐Flag, anti‐MMP11, anti‐MMP9, and anti‐MMP2 antibodies. (J) WB analysis of changes in MMP9, MMP11, MMP2, and SRGN protein expression levels in WT CAFs and SRGN KO CAFs. (K) Gelatin degradation assays were performed to evaluate gelatin degradation after 24 h of co‐culture of CAL27 cells with the supernatants from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs. Scale bar = 20 µm.

Journal: Clinical and Translational Medicine

Article Title: Hypoxia‐induced secretory autophagy in cancer‐associated fibroblasts promotes ECM remodelling through serglycin secretion in oral squamous cell carcinoma

doi: 10.1002/ctm2.70556

Figure Lengend Snippet: CAFs secrete SRGN via autophagy to promote OSCC cell invasion and migration by facilitating ECM remodelling through interaction with MMP2/9. (A, B) WB analysis of SRGN protein expression levels and quantification in WT CAFs and SRGN KO CAFs. (C) qPCR analysis of SRGN gene expression in WT CAFs and SRGN KO CAFs. (D) UV image of the agarose gel. (E) The supernatant from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs was collected and co‐cultured with OSCC cells. Invasion ability was assessed by transwell assays. (F) Invasion cell numbers were quantified using ImageJ software. (* p < .05; ** p < .01; *** p < .001). (G) The supernatant from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs was collected and co‐cultured with SCC9 cells. Migration ability was assessed by scratch assays. (H) Prediction of SRGN‐binding proteins using the STRING database. (I) HEK293T cells were transfected with SRGN‐Flag and incubated for 48 h. Cell lysates were incubated with anti‐Flag beads, and immunoblotting (IB) was performed using anti‐Flag, anti‐MMP11, anti‐MMP9, and anti‐MMP2 antibodies. (J) WB analysis of changes in MMP9, MMP11, MMP2, and SRGN protein expression levels in WT CAFs and SRGN KO CAFs. (K) Gelatin degradation assays were performed to evaluate gelatin degradation after 24 h of co‐culture of CAL27 cells with the supernatants from normoxic and hypoxic WT CAFs, WT CAFs + 3‐MA, and SRGN KO CAFs. Scale bar = 20 µm.

Article Snippet: Primary antibodies used in this assay included: β‐actin (1:4000, 20536‐1, Proteintech), MMP9 (1:1000, bs‐4593R, Bioss), MMP2 (1:1000, CY5189, Abways), MMP11 (1:1000, CY5778, Abways), Flag (1:5000, 80801‐2‐RR, Proteintech).

Techniques: Migration, Expressing, Gene Expression, Agarose Gel Electrophoresis, Cell Culture, Software, Binding Assay, Transfection, Incubation, Western Blot, Co-Culture Assay

CAF‐derived SRGN promotes tumour invasion and ECM degradation via autophagy secretion. (A) In vivo xenograft models were established in nude mice and divided into four groups: (a) CAL27, (b) CAL27 + WT CAFs, (c) CAL27 + WT CAFs (3‐MA), and (d) CAL27 + SRGN KO CAFs. (B) Tumour volume and tumour weight were monitored ( n = 7). (C, D) H&E staining and IHC analysis of COL1, E‐cadherin, MMP2 and MMP9 were performed in orthotopic xenograft tumour tissues. The expression levels of COL1, E‐cadherin, MMP2 and MMP9 were quantitatively analyzed using Fiji software. Scale bar = 100 µm. (* p < .05; ** p < .01; *** p < .001).

Journal: Clinical and Translational Medicine

Article Title: Hypoxia‐induced secretory autophagy in cancer‐associated fibroblasts promotes ECM remodelling through serglycin secretion in oral squamous cell carcinoma

doi: 10.1002/ctm2.70556

Figure Lengend Snippet: CAF‐derived SRGN promotes tumour invasion and ECM degradation via autophagy secretion. (A) In vivo xenograft models were established in nude mice and divided into four groups: (a) CAL27, (b) CAL27 + WT CAFs, (c) CAL27 + WT CAFs (3‐MA), and (d) CAL27 + SRGN KO CAFs. (B) Tumour volume and tumour weight were monitored ( n = 7). (C, D) H&E staining and IHC analysis of COL1, E‐cadherin, MMP2 and MMP9 were performed in orthotopic xenograft tumour tissues. The expression levels of COL1, E‐cadherin, MMP2 and MMP9 were quantitatively analyzed using Fiji software. Scale bar = 100 µm. (* p < .05; ** p < .01; *** p < .001).

Article Snippet: Primary antibodies used in this assay included: β‐actin (1:4000, 20536‐1, Proteintech), MMP9 (1:1000, bs‐4593R, Bioss), MMP2 (1:1000, CY5189, Abways), MMP11 (1:1000, CY5778, Abways), Flag (1:5000, 80801‐2‐RR, Proteintech).

Techniques: Derivative Assay, In Vivo, Staining, Expressing, Software

Mechanism diagram of hypoxic CAFs‐derived SRGN secretion and tumour progression promotion. Under normal conditions, SRGN is translocated into the ER and subsequently transported via the Golgi apparatus for secretion into the extracellular space. Under hypoxic conditions, elevated autophagy levels in CAFs facilitate the release of SRGN into the ECM through secretory autophagy‐mediated plasma membrane fusion. Within the ECM, SRGN interacts with MMP2 and MMP9, enhancing ECM remodelling and ultimately promoting the invasive capacity of OSCC cells.

Journal: Clinical and Translational Medicine

Article Title: Hypoxia‐induced secretory autophagy in cancer‐associated fibroblasts promotes ECM remodelling through serglycin secretion in oral squamous cell carcinoma

doi: 10.1002/ctm2.70556

Figure Lengend Snippet: Mechanism diagram of hypoxic CAFs‐derived SRGN secretion and tumour progression promotion. Under normal conditions, SRGN is translocated into the ER and subsequently transported via the Golgi apparatus for secretion into the extracellular space. Under hypoxic conditions, elevated autophagy levels in CAFs facilitate the release of SRGN into the ECM through secretory autophagy‐mediated plasma membrane fusion. Within the ECM, SRGN interacts with MMP2 and MMP9, enhancing ECM remodelling and ultimately promoting the invasive capacity of OSCC cells.

Article Snippet: Primary antibodies used in this assay included: β‐actin (1:4000, 20536‐1, Proteintech), MMP9 (1:1000, bs‐4593R, Bioss), MMP2 (1:1000, CY5189, Abways), MMP11 (1:1000, CY5778, Abways), Flag (1:5000, 80801‐2‐RR, Proteintech).

Techniques: Derivative Assay, Clinical Proteomics, Membrane

Figure 3. Epithelial‑mesenchymal transition of retinoblastoma cells is suppressed by shRNA‑FEZF1‑AS1. Western blotting was used to analyze the protein expression levels of (A) Vimentin, Snail, Slug and β‑catenin, (B) N‑cadherin, E‑cadherin, Claudin‑1 and (C) MMP2 and MMP9 in Y79 cells transfected with shRNA‑NC or shRNA‑FEZF1‑AS1. All data are expressed as the mean ± SEM. **P<0.01, ***P<0.001 vs. shRNA‑NC group. FEZF1‑AS1, FEZ family zinc finger 1 antisense RNA 1; shRNA, short hairpin RNA; NC, negative control; MMP, matrix metalloproteinase.

Journal: Molecular medicine reports

Article Title: lncRNA FEZF1‑AS1 promotes migration, invasion and epithelial‑mesenchymal transition of retinoblastoma cells by targeting miR‑1236‑3p.

doi: 10.3892/mmr.2020.11478

Figure Lengend Snippet: Figure 3. Epithelial‑mesenchymal transition of retinoblastoma cells is suppressed by shRNA‑FEZF1‑AS1. Western blotting was used to analyze the protein expression levels of (A) Vimentin, Snail, Slug and β‑catenin, (B) N‑cadherin, E‑cadherin, Claudin‑1 and (C) MMP2 and MMP9 in Y79 cells transfected with shRNA‑NC or shRNA‑FEZF1‑AS1. All data are expressed as the mean ± SEM. **P<0.01, ***P<0.001 vs. shRNA‑NC group. FEZF1‑AS1, FEZ family zinc finger 1 antisense RNA 1; shRNA, short hairpin RNA; NC, negative control; MMP, matrix metalloproteinase.

Article Snippet: The membranes were then incubated with the following primary antibodies at 4 ̊C overnight: Anti‐Vimentin (1:1,000; cat. no. 3932; Cell Signaling Technology, Inc.), anti‐Snail (1:1,000; cat. no. 3879; Cell Signaling Technology, Inc.), anti‐Slug (1:1,000; cat. no. 9585; Cell Signaling Technology, Inc.), anti‐Claudin‐1 (1:1,000; cat. no. 4933; Cell Signaling Technology, Inc.), anti‐β-catenin (1:500; cat. no. sc‐59737; Santa Cruz Biotechnology, Inc.), anti‐N‐cadherin (1:500; cat. no. sc‐59987; Santa Cruz Biotechnology, Inc.), anti‐E‐cadherin (1:500; cat. no. sc‐8426; Santa Cruz Biotechnology, Inc.), anti‐matrix metalloproteinase (MMP) 2 (1:1,000; cat. no. 10373‐2‐AP; ProteinTech Group, Inc.), anti‐MMP9 (1:1,000; cat. no. 10375‐2‐AP; ProteinTech Group, Inc.) and anti‐GAPDH (1:1,000; cat. no. SAB5600208; Sigma-aldrich; Merck KGaa).

Techniques: Western Blot, Expressing, Transfection, shRNA, Negative Control

Figure 6. Continued. Inhibition of miR‑1236‑3p reverses the effects of shRNA‑FEZF1‑AS1 on epithelial‑mesenchymal transition. (A) Western blotting was used to analyze the protein expression levels of (A) Vimentin, Snail, Slug and β‑catenin, (B) N‑cadherin, E‑cadherin and Claudin‑1, and (C) MMP2 and MMP9 in Y79 cells transfected with shRNA‑NC or shRNA‑FEZF1‑AS1 with or without miR‑1236‑3p inhibitor or miR‑NC inhibitor. All data are expressed as the mean ± SEM. ***P<0.001 vs. shRNA‑NC group; #P<0.05, ##P<0.01, ###P<0.001 vs. shRNA‑FEZF1‑AS1 + miR‑NC inhibitor group. FEZF1‑AS1, FEZ family zinc finger 1 antisense RNA 1; shRNA, short hairpin RNA; NC, negative control; miR, microRNA; MMP, matrix metalloproteinase.

Journal: Molecular medicine reports

Article Title: lncRNA FEZF1‑AS1 promotes migration, invasion and epithelial‑mesenchymal transition of retinoblastoma cells by targeting miR‑1236‑3p.

doi: 10.3892/mmr.2020.11478

Figure Lengend Snippet: Figure 6. Continued. Inhibition of miR‑1236‑3p reverses the effects of shRNA‑FEZF1‑AS1 on epithelial‑mesenchymal transition. (A) Western blotting was used to analyze the protein expression levels of (A) Vimentin, Snail, Slug and β‑catenin, (B) N‑cadherin, E‑cadherin and Claudin‑1, and (C) MMP2 and MMP9 in Y79 cells transfected with shRNA‑NC or shRNA‑FEZF1‑AS1 with or without miR‑1236‑3p inhibitor or miR‑NC inhibitor. All data are expressed as the mean ± SEM. ***P<0.001 vs. shRNA‑NC group; #P<0.05, ##P<0.01, ###P<0.001 vs. shRNA‑FEZF1‑AS1 + miR‑NC inhibitor group. FEZF1‑AS1, FEZ family zinc finger 1 antisense RNA 1; shRNA, short hairpin RNA; NC, negative control; miR, microRNA; MMP, matrix metalloproteinase.

Article Snippet: The membranes were then incubated with the following primary antibodies at 4 ̊C overnight: Anti‐Vimentin (1:1,000; cat. no. 3932; Cell Signaling Technology, Inc.), anti‐Snail (1:1,000; cat. no. 3879; Cell Signaling Technology, Inc.), anti‐Slug (1:1,000; cat. no. 9585; Cell Signaling Technology, Inc.), anti‐Claudin‐1 (1:1,000; cat. no. 4933; Cell Signaling Technology, Inc.), anti‐β-catenin (1:500; cat. no. sc‐59737; Santa Cruz Biotechnology, Inc.), anti‐N‐cadherin (1:500; cat. no. sc‐59987; Santa Cruz Biotechnology, Inc.), anti‐E‐cadherin (1:500; cat. no. sc‐8426; Santa Cruz Biotechnology, Inc.), anti‐matrix metalloproteinase (MMP) 2 (1:1,000; cat. no. 10373‐2‐AP; ProteinTech Group, Inc.), anti‐MMP9 (1:1,000; cat. no. 10375‐2‐AP; ProteinTech Group, Inc.) and anti‐GAPDH (1:1,000; cat. no. SAB5600208; Sigma-aldrich; Merck KGaa).

Techniques: Inhibition, Western Blot, Expressing, Transfection, shRNA, Negative Control

Downregulation of MMP2/9 by SB-3CT treatment reduced PD-L1 expression. a Spearman’s correlation of group4 score and PD-L1 mRNA expression across 33 cancer types. b – g Evaluation of PD-L1 expression derived from SK-MEL-28 melanoma cell lines and A549 lung cancer cell lines treated with DMSO, SB-3CT (25 μM), IFNγ (200 ng/mL), and IFNγ/SB-3CT in combination for 24 h. b , c PD-L1 expression by RT-PCR in b SK-MEL-28 melanoma cell lines and c A549 lung cancer cell lines. d , e Western blot (left panel: representative images, right panel: quantification) of PD-L1 protein levels in d SK-MEL-28 and e A549. f , g Flow cytometry of PD-L1 + membrane level in f SK-MEL-28 and g A549. h – m PD-L1 expression of SK-MEL-28 melanoma cell line transfected with shMMP2 ( h – j ) and shMMP9 ( k – m ) or the scrambled negative control shRNA (shNC). Western blot ( h , k ) quantification of MMP2, MMP9, and PD-L1 protein expression ( i , l ), and RT-PCR analysis of MMP2, MMP9, and PD-L1 mRNA expression ( j , m )

Journal: Genome Medicine

Article Title: Small-molecule MMP2/MMP9 inhibitor SB-3CT modulates tumor immune surveillance by regulating PD-L1

doi: 10.1186/s13073-020-00780-z

Figure Lengend Snippet: Downregulation of MMP2/9 by SB-3CT treatment reduced PD-L1 expression. a Spearman’s correlation of group4 score and PD-L1 mRNA expression across 33 cancer types. b – g Evaluation of PD-L1 expression derived from SK-MEL-28 melanoma cell lines and A549 lung cancer cell lines treated with DMSO, SB-3CT (25 μM), IFNγ (200 ng/mL), and IFNγ/SB-3CT in combination for 24 h. b , c PD-L1 expression by RT-PCR in b SK-MEL-28 melanoma cell lines and c A549 lung cancer cell lines. d , e Western blot (left panel: representative images, right panel: quantification) of PD-L1 protein levels in d SK-MEL-28 and e A549. f , g Flow cytometry of PD-L1 + membrane level in f SK-MEL-28 and g A549. h – m PD-L1 expression of SK-MEL-28 melanoma cell line transfected with shMMP2 ( h – j ) and shMMP9 ( k – m ) or the scrambled negative control shRNA (shNC). Western blot ( h , k ) quantification of MMP2, MMP9, and PD-L1 protein expression ( i , l ), and RT-PCR analysis of MMP2, MMP9, and PD-L1 mRNA expression ( j , m )

Article Snippet: Human anti-PD-L1-Rb (ab213524) and mouse anti-PD-L1-Rb (ab213480) were purchased from Abcam; anti-CD8α-Rb (GB11068 and GB11068-1) was purchased from Servicebio; anti-PD-1-Rb (84651) was purchased from Cell Signaling Technology; the antibodies specific for human anti-MMP2-Rb (10375-2-AP), anti-MMP9-Rb (10373-2-AP), anti-MMP9-Rb (10373-2-AP), anti-GAPDH-M (60004-1-Ig), and anti-PD-L1-M (66248) were purchased from Proteintech; SB-3CT was purchased from Selleck(S7430); and in vivo mAb anti-PD-1-M (BE0146), anti-CTLA-4-M (BE0164), and IgG isotype control (BE0086, BE0089) were purchased from Bioxcell.

Techniques: Expressing, Derivative Assay, Reverse Transcription Polymerase Chain Reaction, Western Blot, Flow Cytometry, Transfection, Negative Control, shRNA

Regulation of PD-L1 expression through MMP2/9 has an anti-tumor effect. a – f Analysis of PD-L1 expression of SK-MEL-28 melanoma cell line with overexpression (oe) MMP2 ( a – c ), oeMMP9 ( d – f ). Western blot ( a , d ), quantification ( b , e ), and RT-PCR analysis ( c , f ) of MMP2, MMP9, and PD-L1 protein or mRNA expression. g – l PD-L1 expression of shMMP2 ( g – i ) and shMMP9 ( j – l ) SK-MEL-28 melanoma cell line treated with SB-3CT. Western blot ( g , j ); quantification of MMP2, MMP9, and PD-L1 protein ( h , k ); and mRNA expression ( i , l ). m Western blot showed the protein expression of PD-L1 for SK-MEL-28 melanoma cells with overexpression of PD-L1, treated with or without SB-3CT. n Z -scale normalization expression of differentially expressed genes (fold change > 1.5 and two-sided Student’s t test p < 0.05) between A375 melanoma cell lines treated with IFNγ/SB-3CT in combination and IFNγ. o Enriched signaling pathways for genes downregulated in A375 melanoma cell lines treated with SB-3CT and IFNγ in combination (Fisher’s exact test p < 0.05). All experiments were repeated three times independently. Results are mean ± s.d. NS, p > 0.05, * p < 0.05, ** p < 0.01, and *** p < 0.001, as determined by one-way ANOVA and Dunnett’s multiple comparison test

Journal: Genome Medicine

Article Title: Small-molecule MMP2/MMP9 inhibitor SB-3CT modulates tumor immune surveillance by regulating PD-L1

doi: 10.1186/s13073-020-00780-z

Figure Lengend Snippet: Regulation of PD-L1 expression through MMP2/9 has an anti-tumor effect. a – f Analysis of PD-L1 expression of SK-MEL-28 melanoma cell line with overexpression (oe) MMP2 ( a – c ), oeMMP9 ( d – f ). Western blot ( a , d ), quantification ( b , e ), and RT-PCR analysis ( c , f ) of MMP2, MMP9, and PD-L1 protein or mRNA expression. g – l PD-L1 expression of shMMP2 ( g – i ) and shMMP9 ( j – l ) SK-MEL-28 melanoma cell line treated with SB-3CT. Western blot ( g , j ); quantification of MMP2, MMP9, and PD-L1 protein ( h , k ); and mRNA expression ( i , l ). m Western blot showed the protein expression of PD-L1 for SK-MEL-28 melanoma cells with overexpression of PD-L1, treated with or without SB-3CT. n Z -scale normalization expression of differentially expressed genes (fold change > 1.5 and two-sided Student’s t test p < 0.05) between A375 melanoma cell lines treated with IFNγ/SB-3CT in combination and IFNγ. o Enriched signaling pathways for genes downregulated in A375 melanoma cell lines treated with SB-3CT and IFNγ in combination (Fisher’s exact test p < 0.05). All experiments were repeated three times independently. Results are mean ± s.d. NS, p > 0.05, * p < 0.05, ** p < 0.01, and *** p < 0.001, as determined by one-way ANOVA and Dunnett’s multiple comparison test

Article Snippet: Human anti-PD-L1-Rb (ab213524) and mouse anti-PD-L1-Rb (ab213480) were purchased from Abcam; anti-CD8α-Rb (GB11068 and GB11068-1) was purchased from Servicebio; anti-PD-1-Rb (84651) was purchased from Cell Signaling Technology; the antibodies specific for human anti-MMP2-Rb (10375-2-AP), anti-MMP9-Rb (10373-2-AP), anti-MMP9-Rb (10373-2-AP), anti-GAPDH-M (60004-1-Ig), and anti-PD-L1-M (66248) were purchased from Proteintech; SB-3CT was purchased from Selleck(S7430); and in vivo mAb anti-PD-1-M (BE0146), anti-CTLA-4-M (BE0164), and IgG isotype control (BE0086, BE0089) were purchased from Bioxcell.

Techniques: Expressing, Over Expression, Western Blot, Reverse Transcription Polymerase Chain Reaction

(A) DU145 cells with filamin C silencing were fluorescence-labeled and analyzed in a zebrafish cancer metastasis model. The selected pictures were shown from 0 to 3 days post injection. The areas indicated with arrows were enlarged for visualizing disseminated cancer cells. (B) Filamin C was silenced in DU145 cells and the proenzyme (Pro) and activated form of MMP2 were analyzed. (C) Migration of DU145 cells with or without filamin C silencing were analyzed. The third group with filamin C silencing was further treated with the MMP2 inhibitor ARP100. The statistical analysis results were shown in Figure and the Western blot results were shown in Figure . FLNC, filamin C.

Journal: Oncotarget

Article Title: Filamin C, a dysregulated protein in cancer revealed by label-free quantitative proteomic analyses of human gastric cancer cells

doi:

Figure Lengend Snippet: (A) DU145 cells with filamin C silencing were fluorescence-labeled and analyzed in a zebrafish cancer metastasis model. The selected pictures were shown from 0 to 3 days post injection. The areas indicated with arrows were enlarged for visualizing disseminated cancer cells. (B) Filamin C was silenced in DU145 cells and the proenzyme (Pro) and activated form of MMP2 were analyzed. (C) Migration of DU145 cells with or without filamin C silencing were analyzed. The third group with filamin C silencing was further treated with the MMP2 inhibitor ARP100. The statistical analysis results were shown in Figure and the Western blot results were shown in Figure . FLNC, filamin C.

Article Snippet: Antibody for human MMP2 was purchased from Proteintech (Wuhan, China).

Techniques: Fluorescence, Labeling, Injection, Migration, Western Blot

TEM8 promoted invasion and migration in ovarian cancer cells. A-D. Transwell assay showed that TEM8 overexpression promoted invasion of ovarian cancer cells, however, TEM8 knockdown reversed this effect (n = 9; ×200, scale bar = 100 μm). E-H. Scratch assay showed that TEM8 overexpression promoted migration of ovarian cancer cells, however, TEM8 knockdown reversed this effect (n = 9; ×100, scale bar = 100 μm). I, J. Representative images and quantitation of the western blot showed that the protein expression of MMP2, MMP9, and VEGFA in the TEM8 overexpression/knockdown groups (n = 3). GAPDH was used as an internal control. Data are presented as mean ± SD. *, P < 0.05; **, P < 0.01; ***, P < 0.001.

Journal: American Journal of Translational Research

Article Title: Overexpression of TEM8 promotes ovarian cancer progression via Rac1/Cdc42/JNK and MEK/ERK/STAT3 signaling pathways

doi:

Figure Lengend Snippet: TEM8 promoted invasion and migration in ovarian cancer cells. A-D. Transwell assay showed that TEM8 overexpression promoted invasion of ovarian cancer cells, however, TEM8 knockdown reversed this effect (n = 9; ×200, scale bar = 100 μm). E-H. Scratch assay showed that TEM8 overexpression promoted migration of ovarian cancer cells, however, TEM8 knockdown reversed this effect (n = 9; ×100, scale bar = 100 μm). I, J. Representative images and quantitation of the western blot showed that the protein expression of MMP2, MMP9, and VEGFA in the TEM8 overexpression/knockdown groups (n = 3). GAPDH was used as an internal control. Data are presented as mean ± SD. *, P < 0.05; **, P < 0.01; ***, P < 0.001.

Article Snippet: Proteins were separated using 10% SDS-PAGE, transferred to PVDF membranes and blocked using 5% BSA at room temperature for 2 h. Primary antibodies were incubated at 4°C overnight (dilution ratio of 1:1000): rabbit anti-TEM8 (Abcam, Cambridge, UK), rabbit anti-GATA2 (Abcam, Cambridge, UK), rabbit anti-Rac1 (Abcam, Cambridge, UK), rabbit anti-Cdc42 (Wanleibio, Shenyang, China), rabbit anti-p-Rac1/cdc42 (Cell Signaling Technology, California, USA), rabbit anti-JNK (Cell Signaling Technology, California, USA), mouse anti-p-JNK (Cell Signaling Technology, California, USA), rabbit anti-STAT3 (Wanleibio, Shenyang, China), rabbit anti-MEK (Santa Cruz, USA), rabbit anti-p-MEK (Cell Signaling Technology, California, USA), rabbit anti-ERK (Cell Signaling Technology, California, USA), rabbit anti-p-ERK (Cell Signaling Technology, California, USA), rabbit anti-p-STAT3 (Ser727) (Wanleibio, Shenyang, China), anti-Ki-67 (Wanleibio, Shenyang, China), anti-cyclin D1 (Cell Signaling Technology, California, USA), rabbit anti-MMP2 (Proteintech, Wuhan, China), anti-rabbit MMP9 (Proteintech, Wuhan, China), mouse anti-Bcl2 (Proteintech, Wuhan, China), rabbit anti-Bax (Proteintech, Wuhan, China), rabbit anti-VEGFA (Abcam, Cambridge, UK), mouse anti-GAPDH (1:2000, ZSGB-BIO Technology Co., Ltd., Beijing, China).

Techniques: Migration, Transwell Assay, Over Expression, Wound Healing Assay, Quantitation Assay, Western Blot, Expressing