Binding of MMP-9-degraded fibronectin to β6 integrin promotes invasion via the FAK-Src-related Erk1/2 and PI3K/Akt/Smad-1/5/8 pathways in breast cancer
Fibronectin (FN) has been recognized as the key element in promoting cell adhesion, migration and oncogenic transformation. αvβ6 integrin binds with FN in an RGD-dependent manner and is associated with invasion and poor prognosis in many types of cancers. The extracellular matrix (ECM) is commonly d...
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| Veröffentlicht in: | Oncology reports 2015-09, Vol.34 (3), p.1345-1352 |
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| description | Fibronectin (FN) has been recognized as the key element in promoting cell adhesion, migration and oncogenic transformation. αvβ6 integrin binds with FN in an RGD-dependent manner and is associated with invasion and poor prognosis in many types of cancers. The extracellular matrix (ECM) is commonly degraded and becomes disorganized in cancers. Previous studies have shown that FN can be degraded into fragments by MMP-9 in vitro; MMP-9 expression is upregulated in breast cancer, therefore, the role of degraded FN in breast cancer progression needs to be investigated. In the present study, expression of β6 integrin in breast cancer tissues was analyzed. The data were quite consistent with the hypothesis that β6 integrin expression is an indicator of poor prognosis. Cell surface expression of β6 integrin was correlated with the invasive behavior of the breast cancer cell lines. MMP-9-degraded FN was used to explore its effects on cell invasion and expression of β6 integrin. The results indicated that MMP-9-degraded FN can adjust constituents of the αvβ6 heterodimers at the early phase and significantly elevate amounts of β6 integrin subunits at a later period. To better elucidate the mechanism by which β6 integrin regulates FN-induced cell migration and invasion, we determined the expression and activity of the downstream kinases of β6 integrin, and elucidated that focal adhesion kinase (FAK)-Src interaction promoted the invasion and migration of breast cancer cells after treatment of MMP-9-degraded FN through the Erk1/2 and PI3K/Akt/Smad-1/5/8 pathways. |
| doi_str_mv | 10.3892/or.2015.4103 |
| format | Article |
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The extracellular matrix (ECM) is commonly degraded and becomes disorganized in cancers. Previous studies have shown that FN can be degraded into fragments by MMP-9 in vitro; MMP-9 expression is upregulated in breast cancer, therefore, the role of degraded FN in breast cancer progression needs to be investigated. In the present study, expression of β6 integrin in breast cancer tissues was analyzed. The data were quite consistent with the hypothesis that β6 integrin expression is an indicator of poor prognosis. Cell surface expression of β6 integrin was correlated with the invasive behavior of the breast cancer cell lines. MMP-9-degraded FN was used to explore its effects on cell invasion and expression of β6 integrin. The results indicated that MMP-9-degraded FN can adjust constituents of the αvβ6 heterodimers at the early phase and significantly elevate amounts of β6 integrin subunits at a later period. To better elucidate the mechanism by which β6 integrin regulates FN-induced cell migration and invasion, we determined the expression and activity of the downstream kinases of β6 integrin, and elucidated that focal adhesion kinase (FAK)-Src interaction promoted the invasion and migration of breast cancer cells after treatment of MMP-9-degraded FN through the Erk1/2 and PI3K/Akt/Smad-1/5/8 pathways.</description><identifier>ISSN: 1021-335X</identifier><identifier>EISSN: 1791-2431</identifier><identifier>DOI: 10.3892/or.2015.4103</identifier><identifier>PMID: 26134759</identifier><language>eng</language><publisher>Greece: D.A. Spandidos</publisher><subject>Breast cancer ; Breast Neoplasms - genetics ; Breast Neoplasms - pathology ; Cell adhesion & migration ; Cell Movement - genetics ; Colorectal cancer ; Development and progression ; Female ; fibronectin ; Fibronectins ; Fibronectins - genetics ; Fibronectins - metabolism ; Focal Adhesion Kinase 1 - genetics ; Gene expression ; Gene Expression Regulation, Neoplastic ; Genetic aspects ; Health aspects ; Humans ; Integrin beta Chains - genetics ; Integrin beta Chains - metabolism ; Integrins ; invasion ; Kaplan-Meier Estimate ; Kinases ; MAP Kinase Signaling System - genetics ; Matrix Metalloproteinase 9 - genetics ; Matrix Metalloproteinase 9 - metabolism ; MCF-7 Cells ; Medical prognosis ; Metastasis ; MMP-9 ; Neoplasm Invasiveness - genetics ; Oncogene Protein v-akt - genetics ; Ovarian cancer ; Phosphatidylinositol 3-Kinases - genetics ; Phosphorylation ; Properties ; Proteases ; Proteins ; Proteolysis ; Signal transduction ; Smad Proteins - genetics ; src-Family Kinases - genetics ; Studies ; β6 integrin</subject><ispartof>Oncology reports, 2015-09, Vol.34 (3), p.1345-1352</ispartof><rights>Copyright © 2015, Spandidos Publications</rights><rights>COPYRIGHT 2015 Spandidos Publications</rights><rights>Copyright Spandidos Publications UK Ltd. 2015</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4673-6afdf31c48bbd31a3a4b0a0ed137e7af00f66c812129ceb9f37e3aca8d979e093</citedby><cites>FETCH-LOGICAL-c4673-6afdf31c48bbd31a3a4b0a0ed137e7af00f66c812129ceb9f37e3aca8d979e093</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26134759$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>LI, WENTONG</creatorcontrib><creatorcontrib>LIU, ZHIJUN</creatorcontrib><creatorcontrib>ZHAO, CHUNLING</creatorcontrib><creatorcontrib>ZHAI, LIMIN</creatorcontrib><title>Binding of MMP-9-degraded fibronectin to β6 integrin promotes invasion via the FAK-Src-related Erk1/2 and PI3K/Akt/Smad-1/5/8 pathways in breast cancer</title><title>Oncology reports</title><addtitle>Oncol Rep</addtitle><description>Fibronectin (FN) has been recognized as the key element in promoting cell adhesion, migration and oncogenic transformation. αvβ6 integrin binds with FN in an RGD-dependent manner and is associated with invasion and poor prognosis in many types of cancers. The extracellular matrix (ECM) is commonly degraded and becomes disorganized in cancers. Previous studies have shown that FN can be degraded into fragments by MMP-9 in vitro; MMP-9 expression is upregulated in breast cancer, therefore, the role of degraded FN in breast cancer progression needs to be investigated. In the present study, expression of β6 integrin in breast cancer tissues was analyzed. The data were quite consistent with the hypothesis that β6 integrin expression is an indicator of poor prognosis. Cell surface expression of β6 integrin was correlated with the invasive behavior of the breast cancer cell lines. MMP-9-degraded FN was used to explore its effects on cell invasion and expression of β6 integrin. The results indicated that MMP-9-degraded FN can adjust constituents of the αvβ6 heterodimers at the early phase and significantly elevate amounts of β6 integrin subunits at a later period. To better elucidate the mechanism by which β6 integrin regulates FN-induced cell migration and invasion, we determined the expression and activity of the downstream kinases of β6 integrin, and elucidated that focal adhesion kinase (FAK)-Src interaction promoted the invasion and migration of breast cancer cells after treatment of MMP-9-degraded FN through the Erk1/2 and PI3K/Akt/Smad-1/5/8 pathways.</description><subject>Breast cancer</subject><subject>Breast Neoplasms - genetics</subject><subject>Breast Neoplasms - pathology</subject><subject>Cell adhesion & migration</subject><subject>Cell Movement - genetics</subject><subject>Colorectal cancer</subject><subject>Development and progression</subject><subject>Female</subject><subject>fibronectin</subject><subject>Fibronectins</subject><subject>Fibronectins - genetics</subject><subject>Fibronectins - metabolism</subject><subject>Focal Adhesion Kinase 1 - genetics</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Genetic aspects</subject><subject>Health aspects</subject><subject>Humans</subject><subject>Integrin beta Chains - genetics</subject><subject>Integrin beta Chains - metabolism</subject><subject>Integrins</subject><subject>invasion</subject><subject>Kaplan-Meier Estimate</subject><subject>Kinases</subject><subject>MAP Kinase Signaling System - genetics</subject><subject>Matrix Metalloproteinase 9 - genetics</subject><subject>Matrix Metalloproteinase 9 - metabolism</subject><subject>MCF-7 Cells</subject><subject>Medical prognosis</subject><subject>Metastasis</subject><subject>MMP-9</subject><subject>Neoplasm Invasiveness - genetics</subject><subject>Oncogene Protein v-akt - genetics</subject><subject>Ovarian cancer</subject><subject>Phosphatidylinositol 3-Kinases - genetics</subject><subject>Phosphorylation</subject><subject>Properties</subject><subject>Proteases</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Signal transduction</subject><subject>Smad Proteins - genetics</subject><subject>src-Family Kinases - genetics</subject><subject>Studies</subject><subject>β6 integrin</subject><issn>1021-335X</issn><issn>1791-2431</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><recordid>eNptks9u1DAQxiMEoqVw44wsISEOeOM_iRMfl6qFqq2oVJC4RRPb2XWb2IvtLeqb8Bw8CM-Eo5aWIuSD7fFvPnvGX1G8pGTBW8lKHxaM0HpRUcIfFbu0kRSzitPHeU0YxZzXX3eKZzFeEMIaIuTTYocJyqumlrvFj_fWaetWyA_o9PQMS6zNKoA2Gg22D94ZlaxDyaNfPwWyLuXTvN8EP_lkYo5cQbTeoSsLKK0NOlwe4_OgcDAjpKxyEC5pyRA4jc6O-HG5vEzl-QQa07IuW7SBtP4O17MQ6oOBmJACp0x4XjwZYIzmxe28V3w5PPi8_xGffPpwtL88waoSDccCBj1wqqq27zWnwKHqCRCjKW9MAwMhgxCqpYwyqUwvhxzmoKDVspGGSL5XvL3RzSV925qYuslGZcYRnPHb2NGGMFEzKkRGX_-DXvhtcPl1HZWcibYWXN5TKxhNZ93gUwA1i3bLivOq5aJimVr8h8pDm8mq3PbB5viDhDd_JawNjGkd_bhNufnxIfjuBlTBxxjM0G2CnSBcd5R0s2M6H7rZMd3smIy_ui1q209G38F_LHJ_cdzkT7TaxzvGB8wrTDjOaM1_A0TsxMo</recordid><startdate>201509</startdate><enddate>201509</enddate><creator>LI, WENTONG</creator><creator>LIU, ZHIJUN</creator><creator>ZHAO, CHUNLING</creator><creator>ZHAI, LIMIN</creator><general>D.A. 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genetics</topic><topic>Breast Neoplasms - pathology</topic><topic>Cell adhesion & migration</topic><topic>Cell Movement - genetics</topic><topic>Colorectal cancer</topic><topic>Development and progression</topic><topic>Female</topic><topic>fibronectin</topic><topic>Fibronectins</topic><topic>Fibronectins - genetics</topic><topic>Fibronectins - metabolism</topic><topic>Focal Adhesion Kinase 1 - genetics</topic><topic>Gene expression</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>Genetic aspects</topic><topic>Health aspects</topic><topic>Humans</topic><topic>Integrin beta Chains - genetics</topic><topic>Integrin beta Chains - metabolism</topic><topic>Integrins</topic><topic>invasion</topic><topic>Kaplan-Meier Estimate</topic><topic>Kinases</topic><topic>MAP Kinase Signaling System - genetics</topic><topic>Matrix Metalloproteinase 9 - genetics</topic><topic>Matrix Metalloproteinase 9 - metabolism</topic><topic>MCF-7 Cells</topic><topic>Medical prognosis</topic><topic>Metastasis</topic><topic>MMP-9</topic><topic>Neoplasm Invasiveness - genetics</topic><topic>Oncogene Protein v-akt - genetics</topic><topic>Ovarian cancer</topic><topic>Phosphatidylinositol 3-Kinases - genetics</topic><topic>Phosphorylation</topic><topic>Properties</topic><topic>Proteases</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Signal transduction</topic><topic>Smad Proteins - genetics</topic><topic>src-Family Kinases - genetics</topic><topic>Studies</topic><topic>β6 integrin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>LI, WENTONG</creatorcontrib><creatorcontrib>LIU, ZHIJUN</creatorcontrib><creatorcontrib>ZHAO, CHUNLING</creatorcontrib><creatorcontrib>ZHAI, LIMIN</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>British Nursing Database</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><jtitle>Oncology reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>LI, WENTONG</au><au>LIU, ZHIJUN</au><au>ZHAO, CHUNLING</au><au>ZHAI, LIMIN</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Binding of MMP-9-degraded fibronectin to β6 integrin promotes invasion via the FAK-Src-related Erk1/2 and PI3K/Akt/Smad-1/5/8 pathways in breast cancer</atitle><jtitle>Oncology reports</jtitle><addtitle>Oncol Rep</addtitle><date>2015-09</date><risdate>2015</risdate><volume>34</volume><issue>3</issue><spage>1345</spage><epage>1352</epage><pages>1345-1352</pages><issn>1021-335X</issn><eissn>1791-2431</eissn><abstract>Fibronectin (FN) has been recognized as the key element in promoting cell adhesion, migration and oncogenic transformation. αvβ6 integrin binds with FN in an RGD-dependent manner and is associated with invasion and poor prognosis in many types of cancers. The extracellular matrix (ECM) is commonly degraded and becomes disorganized in cancers. Previous studies have shown that FN can be degraded into fragments by MMP-9 in vitro; MMP-9 expression is upregulated in breast cancer, therefore, the role of degraded FN in breast cancer progression needs to be investigated. In the present study, expression of β6 integrin in breast cancer tissues was analyzed. The data were quite consistent with the hypothesis that β6 integrin expression is an indicator of poor prognosis. Cell surface expression of β6 integrin was correlated with the invasive behavior of the breast cancer cell lines. MMP-9-degraded FN was used to explore its effects on cell invasion and expression of β6 integrin. The results indicated that MMP-9-degraded FN can adjust constituents of the αvβ6 heterodimers at the early phase and significantly elevate amounts of β6 integrin subunits at a later period. To better elucidate the mechanism by which β6 integrin regulates FN-induced cell migration and invasion, we determined the expression and activity of the downstream kinases of β6 integrin, and elucidated that focal adhesion kinase (FAK)-Src interaction promoted the invasion and migration of breast cancer cells after treatment of MMP-9-degraded FN through the Erk1/2 and PI3K/Akt/Smad-1/5/8 pathways.</abstract><cop>Greece</cop><pub>D.A. Spandidos</pub><pmid>26134759</pmid><doi>10.3892/or.2015.4103</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1021-335X |
| ispartof | Oncology reports, 2015-09, Vol.34 (3), p.1345-1352 |
| issn | 1021-335X 1791-2431 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Breast cancer Breast Neoplasms - genetics Breast Neoplasms - pathology Cell adhesion & migration Cell Movement - genetics Colorectal cancer Development and progression Female fibronectin Fibronectins Fibronectins - genetics Fibronectins - metabolism Focal Adhesion Kinase 1 - genetics Gene expression Gene Expression Regulation, Neoplastic Genetic aspects Health aspects Humans Integrin beta Chains - genetics Integrin beta Chains - metabolism Integrins invasion Kaplan-Meier Estimate Kinases MAP Kinase Signaling System - genetics Matrix Metalloproteinase 9 - genetics Matrix Metalloproteinase 9 - metabolism MCF-7 Cells Medical prognosis Metastasis MMP-9 Neoplasm Invasiveness - genetics Oncogene Protein v-akt - genetics Ovarian cancer Phosphatidylinositol 3-Kinases - genetics Phosphorylation Properties Proteases Proteins Proteolysis Signal transduction Smad Proteins - genetics src-Family Kinases - genetics Studies β6 integrin |
| title | Binding of MMP-9-degraded fibronectin to β6 integrin promotes invasion via the FAK-Src-related Erk1/2 and PI3K/Akt/Smad-1/5/8 pathways in breast cancer |
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