Fibronectin affects transient MMP2 gene expression through DNA demethylation changes in non-invasive breast cancer cell lines
Metastasis accounts for more than 90% of cancer deaths. Cells from primary solid tumors may invade adjacent tissues and migrate to distant sites where they establish new colonies. The tumor microenvironment is now recognized as an important participant in the signaling that induces cancer cell migra...
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| creator | Pereira, Isabela T Ramos, Edneia A S Costa, Erico T Camargo, Anamaria A Manica, Graciele C M Klassen, Liliane M B Chequin, Andressa Braun-Prado, Karin Pedrosa, Fábio de O Souza, Emanuel M Costa, Fabricio F Klassen, Giseli |
| description | Metastasis accounts for more than 90% of cancer deaths. Cells from primary solid tumors may invade adjacent tissues and migrate to distant sites where they establish new colonies. The tumor microenvironment is now recognized as an important participant in the signaling that induces cancer cell migration. An essential process for metastasis is extracellular matrix (ECM) degradation by metalloproteases (MMPs), which allows tumor cells to invade local tissues and to reach blood vessels. The members of this protein family include gelatinase A, or MMP-2, which is responsible for the degradation of type IV collagen, the most abundant component of the basal membrane, that separates epithelial cells in the stroma. It is known that fibronectin is capable of promoting the expression of MMP-2 in MCF7 breast cancer cells in culture. In addition, it was already shown that the MMP2 gene expression is regulated by epigenetic mechanisms. In this work, we showed that fibronectin was able to induce MMP2 expression by 30% decrease in its promoter methylation. In addition, a histone marker for an open chromatin conformation was significantly increased. These results indicate a new role for fibronectin in the communication between cancer cells and the ECM, promoting epigenetic modifications. |
| doi_str_mv | 10.1371/journal.pone.0105806 |
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Cells from primary solid tumors may invade adjacent tissues and migrate to distant sites where they establish new colonies. The tumor microenvironment is now recognized as an important participant in the signaling that induces cancer cell migration. An essential process for metastasis is extracellular matrix (ECM) degradation by metalloproteases (MMPs), which allows tumor cells to invade local tissues and to reach blood vessels. The members of this protein family include gelatinase A, or MMP-2, which is responsible for the degradation of type IV collagen, the most abundant component of the basal membrane, that separates epithelial cells in the stroma. It is known that fibronectin is capable of promoting the expression of MMP-2 in MCF7 breast cancer cells in culture. In addition, it was already shown that the MMP2 gene expression is regulated by epigenetic mechanisms. In this work, we showed that fibronectin was able to induce MMP2 expression by 30% decrease in its promoter methylation. In addition, a histone marker for an open chromatin conformation was significantly increased. These results indicate a new role for fibronectin in the communication between cancer cells and the ECM, promoting epigenetic modifications.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0105806</identifier><identifier>PMID: 25208219</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Azacitidine - analogs & derivatives ; Azacitidine - pharmacology ; Base Sequence ; Biochemistry ; Biology and Life Sciences ; Blood vessels ; Breast cancer ; Breast Neoplasms - pathology ; Cancer ; Cancer therapies ; Cell culture ; Cell Line, Tumor ; Cell migration ; Cell Movement - drug effects ; Chromatin ; Collagen (type IV) ; Degradation ; Demethylation ; Deoxyribonucleic acid ; DNA ; DNA methylation ; DNA Methylation - drug effects ; Epigenetics ; Epithelial cells ; Extracellular matrix ; Fibronectin ; Fibronectins - pharmacology ; Gelatinase ; Gelatinase A ; Gene expression ; Gene Expression Regulation, Neoplastic - drug effects ; Gene Expression Regulation, Neoplastic - genetics ; Humans ; Matrix Metalloproteinase 2 - genetics ; Medical research ; Metastases ; Metastasis ; Molecular biology ; Molecular Sequence Data ; Neoplasm Invasiveness ; Oncology ; Pathology ; Promoter Regions, Genetic - genetics ; Proteins ; RNA polymerase ; Solid tumors ; Stroma ; Time Factors ; Tissues ; Transcriptional Activation - drug effects ; Tumor cell lines ; Tumor cells ; Tumors</subject><ispartof>PloS one, 2014-09, Vol.9 (9), p.e105806</ispartof><rights>2014 Pereira et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014 Pereira et al 2014 Pereira et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c592t-df42d1a022cbc5772eb61a404cbba3501f7c3870279db8089d165d44e78431053</citedby><cites>FETCH-LOGICAL-c592t-df42d1a022cbc5772eb61a404cbba3501f7c3870279db8089d165d44e78431053</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4160184/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4160184/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25208219$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pereira, Isabela T</creatorcontrib><creatorcontrib>Ramos, Edneia A S</creatorcontrib><creatorcontrib>Costa, Erico T</creatorcontrib><creatorcontrib>Camargo, Anamaria A</creatorcontrib><creatorcontrib>Manica, Graciele C M</creatorcontrib><creatorcontrib>Klassen, Liliane M B</creatorcontrib><creatorcontrib>Chequin, Andressa</creatorcontrib><creatorcontrib>Braun-Prado, Karin</creatorcontrib><creatorcontrib>Pedrosa, Fábio de O</creatorcontrib><creatorcontrib>Souza, Emanuel M</creatorcontrib><creatorcontrib>Costa, Fabricio F</creatorcontrib><creatorcontrib>Klassen, Giseli</creatorcontrib><title>Fibronectin affects transient MMP2 gene expression through DNA demethylation changes in non-invasive breast cancer cell lines</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Metastasis accounts for more than 90% of cancer deaths. Cells from primary solid tumors may invade adjacent tissues and migrate to distant sites where they establish new colonies. The tumor microenvironment is now recognized as an important participant in the signaling that induces cancer cell migration. An essential process for metastasis is extracellular matrix (ECM) degradation by metalloproteases (MMPs), which allows tumor cells to invade local tissues and to reach blood vessels. The members of this protein family include gelatinase A, or MMP-2, which is responsible for the degradation of type IV collagen, the most abundant component of the basal membrane, that separates epithelial cells in the stroma. It is known that fibronectin is capable of promoting the expression of MMP-2 in MCF7 breast cancer cells in culture. In addition, it was already shown that the MMP2 gene expression is regulated by epigenetic mechanisms. In this work, we showed that fibronectin was able to induce MMP2 expression by 30% decrease in its promoter methylation. In addition, a histone marker for an open chromatin conformation was significantly increased. These results indicate a new role for fibronectin in the communication between cancer cells and the ECM, promoting epigenetic modifications.</description><subject>Azacitidine - analogs & derivatives</subject><subject>Azacitidine - pharmacology</subject><subject>Base Sequence</subject><subject>Biochemistry</subject><subject>Biology and Life Sciences</subject><subject>Blood vessels</subject><subject>Breast cancer</subject><subject>Breast Neoplasms - pathology</subject><subject>Cancer</subject><subject>Cancer therapies</subject><subject>Cell culture</subject><subject>Cell Line, Tumor</subject><subject>Cell migration</subject><subject>Cell Movement - drug effects</subject><subject>Chromatin</subject><subject>Collagen (type IV)</subject><subject>Degradation</subject><subject>Demethylation</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA methylation</subject><subject>DNA Methylation - drug effects</subject><subject>Epigenetics</subject><subject>Epithelial cells</subject><subject>Extracellular matrix</subject><subject>Fibronectin</subject><subject>Fibronectins - pharmacology</subject><subject>Gelatinase</subject><subject>Gelatinase A</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Neoplastic - drug effects</subject><subject>Gene Expression Regulation, Neoplastic - genetics</subject><subject>Humans</subject><subject>Matrix Metalloproteinase 2 - genetics</subject><subject>Medical research</subject><subject>Metastases</subject><subject>Metastasis</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Neoplasm Invasiveness</subject><subject>Oncology</subject><subject>Pathology</subject><subject>Promoter Regions, Genetic - genetics</subject><subject>Proteins</subject><subject>RNA polymerase</subject><subject>Solid tumors</subject><subject>Stroma</subject><subject>Time Factors</subject><subject>Tissues</subject><subject>Transcriptional Activation - drug effects</subject><subject>Tumor cell lines</subject><subject>Tumor cells</subject><subject>Tumors</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNp1UstuEzEUHSEQLYE_QGCJdYJfY3s2SFWhUKkFFrC2PPadGUcTO9hORBf9907ItGoXrHzlex5XR6eq3hK8IkySj-u4S8GMq20MsMIE1wqLZ9UpaRhdCorZ80fzSfUq5zXGNVNCvKxOaE2xoqQ5rW4vfJsmBVt8QKbrpiGjkkzIHkJB19c_KeohAIK_2wQ5-xhQGVLc9QP6_P0MOdhAGW5GUw4bO5jQQ0aTVohh6cPeZL8H1CYwuSBrgoWELIwjGn2A_Lp60Zkxw5v5XVS_L778Ov-2vPrx9fL87Gpp64aWpes4dcRgSm1raykptIIYjrltW8NqTDppmZKYysa1CqvGEVE7zkEqzqZk2KJ6f9TdjjHrObmsSS0IVVRSMiEujwgXzVpvk9-YdKOj8frfR0y9Nql4O4LuaqEmG946Jzm4xtRGdEo2nArJjKCT1qfZbdduwNkpyGTGJ6JPN8EPuo97zYnAZDp5UX2YBVL8s4Nc_nMyP6Jsijkn6B4cCNaHityz9KEieq7IRHv3-LoH0n0n2B3SAbvC</recordid><startdate>20140910</startdate><enddate>20140910</enddate><creator>Pereira, Isabela T</creator><creator>Ramos, Edneia A S</creator><creator>Costa, Erico T</creator><creator>Camargo, Anamaria A</creator><creator>Manica, Graciele C M</creator><creator>Klassen, Liliane M B</creator><creator>Chequin, Andressa</creator><creator>Braun-Prado, Karin</creator><creator>Pedrosa, Fábio de O</creator><creator>Souza, Emanuel M</creator><creator>Costa, Fabricio F</creator><creator>Klassen, Giseli</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20140910</creationdate><title>Fibronectin affects transient MMP2 gene expression through DNA demethylation changes in non-invasive breast cancer cell lines</title><author>Pereira, Isabela T ; Ramos, Edneia A S ; Costa, Erico T ; Camargo, Anamaria A ; Manica, Graciele C M ; Klassen, Liliane M B ; Chequin, Andressa ; Braun-Prado, Karin ; Pedrosa, Fábio de O ; Souza, Emanuel M ; Costa, Fabricio F ; Klassen, Giseli</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c592t-df42d1a022cbc5772eb61a404cbba3501f7c3870279db8089d165d44e78431053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Azacitidine - 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Cells from primary solid tumors may invade adjacent tissues and migrate to distant sites where they establish new colonies. The tumor microenvironment is now recognized as an important participant in the signaling that induces cancer cell migration. An essential process for metastasis is extracellular matrix (ECM) degradation by metalloproteases (MMPs), which allows tumor cells to invade local tissues and to reach blood vessels. The members of this protein family include gelatinase A, or MMP-2, which is responsible for the degradation of type IV collagen, the most abundant component of the basal membrane, that separates epithelial cells in the stroma. It is known that fibronectin is capable of promoting the expression of MMP-2 in MCF7 breast cancer cells in culture. In addition, it was already shown that the MMP2 gene expression is regulated by epigenetic mechanisms. In this work, we showed that fibronectin was able to induce MMP2 expression by 30% decrease in its promoter methylation. In addition, a histone marker for an open chromatin conformation was significantly increased. These results indicate a new role for fibronectin in the communication between cancer cells and the ECM, promoting epigenetic modifications.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25208219</pmid><doi>10.1371/journal.pone.0105806</doi><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2014-09, Vol.9 (9), p.e105806 |
| issn | 1932-6203 1932-6203 |
| language | eng |
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| source | PubMed (Medline); MEDLINE; Public Library of Science; Free Full-Text Journals in Chemistry; DOAJ: Directory of Open Access Journals; EZB Electronic Journals Library |
| subjects | Azacitidine - analogs & derivatives Azacitidine - pharmacology Base Sequence Biochemistry Biology and Life Sciences Blood vessels Breast cancer Breast Neoplasms - pathology Cancer Cancer therapies Cell culture Cell Line, Tumor Cell migration Cell Movement - drug effects Chromatin Collagen (type IV) Degradation Demethylation Deoxyribonucleic acid DNA DNA methylation DNA Methylation - drug effects Epigenetics Epithelial cells Extracellular matrix Fibronectin Fibronectins - pharmacology Gelatinase Gelatinase A Gene expression Gene Expression Regulation, Neoplastic - drug effects Gene Expression Regulation, Neoplastic - genetics Humans Matrix Metalloproteinase 2 - genetics Medical research Metastases Metastasis Molecular biology Molecular Sequence Data Neoplasm Invasiveness Oncology Pathology Promoter Regions, Genetic - genetics Proteins RNA polymerase Solid tumors Stroma Time Factors Tissues Transcriptional Activation - drug effects Tumor cell lines Tumor cells Tumors |
| title | Fibronectin affects transient MMP2 gene expression through DNA demethylation changes in non-invasive breast cancer cell lines |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-07T19%3A16%3A21IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_plos_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Fibronectin%20affects%20transient%20MMP2%20gene%20expression%20through%20DNA%20demethylation%20changes%20in%20non-invasive%20breast%20cancer%20cell%20lines&rft.jtitle=PloS%20one&rft.au=Pereira,%20Isabela%20T&rft.date=2014-09-10&rft.volume=9&rft.issue=9&rft.spage=e105806&rft.pages=e105806-&rft.issn=1932-6203&rft.eissn=1932-6203&rft_id=info:doi/10.1371/journal.pone.0105806&rft_dat=%3Cproquest_plos_%3E3428783041%3C/proquest_plos_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1561282721&rft_id=info:pmid/25208219&rft_doaj_id=oai_doaj_org_article_f568db84bdd74ed9a5a6f87942673a62&rfr_iscdi=true |