Matrix Metalloproteinase Activity in Early-Stage Lung Cancer

Weng, Yuan; Cai, Mingjun; Zhu, Jun; Geng, Jiqun; Zhu, Koujun; Xiao-yin, Jin; Ding, Wei

doi:10.1159/000350304

Cited by 26 publications

(18 citation statements)

References 9 publications

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“…Additionally, MMP-2 and MMP-9 were closely associated with lymph node metastasis, lymphatic invasion and prognosis of gastric cancer (32). Similar results have also been demonstrated in vitro, including gastric, ovarian and laryngeal cancer cells (33)(34)(35).…”

Section: Discussionsupporting

confidence: 78%

Silibinin inhibits the migration and invasion of human gastric cancer SGC7901 cells by downregulating MMP‑2 and MMP‑9 expression via the p38MAPK signaling pathway

Zhang

Chen

et al. 2017

Oncol Lett

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Abstract. The objective of the present study was to observe the effects of silibinin and the p38 mitogen-activated protein kinase (MAPK) signaling pathway inhibitor SB203580 on the migration and invasion capabilities of SGC7901 cells, and to explore the underlying associated mechanisms. Scratch, Transwell and Matrigel invasion assays were performed to study the effects of silibinin on cell migration and invasion. Western blot analysis was used to determine the expression levels of p38MAPK, phosphorylated (p-)p38MAPK, matrix metalloproteinase (MMP)-2 and MMP-9. At the genomic level, quantitative polymerase chain reaction was performed to evaluate the expression levels of MMP-2 and MMP-9. The results of scratch assay indicated that silibinin inhibited the migration capabilities of human gastric cancer SGC7901 cells in a dose-dependent manner. Additionally, Matrigel invasion and Transwell migration assays revealed that silibinin and SB203580 combined treatment significantly reduced the number of invasive cells. Western blot analysis indicated a reduced phosphorylation of p38MAPK without marked changes in p38MAPK expression. In addition, the expression of MMP-2 and MMP-9 significantly decreased in the presence of silibinin, SB203580, and the combination of silibinin and SB203580. In summary, silibinin decreased the invasion and migration abilities of SGC7901 cells by downregulating the expression of MMP-2 and MMP-9 through inhibiting p38MAPK signaling cascades.

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Section: Discussionsupporting

confidence: 78%

Silibinin inhibits the migration and invasion of human gastric cancer SGC7901 cells by downregulating MMP‑2 and MMP‑9 expression via the p38MAPK signaling pathway

Zhang

Chen

et al. 2017

Oncol Lett

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“…The studies of Weng et al [8] and Tsao et al [9] revealed that the activation of MAPK and NF-κB pathways in non-small cell lung cancer (NSCLC) cells promoted the massive production of oxidative, inflammatory and angiogenic factors including reactive oxygen species (ROS), tumor necrosis factor (TNF)-α, intercellular adhesion molecule (ICAM)-1, transforming growth factor (TGF)-β1, vascular endothelial growth factor (VEGF), fibronectin and matrix metalloproteinases (MMPs). Moreover, higher TGF-β1, ICAM-1 and MMP-2 levels in circulation and/or lung tissue were correlated with poor prognosis in NSCLC patients [10,11].…”

Section: Introductionmentioning

confidence: 99%

RETRACTED: Advanced Glycation End-Products Enhance Lung Cancer Cell Invasion and Migration

Hsia

Yin

Mong

2016

IJMS

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Effects of carboxymethyllysine (CML) and pentosidine, two advanced glycation end-products (AGEs), upon invasion and migration in A549 and Calu-6 cells, two non-small cell lung cancer (NSCLC) cell lines were examined. CML or pentosidine at 1, 2, 4, 8 or 16 μmol/L were added into cells. Proliferation, invasion and migration were measured. CML or pentosidine at 4–16 μmol/L promoted invasion and migration in both cell lines, and increased the production of reactive oxygen species, tumor necrosis factor-α, interleukin-6 and transforming growth factor-β1. CML or pentosidine at 2–16 μmol/L up-regulated the protein expression of AGE receptor, p47phox, intercellular adhesion molecule-1 and fibronectin in test NSCLC cells. Matrix metalloproteinase-2 protein expression in A549 and Calu-6 cells was increased by CML or pentosidine at 4–16 μmol/L. These two AGEs at 2–16 μmol/L enhanced nuclear factor κ-B (NF-κ B) p65 protein expression and p38 phosphorylation in A549 cells. However, CML or pentosidine at 4–16 μmol/L up-regulated NF-κB p65 and p-p38 protein expression in Calu-6 cells. These findings suggest that CML and pentosidine, by promoting the invasion, migration and production of associated factors, benefit NSCLC metastasis.

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“…Active MMP-2 and MMP-9 levels in malignant breast tissue were higher compared with that in adjacent tissue, and proMMP-2 levels were significantly higher in adjacent tissue compared with malignant breast tissue, which is consistent with the results of the present study. Weng et al (19) investigated the role of the activity of MMP-2 and MMP-9 in Chinese patients with early-stage lung cancer, revealing that MMP-9 activity decreased, while MMP-2 activity increased, in cancer tissues compared with that in normal samples (19). In addition, in Italian patients with bladder tumors, prostate cancer and renal carcinoma, the majority of cancerous urine samples contained MMP-9 activity, but only a small number contained MMP-2 activity (20–22).…”

Section: Discussionmentioning

confidence: 99%

Matrix metalloproteinases in Vietnamese patients with colorectal cancer

Bui

Hoang

et al. 2017

Oncology Letters

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Matrix metalloproteinases (MMPs), a family of endopeptidases also known as gelatinases, have been reported to affect the acquisition of the cell proliferative, cell invasive and metastatic phenotype of several types of cancer. In particular, the gelatinases MMP-2 and −9 have been revealed to facilitate tumor growth and invasion in patients with colorectal cancer (CRC). However, it is not known whether the gelatinase activity of MMP-2 and −9 is also elevated in Vietnamese patients with CRC. The activity of MMP-2 and −9 in the tissue samples of 103 patients with CRC was evaluated by gelatin zymography and quantified using ImageJ. The association between the level of activity of MMP-2 and −9 and various clinicopathological factors was analyzed, and Chisio BioPAX Editor software was used to visualize the biological pathways regulating the activity of the MMPs. The present study noticed significantly increased activity of active MMP-2 and MMP-9 in tumor tissues (P<0.01), and significantly decreased levels of pro-form MMP-2 and MMP-9 in tumor tissues (P<0.01), compared with that in adjacent tissues in patients with CRC. A correlation between the normalized different activity of MMP-2 and −9 and various clinicopathological features was observed. Furthermore, bioinformatics analysis indicated that the alteration in the activity of MMP-2 and MMP-9 may have been controlled by biological pathways involving the tissue inhibitors of metalloprotease-2 and −1. These findings indicate that the activity of the gelatinases MMP-2 and −9 affects the tumor progression and metastasis of patients with CRC, providing a potential novel approach for determining the prognosis of CRC.

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Matrix Metalloproteinase Activity in Early-Stage Lung Cancer

Cited by 26 publications

References 9 publications

Silibinin inhibits the migration and invasion of human gastric cancer SGC7901 cells by downregulating MMP‑2 and MMP‑9 expression via the p38MAPK signaling pathway

Silibinin inhibits the migration and invasion of human gastric cancer SGC7901 cells by downregulating MMP‑2 and MMP‑9 expression via the p38MAPK signaling pathway

RETRACTED: Advanced Glycation End-Products Enhance Lung Cancer Cell Invasion and Migration

Matrix metalloproteinases in Vietnamese patients with colorectal cancer

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