Rapid expression and activation of MMP-2 and MMP-9 upon exposure of human breast cancer cells (MCF-7) to fibronectin in serum free medium

Das, Shamik; Banerji, Aniruddha; Frei, Eva; Chatterjee, Amitava

doi:10.1016/j.lfs.2007.12.013

Cited by 82 publications

(87 citation statements)

References 40 publications

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“…The balance between the two groups was the determinant factor to maintain the stability of the internal environment of ECM. Therefore, MMPs-TIMPs out of balance could cause ECM degradation and BM destruction thereafter tumor metastasis (Xia et al, 2004;Clark et al, 2008;Das et al, 2008;Lee et al, 2009). TIMPs were often synthesized by the same cell secreting MMPs, which could specifically close the catalytic active site and play an important role in ECM remodeling and the invasion, metastasis of tumors.…”

Section: Discussionmentioning

confidence: 99%

Preparation of Microspheres Encapsulating a Recombinant TIMP-1 Adenovirus and their Inhibition of Proliferation of Hepatocellular Carcinoma Cells

Dong¹,

Yao²,

Liu³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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Section: Discussionmentioning

confidence: 99%

Preparation of Microspheres Encapsulating a Recombinant TIMP-1 Adenovirus and their Inhibition of Proliferation of Hepatocellular Carcinoma Cells

Dong¹,

Yao²,

Liu³

et al. 2012

Asian Pacific Journal of Cancer Prevention

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“…Previous studies from our lab on effects of different ECM components on MMP-2 and MMP-9 activities in cancer cell lines indicate that, such responses and the underlying signaling vary according to the type of cancer cells and the type of ECM components used [8,11,12]. Human breast cancer cell line MCF-7, which normally secretes pro-MMP-2, was found to exhibit pro-MMP-9 activity and activation of MMP-2 in presence of soluble fibronectin [8].…”

Section: Discussionmentioning

confidence: 99%

“…of 50 μM each) in SFCM [8] for 1 h at 37°C, 5 % CO 2 . Bay 117085, the NF-κB inhibitor, was treated in 5 and 10 μM concentration [18] for 24 h at 37°C, 5 % CO 2 .…”

Section: Study the Effects Of Cell Signaling Inhibition On Mmpsmentioning

confidence: 99%

“…Gelatinase A (MMP-2) and gelatinase B (MMP-9) readily digest the denatured collagens, gelatins. Both MMP-2 and MMP-9 expression and activity are important for experimental metastasis [8]. Culturing of cells in presence of intact matrix proteins such as fibronectin or laminin or matrix-derived peptides was shown to influence metalloproteinase expression [9,10].…”

Section: Introductionmentioning

confidence: 99%

“…Culturing of cells in presence of intact matrix proteins such as fibronectin or laminin or matrix-derived peptides was shown to influence metalloproteinase expression [9,10]. However, some of our previous works have showed that, different cancer cells exhibit more enhanced gelatinolytic activity upon interaction with intact matrix proteins rather than with their small peptide derivative indicating multivalent ligand receptor interaction is more effective [8,11,12].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Extracellular Matrix Protein Laminin Induces Matrix Metalloproteinase-9 in Human Breast Cancer Cell Line MCF-7

Pal

Moulik

Dutta

et al. 2014

Cancer Microenvironment

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Studies on interaction of tumor cells with extracellular matrix (ECM) components showed increased extracellular protease activity mediated by the family of matrix metalloproteinases (MMPs). Here we studied the effect of human breast cancer cell line MCF-7-laminin (LM) interaction on MMPs and the underlying signaling pathways. Culturing of MCF-7 cells on LM coated surface upregulated MMP-9 expression as well as reduced tissue inhibitor of metalloproteinases-1 (TIMP-1) expression. LM induced MMP-9 expression is abrogated by the blockade of α 2 integrin. Inhibitor studies indicate possible involvement of phosphatidyl-inositol-3-kinase (PI3K), extracellular signal regulated kinase (ERK) and nuclear factor-kappaB (NF-κB) in LM induced signaling. LM treatment also enhanced phosphorylation of FAK (focal adhesion kinase), PI3K, ERK; nuclear translocation of ERK, pERK, NF-κB and cell migration. Our findings indicate that, binding of MCF-7 cells to LM, possibly via α 2 β 1 integrin, induces signaling involving FAK, PI3K, ERK, NF-κB followed by upregulation of MMP-9 and cell migration.

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ADAM8 expression in breast cancer derived brain metastases: Functional implications on MMP‐9 expression and transendothelial migration in breast cancer cells

Conrad

Götte

Schlomann

et al. 2017

Intl Journal of Cancer

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Metastatic breast cancer affects long-term survival and is a major cause of cancer death for women worldwide. The Metalloprotease-Disintegrin ADAM8 promotes breast cancer development and brain metastasis in a mouse breast cancer model. Here, abundant ADAM8 expression was detected in primary human breast tumors and associated brain metastases. To investigate the function of ADAM8 in metastasis, MB-231 breast cancer cells with ADAM8 knockdown (MB-231_shA8) and scramble control cells (MB-231_shCtrl) were analyzed for their capability to develop metastases. In vitro, formation of metastatic complexes in hanging drops is dependent on ADAM8 and blocked by ADAM8 inhibition. MB-231_shA8 in contrast to MB-231_shCtrl cells were impaired in transmigration through an endothelial and a reconstituted blood-brain barrier. Out of 23 MMP and 22 ADAM genes, only the MMP-9 gene was affected by ADAM8 knockdown in MB-231_shA8 cells. Following re-expression of wild-type ADAM8 in contrast to ADAM8 lacking the cytoplasmic domain in MB-231_shA8 cells caused increased levels of activated pERK1/2 and pCREB (S133) that were associated with elevated MMP-9 transcription. Application of ADAM8 and MMP-9 antibodies reduced transmigration of MB-231 cells suggesting that ADAM8 affects transmigration of breast cancer cells by MMP-9 regulation. ADAM8-dependent transmigration was confirmed in Hs578t cells overexpressing ADAM8. Moreover, transmigration of MB-231 and Hs578t cells was significantly reduced for cells treated with an antibody directed against P-selectin glycoprotein ligand (PSGL-1), a substrate of ADAM8. From these data we conclude that ADAM8 promotes early metastatic processes such as transendothelial migration by upregulation of MMP-9 and shedding of PSGL-1 from breast cancer cells.

show abstract

Rapid expression and activation of MMP-2 and MMP-9 upon exposure of human breast cancer cells (MCF-7) to fibronectin in serum free medium

Cited by 82 publications

References 40 publications

Preparation of Microspheres Encapsulating a Recombinant TIMP-1 Adenovirus and their Inhibition of Proliferation of Hepatocellular Carcinoma Cells

Preparation of Microspheres Encapsulating a Recombinant TIMP-1 Adenovirus and their Inhibition of Proliferation of Hepatocellular Carcinoma Cells

Extracellular Matrix Protein Laminin Induces Matrix Metalloproteinase-9 in Human Breast Cancer Cell Line MCF-7

ADAM8 expression in breast cancer derived brain metastases: Functional implications on MMP‐9 expression and transendothelial migration in breast cancer cells

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