MMP7 Antibody - #AF0218

Fig. 4. Ecn inhibits the migration and invasion of OS cells. (A) The effect of Ecn on the migration of OS cells (Wound healing assay, 100 ×). (B) The effect of Ecn on the migration of OS cells (Transwell assay, 100 ×). (C) The effect of Ecn on the invasion of OS cells (Matrigel-coated Transwell assay, 100 ×). (D) The effect of Ecn on the protein level of MMP2, MMP7, MMP9, Snail, Vimentin, N-Cadherin and E-Cadherin in OS cells (Western blot). ##P 

FIGURE 2 High glucose induced the expression of MMP‐7 in peritoneal mesothelial cells. (a, b) Peritoneal mesothelial cells were seeded in the 6‐well plate (1 × 106 cells/well) and then stimulated with different concentrations of glucose for 24 hours. The mRNA level of MMP‐7 was detected through quantitative RT‐PCR (a), the protein level of MMP‐7 in the cells was detected by Western blotting analysis (b), and the production of MMP‐7 in the culture medium was detected by ELISA (c). (d‐e) Cells were incubated in dialysate with 4.25% glucose for indicated time points. The mRNA level of MMP‐7 was detected through quantitative RT‐PCR (d), the protein level of MMP‐7 in the cells was detected by Western blotting analysis (e), and the production of MMP‐7 in the culture medium was detected by ELISA (F). *P < 0.05, **P < 0.01, one of the three independent experiments is shown

FIGURE 3 Recombinant MMP‐7 protein up‐regulated cell volume and enhanced aquaporin‐1 expression in peritoneal mesothelial cells. The HMrSV5 cells were seeded in the 6‐well plate (1 × 106 cells/well). (a) Cells were stimulated with MMP‐7 protein for 12 hours, followed by incubating in normal saline (NS) or dialysate with 4.25% glucose for 1 minute. The cell diameter of peritoneal mesothelial cells was evaluated by the Scepter 2.0 cell counter. The changes of cell diameter after glucose stimulation, with or without MMP‐7 incubation, were calculated. (b, c) The cells were treated with 50 ng/ml MMP‐7 for different time points. The mRNA level of AQP‐1 was detected by quantitative RT‐PCR (b), and the protein levels of AQP‐1 were detected by Western blotting (c). (d, e) The cells were treated with different concentrations of MMP‐7 for different time points. The mRNA level of AQP‐1 was detected by quantitative RT‐PCR (d), and the protein levels of AQP‐1 were detected by Western blotting (e). (f) The cells were treated with indicated 50 ng/ml MMP‐7 for 12 hours. The cells were then permeabilized by Triton‐X 100, and immunofluorescence assay was used to detect the expression of AQP‐1 (red, with DAPI‐stained blue nuclei). (g, h) The cells were treated with the indicated 50 ng/ml MMP‐7 for 12 hours. The expression of AQP‐1 in the HMrSV5 cell membrane was evaluated by Western blotting (g) and immunofluorescence assay (H). *P < 0.05, **P < 0.01, one of the three independent experiments is shown

Fig. 3. SEC suppresses the migration and invasion of BC cells. (A) The effect of SEC on the migration of BC cells (Wound healing assay, 100 × ). (B) The effect of SEC on the migration of BC cells (Transwell assay, 100 × ). (C) The effect of SEC on the invasion of BC cells (Matrigel-coated transwell assay, 100 × ). (D) The effect of SEC on the protein levels of EMT markers and MMPs of BC cells (Western blot). Data are shown as mean ± SD from three independent experiments.

Fig. 4 Supplementation of n-3 polyunsaturated fatty acids contributes to improved interstitial fibrosis in rat renal transplantation models. A Schematic view of the establishment of rat renal transplantation models and the dietary mode. B Fatty acid constitution of soybean oil feed (SbOF) and linseed oil feed (LOF). C Gross morphology of bilateral kidneys from SbOF and LOF rats. D, E Masson staining detected the fibrosis level of transplanted kidneys from SbOF and LOF diet rats. F HE staining in heart, liver, spleen, lung, and normal kidney tissues from SbOF and LOF diet rats. G, H IHC detected fibrosis markers in transplanted kidneys from SbOF and LOF diet rats. Significance was determined by Student’s t test.

Figure 3. miR-708-5p suppresses epithelial-to-mesenchymal transition (EMT) of OS cells. (A) mRNA and (C, left column) protein levels of MMP2, MMP7, MMP9, N-cadherin, vimentin, E-cadherin and Snail after miR-708-5p overexpression (708-5p mimics) compared to the scramble negative control (NC mimic) in MG63 cells. (B) mRNA and (C, right column) protein levels of MMP2, MMP9, N-cadherin, vimentin, E-cadherin and Snail after miR-708-5p overexpression (708-5p mimics) compared to the scramble negative control (NC mimic) in SaOS-2 cells. Relative protein expression levels in (D) MG63 and (E) SaOS-2 cells. All data are presented as mean ± SD from at least three independent experiments. *P<0.05, **P<0.01, NC mimic vs. 708-5p mimic. OS, osteosarcoma; MMP, matrix metalloproteinase.

Figure 6 Upregulation of ATF1 promotes the growth of lung adenocarcinoma cells in vivo Upregulation of ATF1 accelerated the xenograft tumor growth of A549 cells. (A) The volumes of xenograft tumors were determined. (B) An image of the xenograft tumor is shown. (C) The weight of xenograft tumors was quantified. (D) The expressions of ZNF143, Ki67, MMP7, and MMP9 were increased in ATF1-overexpressing xenograft tumors, as detected by IHC assay. Data are presented as the mean±SD.