Inhibition of MT1-MMP proteolytic function and ERK1/2 signalling influences cell migration and invasion through changes in MMP-2 and MMP-9 levels
Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP-14) is a unique protease that cleaves extracellular proteins, activates proMMPs, and initiates intracellular signalling. MCF-7 cells are non-invasive and deficient in MT1-MMP, MMP-2, and MMP-9 expression. We created an MCF-7 cell line (C2) that...
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| Published in: | Journal of cell communication and signaling Vol. 11; no. 2; pp. 167 - 179 |
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| Main Authors: | , , , |
| Format: | Journal Article |
| Language: | English |
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Dordrecht
Springer Netherlands
01.06.2017
John Wiley & Sons, Inc |
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| ISSN: | 1873-9601, 1873-961X |
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| Abstract | Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP-14) is a unique protease that cleaves extracellular proteins, activates proMMPs, and initiates intracellular signalling. MCF-7 cells are non-invasive and deficient in MT1-MMP, MMP-2, and MMP-9 expression. We created an MCF-7 cell line (C2) that stably produces active MT1-MMP and demonstrated increased ERK1/2 phosphorylation. MAPK inhibition in this cell line showed an inverse relationship in MMP-2 and MMP-9 transcripts where levels of these genes increased and decreased, respectively. Using invasive MDA-MB 231 cells that endogenously produce MT1-MMP and have naturally high pERK levels, we demonstrated the identical inverse relationship between MMP-2 and -9 transcript and protein levels, suggesting that this novel relationship is conserved amongst MT1-MMP positive breast cancer cells. To further analyze the relationship between MMP-2 and -9 levels, we chemically inhibited activation and catalytic activity of MT1-MMP using a furin and MMP inhibitor, respectively, to show that interference with the functions of MT1-MMP induced changes in MMP-2 and 9 transcript levels that were always inverse of each other, and likely mediated by differential transcriptional activity of the NF-κB transcription factor. Furthermore, we analyzed the functional consequences of these expression changes to show MMP, and in particular ERK, inhibition decreased migration and invasion using 2D culture, and inhibits the formation of an invasive phenotype in Matrigel 3D culture. This study demonstrated a novel inverse transcriptional relationship between MMP-2 and -9 levels and MT1-MMP activity that have functional consequences, and also showed that increases in the levels of MMPs does not necessarily correlate with an invasive phenotype. |
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| AbstractList | Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP-14) is a unique protease that cleaves extracellular proteins, activates proMMPs, and initiates intracellular signalling. MCF-7 cells are non-invasive and deficient in MT1-MMP, MMP-2, and MMP-9 expression. We created an MCF-7 cell line (C2) that stably produces active MT1-MMP and demonstrated increased ERK1/2 phosphorylation. MAPK inhibition in this cell line showed an inverse relationship in MMP-2 and MMP-9 transcripts where levels of these genes increased and decreased, respectively. Using invasive MDA-MB 231 cells that endogenously produce MT1-MMP and have naturally high pERK levels, we demonstrated the identical inverse relationship between MMP-2 and -9 transcript and protein levels, suggesting that this novel relationship is conserved amongst MT1-MMP positive breast cancer cells. To further analyze the relationship between MMP-2 and -9 levels, we chemically inhibited activation and catalytic activity of MT1-MMP using a furin and MMP inhibitor, respectively, to show that interference with the functions of MT1-MMP induced changes in MMP-2 and 9 transcript levels that were always inverse of each other, and likely mediated by differential transcriptional activity of the NF-κB transcription factor. Furthermore, we analyzed the functional consequences of these expression changes to show MMP, and in particular ERK, inhibition decreased migration and invasion using 2D culture, and inhibits the formation of an invasive phenotype in Matrigel 3D culture. This study demonstrated a novel inverse transcriptional relationship between MMP-2 and -9 levels and MT1-MMP activity that have functional consequences, and also showed that increases in the levels of MMPs does not necessarily correlate with an invasive phenotype. Membrane type‐1 matrix metalloproteinase (MT1‐MMP, MMP‐14) is a unique protease that cleaves extracellular proteins, activates proMMPs, and initiates intracellular signalling. MCF‐7 cells are non‐invasive and deficient in MT1‐MMP, MMP‐2, and MMP‐9 expression. We created an MCF‐7 cell line (C2) that stably produces active MT1‐MMP and demonstrated increased ERK1/2 phosphorylation. MAPK inhibition in this cell line showed an inverse relationship in MMP‐2 and MMP‐9 transcripts where levels of these genes increased and decreased, respectively. Using invasive MDA‐MB 231 cells that endogenously produce MT1‐MMP and have naturally high pERK levels, we demonstrated the identical inverse relationship between MMP‐2 and ‐9 transcript and protein levels, suggesting that this novel relationship is conserved amongst MT1‐MMP positive breast cancer cells. To further analyze the relationship between MMP‐2 and ‐9 levels, we chemically inhibited activation and catalytic activity of MT1‐MMP using a furin and MMP inhibitor, respectively, to show that interference with the functions of MT1‐MMP induced changes in MMP‐2 and 9 transcript levels that were always inverse of each other, and likely mediated by differential transcriptional activity of the NF‐κB transcription factor. Furthermore, we analyzed the functional consequences of these expression changes to show MMP, and in particular ERK, inhibition decreased migration and invasion using 2D culture, and inhibits the formation of an invasive phenotype in Matrigel 3D culture. This study demonstrated a novel inverse transcriptional relationship between MMP‐2 and ‐9 levels and MT1‐MMP activity that have functional consequences, and also showed that increases in the levels of MMPs does not necessarily correlate with an invasive phenotype. Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP-14) is a unique protease that cleaves extracellular proteins, activates proMMPs, and initiates intracellular signalling. MCF-7 cells are non-invasive and deficient in MT1-MMP, MMP-2, and MMP-9 expression. We created an MCF-7 cell line (C2) that stably produces active MT1-MMP and demonstrated increased ERK1/2 phosphorylation. MAPK inhibition in this cell line showed an inverse relationship in MMP-2 and MMP-9 transcripts where levels of these genes increased and decreased, respectively. Using invasive MDA-MB 231 cells that endogenously produce MT1-MMP and have naturally high pERK levels, we demonstrated the identical inverse relationship between MMP-2 and -9 transcript and protein levels, suggesting that this novel relationship is conserved amongst MT1-MMP positive breast cancer cells. To further analyze the relationship between MMP-2 and -9 levels, we chemically inhibited activation and catalytic activity of MT1-MMP using a furin and MMP inhibitor, respectively, to show that interference with the functions of MT1-MMP induced changes in MMP-2 and 9 transcript levels that were always inverse of each other, and likely mediated by differential transcriptional activity of the NF-κB transcription factor. Furthermore, we analyzed the functional consequences of these expression changes to show MMP, and in particular ERK, inhibition decreased migration and invasion using 2D culture, and inhibits the formation of an invasive phenotype in Matrigel 3D culture. This study demonstrated a novel inverse transcriptional relationship between MMP-2 and -9 levels and MT1-MMP activity that have functional consequences, and also showed that increases in the levels of MMPs does not necessarily correlate with an invasive phenotype.Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP-14) is a unique protease that cleaves extracellular proteins, activates proMMPs, and initiates intracellular signalling. MCF-7 cells are non-invasive and deficient in MT1-MMP, MMP-2, and MMP-9 expression. We created an MCF-7 cell line (C2) that stably produces active MT1-MMP and demonstrated increased ERK1/2 phosphorylation. MAPK inhibition in this cell line showed an inverse relationship in MMP-2 and MMP-9 transcripts where levels of these genes increased and decreased, respectively. Using invasive MDA-MB 231 cells that endogenously produce MT1-MMP and have naturally high pERK levels, we demonstrated the identical inverse relationship between MMP-2 and -9 transcript and protein levels, suggesting that this novel relationship is conserved amongst MT1-MMP positive breast cancer cells. To further analyze the relationship between MMP-2 and -9 levels, we chemically inhibited activation and catalytic activity of MT1-MMP using a furin and MMP inhibitor, respectively, to show that interference with the functions of MT1-MMP induced changes in MMP-2 and 9 transcript levels that were always inverse of each other, and likely mediated by differential transcriptional activity of the NF-κB transcription factor. Furthermore, we analyzed the functional consequences of these expression changes to show MMP, and in particular ERK, inhibition decreased migration and invasion using 2D culture, and inhibits the formation of an invasive phenotype in Matrigel 3D culture. This study demonstrated a novel inverse transcriptional relationship between MMP-2 and -9 levels and MT1-MMP activity that have functional consequences, and also showed that increases in the levels of MMPs does not necessarily correlate with an invasive phenotype. |
| Author | Damjanovski, Sashko Cepeda, Mario A. Evered, Caitlin L. Pelling, Jacob J. H . |
| Author_xml | – sequence: 1 givenname: Mario A. surname: Cepeda fullname: Cepeda, Mario A. organization: Department of Biology, Faculty of Science, University of Western Ontario – sequence: 2 givenname: Caitlin L. surname: Evered fullname: Evered, Caitlin L. organization: Department of Biology, Faculty of Science, University of Western Ontario – sequence: 3 givenname: Jacob J. H . surname: Pelling fullname: Pelling, Jacob J. H . organization: Department of Biology, Faculty of Science, University of Western Ontario – sequence: 4 givenname: Sashko orcidid: 0000-0002-3479-721X surname: Damjanovski fullname: Damjanovski, Sashko email: sdamjano@uwo.ca organization: Department of Biology, Faculty of Science, University of Western Ontario, Lawson Health Research Institute |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/28070797$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1038_s41598_019_50141_z crossref_primary_10_1155_2019_1061979 crossref_primary_10_3390_cells8030203 crossref_primary_10_1016_j_biopha_2017_08_049 crossref_primary_10_1186_s12885_019_5768_0 crossref_primary_10_3892_ijmm_2017_3288 crossref_primary_10_1186_s40709_019_0108_8 crossref_primary_10_1007_s00259_019_04607_x crossref_primary_10_3892_mmr_2018_8950 crossref_primary_10_1016_j_taap_2021_115593 crossref_primary_10_1002_ijc_30714 crossref_primary_10_1038_s41374_018_0150_4 crossref_primary_10_1016_j_bioorg_2025_108729 crossref_primary_10_1016_j_ejcb_2017_04_002 crossref_primary_10_3390_biom10010032 crossref_primary_10_1007_s43032_021_00686_0 crossref_primary_10_1007_s12079_017_0407_5 |
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| Keywords | MMP inhibition ERK signalling MT1-MMP 3D culture MMP-2 Cell migration |
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| Snippet | Membrane type-1 matrix metalloproteinase (MT1-MMP, MMP-14) is a unique protease that cleaves extracellular proteins, activates proMMPs, and initiates... Membrane type‐1 matrix metalloproteinase (MT1‐MMP, MMP‐14) is a unique protease that cleaves extracellular proteins, activates proMMPs, and initiates... |
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| SubjectTerms | 3D culture Biomedical and Life Sciences Biomedicine Breast cancer Cell adhesion & migration Cell Biology Cell culture Cell migration ERK signalling Extracellular signal-regulated kinase Furin Gelatinase A Gelatinase B Intracellular signalling Kinases Life Sciences MAP kinase Matrix metalloproteinase Metalloproteinase MMP inhibition MMP‐2 MT1‐MMP Phosphorylation Proteinase Proteolysis Research Article |
| Title | Inhibition of MT1-MMP proteolytic function and ERK1/2 signalling influences cell migration and invasion through changes in MMP-2 and MMP-9 levels |
| URI | https://link.springer.com/article/10.1007/s12079-016-0373-3 https://onlinelibrary.wiley.com/doi/abs/10.1007%2Fs12079-016-0373-3 https://www.ncbi.nlm.nih.gov/pubmed/28070797 https://www.proquest.com/docview/1901406211 https://www.proquest.com/docview/1857370189 https://pubmed.ncbi.nlm.nih.gov/PMC5440346 |
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