Antibodies blocking adhesion and matrix binding domains of laminin‐332 inhibit tumor growth and metastasis in vivo
Laminin‐332 (LN‐332), which is essential for epithelial cell adhesion and migration, is up‐regulated in most invasive carcinomas. Association between LN‐332 and carcinoma cell integrins and stroma collagen is thought to be important for tumor growth and metastasis. Here, we show that function blocki...
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| Veröffentlicht in: | International journal of cancer 2009-10, Vol.125 (8), p.1814-1825 |
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| container_title | International journal of cancer |
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| creator | Salo, Sirpa Boutaud, Ariel Hansen, Anker Jon He, Liqun Sun, Yi Morales, Sylvia Venturini, Amy Martin, Paula Nokelainen, Pasi Betsholtz, Christer Mathiasen, Ida Stenfeldt Tryggvason, Karl |
| description | Laminin‐332 (LN‐332), which is essential for epithelial cell adhesion and migration, is up‐regulated in most invasive carcinomas. Association between LN‐332 and carcinoma cell integrins and stroma collagen is thought to be important for tumor growth and metastasis. Here, we show that function blocking LN‐332 antibodies interfering with cellular adhesion and migration in vitro evoke apoptotic pathways. The antibodies also target epithelial tumors in vivo. Antibodies against the cell binding domain of the α3 chain of LN‐332 inhibited tumor growth by up to 68%, and antibodies against the matrix binding domains of the β3 and γ2 chains significantly decreased lung metastases. The LN‐332 antibodies appear to induce tumor cell anoikis and subsequent programmed cell death and reduce migration by interfering with tumor cell matrix interactions. © 2009 UICC |
| doi_str_mv | 10.1002/ijc.24532 |
| format | Article |
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Association between LN‐332 and carcinoma cell integrins and stroma collagen is thought to be important for tumor growth and metastasis. Here, we show that function blocking LN‐332 antibodies interfering with cellular adhesion and migration in vitro evoke apoptotic pathways. The antibodies also target epithelial tumors in vivo. Antibodies against the cell binding domain of the α3 chain of LN‐332 inhibited tumor growth by up to 68%, and antibodies against the matrix binding domains of the β3 and γ2 chains significantly decreased lung metastases. The LN‐332 antibodies appear to induce tumor cell anoikis and subsequent programmed cell death and reduce migration by interfering with tumor cell matrix interactions. © 2009 UICC</description><identifier>ISSN: 0020-7136</identifier><identifier>ISSN: 1097-0215</identifier><identifier>EISSN: 1097-0215</identifier><identifier>DOI: 10.1002/ijc.24532</identifier><identifier>PMID: 19582877</identifier><identifier>CODEN: IJCNAW</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Adenocarcinoma - immunology ; Adenocarcinoma - pathology ; Animals ; Antibodies, Blocking - therapeutic use ; Antibodies, Monoclonal - therapeutic use ; Antineoplastic agents ; basement membranes ; Biological and medical sciences ; Carcinoma, Squamous Cell - immunology ; Carcinoma, Squamous Cell - pathology ; Cell Adhesion - drug effects ; Cell Adhesion Molecules - immunology ; Cell Movement ; Cell Proliferation ; Extracellular Matrix - metabolism ; Female ; Gene Expression Profiling ; Gene Expression Regulation, Neoplastic ; Humans ; Immunotherapy ; Kalinin ; laminin ; Lung Neoplasms - immunology ; Lung Neoplasms - pathology ; Male ; Medical sciences ; Medicin och hälsovetenskap ; metastasis ; Mice ; Mice, Inbred DBA ; Mice, Nude ; Multiple tumors. Solid tumors. Tumors in childhood (general aspects) ; Oligonucleotide Array Sequence Analysis ; Pharmacology. Drug treatments ; Tumor Cells, Cultured ; Tumors</subject><ispartof>International journal of cancer, 2009-10, Vol.125 (8), p.1814-1825</ispartof><rights>Copyright © 2009 UICC</rights><rights>2009 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5422-c80992859ca764a9d190c0f3c94ac4db17428b305fa8fa209046ae3892964b893</citedby><cites>FETCH-LOGICAL-c5422-c80992859ca764a9d190c0f3c94ac4db17428b305fa8fa209046ae3892964b893</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fijc.24532$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fijc.24532$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>230,314,780,784,885,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21884860$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19582877$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:119363091$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Salo, Sirpa</creatorcontrib><creatorcontrib>Boutaud, Ariel</creatorcontrib><creatorcontrib>Hansen, Anker Jon</creatorcontrib><creatorcontrib>He, Liqun</creatorcontrib><creatorcontrib>Sun, Yi</creatorcontrib><creatorcontrib>Morales, Sylvia</creatorcontrib><creatorcontrib>Venturini, Amy</creatorcontrib><creatorcontrib>Martin, Paula</creatorcontrib><creatorcontrib>Nokelainen, Pasi</creatorcontrib><creatorcontrib>Betsholtz, Christer</creatorcontrib><creatorcontrib>Mathiasen, Ida Stenfeldt</creatorcontrib><creatorcontrib>Tryggvason, Karl</creatorcontrib><title>Antibodies blocking adhesion and matrix binding domains of laminin‐332 inhibit tumor growth and metastasis in vivo</title><title>International journal of cancer</title><addtitle>Int J Cancer</addtitle><description>Laminin‐332 (LN‐332), which is essential for epithelial cell adhesion and migration, is up‐regulated in most invasive carcinomas. Association between LN‐332 and carcinoma cell integrins and stroma collagen is thought to be important for tumor growth and metastasis. Here, we show that function blocking LN‐332 antibodies interfering with cellular adhesion and migration in vitro evoke apoptotic pathways. The antibodies also target epithelial tumors in vivo. Antibodies against the cell binding domain of the α3 chain of LN‐332 inhibited tumor growth by up to 68%, and antibodies against the matrix binding domains of the β3 and γ2 chains significantly decreased lung metastases. The LN‐332 antibodies appear to induce tumor cell anoikis and subsequent programmed cell death and reduce migration by interfering with tumor cell matrix interactions. © 2009 UICC</description><subject>Adenocarcinoma - immunology</subject><subject>Adenocarcinoma - pathology</subject><subject>Animals</subject><subject>Antibodies, Blocking - therapeutic use</subject><subject>Antibodies, Monoclonal - therapeutic use</subject><subject>Antineoplastic agents</subject><subject>basement membranes</subject><subject>Biological and medical sciences</subject><subject>Carcinoma, Squamous Cell - immunology</subject><subject>Carcinoma, Squamous Cell - pathology</subject><subject>Cell Adhesion - drug effects</subject><subject>Cell Adhesion Molecules - immunology</subject><subject>Cell Movement</subject><subject>Cell Proliferation</subject><subject>Extracellular Matrix - metabolism</subject><subject>Female</subject><subject>Gene Expression Profiling</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Humans</subject><subject>Immunotherapy</subject><subject>Kalinin</subject><subject>laminin</subject><subject>Lung Neoplasms - immunology</subject><subject>Lung Neoplasms - pathology</subject><subject>Male</subject><subject>Medical sciences</subject><subject>Medicin och hälsovetenskap</subject><subject>metastasis</subject><subject>Mice</subject><subject>Mice, Inbred DBA</subject><subject>Mice, Nude</subject><subject>Multiple tumors. Solid tumors. Tumors in childhood (general aspects)</subject><subject>Oligonucleotide Array Sequence Analysis</subject><subject>Pharmacology. Drug treatments</subject><subject>Tumor Cells, Cultured</subject><subject>Tumors</subject><issn>0020-7136</issn><issn>1097-0215</issn><issn>1097-0215</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kc9u1DAQxi0EokvhwAsgXzhwSOu_iX2sVvxpVYkLnKOJ7XSnTexVnHbpjUfgGXkSvGTbniqN5NHM7_vG0kfIe85OOGPiFK_diVBaihdkxZltKia4fklWZceqhsv6iLzJ-ZoxzjVTr8kRt9oI0zQrMp_FGbvkMWTaDcndYLyi4DchY4oUoqcjzBP-oh1Gv9_5NALGTFNPBxgxYvz7-4-UgmLcYIcznW_HNNGrKe3mzWIQZsilMBeG3uFdekte9TDk8O7wHpOfXz7_WH-rLr9_PV-fXVZOKyEqZ5i1wmjroKkVWM8tc6yXzipwyne8UcJ0kukeTA-CWaZqCNJYYWvVGSuPSbX45l3Y3nbtdsIRpvs2AbaH0U3pQqt1wzkrvH2W307JP4kehJxbWUtmedF-WrRuSjlPoX9Uc9buU2pLSu3_lAr7YWGL2Rj8E3mIpQAfDwBkB0M_QXSYHznBjVGm3n_4dOF2OIT75y-25xfr5fQ_sA6rjw</recordid><startdate>20091015</startdate><enddate>20091015</enddate><creator>Salo, Sirpa</creator><creator>Boutaud, Ariel</creator><creator>Hansen, Anker Jon</creator><creator>He, Liqun</creator><creator>Sun, Yi</creator><creator>Morales, Sylvia</creator><creator>Venturini, Amy</creator><creator>Martin, Paula</creator><creator>Nokelainen, Pasi</creator><creator>Betsholtz, Christer</creator><creator>Mathiasen, Ida Stenfeldt</creator><creator>Tryggvason, Karl</creator><general>Wiley Subscription Services, Inc., A Wiley Company</general><general>Wiley-Blackwell</general><scope>IQODW</scope><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>ADTPV</scope><scope>AOWAS</scope></search><sort><creationdate>20091015</creationdate><title>Antibodies blocking adhesion and matrix binding domains of laminin‐332 inhibit tumor growth and metastasis in vivo</title><author>Salo, Sirpa ; Boutaud, Ariel ; Hansen, Anker Jon ; He, Liqun ; Sun, Yi ; Morales, Sylvia ; Venturini, Amy ; Martin, Paula ; Nokelainen, Pasi ; Betsholtz, Christer ; Mathiasen, Ida Stenfeldt ; Tryggvason, Karl</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5422-c80992859ca764a9d190c0f3c94ac4db17428b305fa8fa209046ae3892964b893</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Adenocarcinoma - immunology</topic><topic>Adenocarcinoma - pathology</topic><topic>Animals</topic><topic>Antibodies, Blocking - therapeutic use</topic><topic>Antibodies, Monoclonal - therapeutic use</topic><topic>Antineoplastic agents</topic><topic>basement membranes</topic><topic>Biological and medical sciences</topic><topic>Carcinoma, Squamous Cell - immunology</topic><topic>Carcinoma, Squamous Cell - pathology</topic><topic>Cell Adhesion - drug effects</topic><topic>Cell Adhesion Molecules - immunology</topic><topic>Cell Movement</topic><topic>Cell Proliferation</topic><topic>Extracellular Matrix - metabolism</topic><topic>Female</topic><topic>Gene Expression Profiling</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>Humans</topic><topic>Immunotherapy</topic><topic>Kalinin</topic><topic>laminin</topic><topic>Lung Neoplasms - immunology</topic><topic>Lung Neoplasms - pathology</topic><topic>Male</topic><topic>Medical sciences</topic><topic>Medicin och hälsovetenskap</topic><topic>metastasis</topic><topic>Mice</topic><topic>Mice, Inbred DBA</topic><topic>Mice, Nude</topic><topic>Multiple tumors. Solid tumors. Tumors in childhood (general aspects)</topic><topic>Oligonucleotide Array Sequence Analysis</topic><topic>Pharmacology. Drug treatments</topic><topic>Tumor Cells, Cultured</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Salo, Sirpa</creatorcontrib><creatorcontrib>Boutaud, Ariel</creatorcontrib><creatorcontrib>Hansen, Anker Jon</creatorcontrib><creatorcontrib>He, Liqun</creatorcontrib><creatorcontrib>Sun, Yi</creatorcontrib><creatorcontrib>Morales, Sylvia</creatorcontrib><creatorcontrib>Venturini, Amy</creatorcontrib><creatorcontrib>Martin, Paula</creatorcontrib><creatorcontrib>Nokelainen, Pasi</creatorcontrib><creatorcontrib>Betsholtz, Christer</creatorcontrib><creatorcontrib>Mathiasen, Ida Stenfeldt</creatorcontrib><creatorcontrib>Tryggvason, Karl</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>SwePub</collection><collection>SwePub Articles</collection><jtitle>International journal of cancer</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Salo, Sirpa</au><au>Boutaud, Ariel</au><au>Hansen, Anker Jon</au><au>He, Liqun</au><au>Sun, Yi</au><au>Morales, Sylvia</au><au>Venturini, Amy</au><au>Martin, Paula</au><au>Nokelainen, Pasi</au><au>Betsholtz, Christer</au><au>Mathiasen, Ida Stenfeldt</au><au>Tryggvason, Karl</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antibodies blocking adhesion and matrix binding domains of laminin‐332 inhibit tumor growth and metastasis in vivo</atitle><jtitle>International journal of cancer</jtitle><addtitle>Int J Cancer</addtitle><date>2009-10-15</date><risdate>2009</risdate><volume>125</volume><issue>8</issue><spage>1814</spage><epage>1825</epage><pages>1814-1825</pages><issn>0020-7136</issn><issn>1097-0215</issn><eissn>1097-0215</eissn><coden>IJCNAW</coden><abstract>Laminin‐332 (LN‐332), which is essential for epithelial cell adhesion and migration, is up‐regulated in most invasive carcinomas. Association between LN‐332 and carcinoma cell integrins and stroma collagen is thought to be important for tumor growth and metastasis. Here, we show that function blocking LN‐332 antibodies interfering with cellular adhesion and migration in vitro evoke apoptotic pathways. The antibodies also target epithelial tumors in vivo. Antibodies against the cell binding domain of the α3 chain of LN‐332 inhibited tumor growth by up to 68%, and antibodies against the matrix binding domains of the β3 and γ2 chains significantly decreased lung metastases. The LN‐332 antibodies appear to induce tumor cell anoikis and subsequent programmed cell death and reduce migration by interfering with tumor cell matrix interactions. © 2009 UICC</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>19582877</pmid><doi>10.1002/ijc.24532</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0020-7136 |
| ispartof | International journal of cancer, 2009-10, Vol.125 (8), p.1814-1825 |
| issn | 0020-7136 1097-0215 1097-0215 |
| language | eng |
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| subjects | Adenocarcinoma - immunology Adenocarcinoma - pathology Animals Antibodies, Blocking - therapeutic use Antibodies, Monoclonal - therapeutic use Antineoplastic agents basement membranes Biological and medical sciences Carcinoma, Squamous Cell - immunology Carcinoma, Squamous Cell - pathology Cell Adhesion - drug effects Cell Adhesion Molecules - immunology Cell Movement Cell Proliferation Extracellular Matrix - metabolism Female Gene Expression Profiling Gene Expression Regulation, Neoplastic Humans Immunotherapy Kalinin laminin Lung Neoplasms - immunology Lung Neoplasms - pathology Male Medical sciences Medicin och hälsovetenskap metastasis Mice Mice, Inbred DBA Mice, Nude Multiple tumors. Solid tumors. Tumors in childhood (general aspects) Oligonucleotide Array Sequence Analysis Pharmacology. Drug treatments Tumor Cells, Cultured Tumors |
| title | Antibodies blocking adhesion and matrix binding domains of laminin‐332 inhibit tumor growth and metastasis in vivo |
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