In vivo Evidence That the Stromelysin-3 Metalloproteinase Contributes in a Paracrine Manner to Epithelial Cell Malignancy
Stromelysin-3 (ST3; Basset, P., J.P. Bellocq, C. Wolf, I. Stoll, P. Hutin, J.M. Limacher, O.L. Podhajcer, M.P. Chenard, M.C. Rio, P. Chambon. 1990. Nature. 348:699-704) is a matrix metalloproteinase (MMP) expressed in mesenchymal cells located close to epithelial cells, during physiological and path...
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| Veröffentlicht in: | The Journal of cell biology 1998-03, Vol.140 (6), p.1535-1541 |
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| creator | Masson, Régis Lefebvre, Olivier Noël, Agnès El Fahime, Mostapha Chenard, Marie-Pierre Wendling, Corinne Kebers, Florence LeMeur, Marianne Dierich, Andrée Foidart, Jean-Michel Basset, Paul Rio, Marie-Christine |
| description | Stromelysin-3 (ST3; Basset, P., J.P. Bellocq, C. Wolf, I. Stoll, P. Hutin, J.M. Limacher, O.L. Podhajcer, M.P. Chenard, M.C. Rio, P. Chambon. 1990. Nature. 348:699-704) is a matrix metalloproteinase (MMP) expressed in mesenchymal cells located close to epithelial cells, during physiological and pathological tissue remodeling processes. In human carcinomas, high ST3 levels are associated with a poor clinical outcome, suggesting that ST3 plays a role during malignant processes. In this study we report the ST3 gene inactivation by homologous recombination. Although ST3 null mice ( ST3-/-) were fertile and did not exhibit obvious alterations in appearance and behavior, the lack of ST3 altered malignant processes. Thus, the suppression of ST3 results in a decreased 7,12-dimethylbenzan-thracene-induced tumorigenesis in ST3-/- mice. Moreover, ST3-/- fibroblasts have lost the capacity to promote implantation of MCF7 human malignant epithelial cells in nude mice (P < 0.008). Finally, we show that this ST3 paracrine function requires extracellular matrix (ECM)-associated growth factors. Altogether, these findings give evidence that ST3 promotes, in a paracrine manner, homing of malignant epithelial cells, a key process for both primary tumors and metastases. Therefore, ST3 represents an appropriate target for specific MMP inhibitor(s) in future therapeutical approaches directed against the stromal compartment of human carcinomas. |
| doi_str_mv | 10.1083/jcb.140.6.1535 |
| format | Article |
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Bellocq, C. Wolf, I. Stoll, P. Hutin, J.M. Limacher, O.L. Podhajcer, M.P. Chenard, M.C. Rio, P. Chambon. 1990. Nature. 348:699-704) is a matrix metalloproteinase (MMP) expressed in mesenchymal cells located close to epithelial cells, during physiological and pathological tissue remodeling processes. In human carcinomas, high ST3 levels are associated with a poor clinical outcome, suggesting that ST3 plays a role during malignant processes. In this study we report the ST3 gene inactivation by homologous recombination. Although ST3 null mice ( ST3-/-) were fertile and did not exhibit obvious alterations in appearance and behavior, the lack of ST3 altered malignant processes. Thus, the suppression of ST3 results in a decreased 7,12-dimethylbenzan-thracene-induced tumorigenesis in ST3-/- mice. Moreover, ST3-/- fibroblasts have lost the capacity to promote implantation of MCF7 human malignant epithelial cells in nude mice (P < 0.008). Finally, we show that this ST3 paracrine function requires extracellular matrix (ECM)-associated growth factors. Altogether, these findings give evidence that ST3 promotes, in a paracrine manner, homing of malignant epithelial cells, a key process for both primary tumors and metastases. Therefore, ST3 represents an appropriate target for specific MMP inhibitor(s) in future therapeutical approaches directed against the stromal compartment of human carcinomas.</description><identifier>ISSN: 0021-9525</identifier><identifier>ISSN: 1540-8140</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.140.6.1535</identifier><identifier>PMID: 9508784</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>9,10-Dimethyl-1,2-benzanthracene ; Animals ; Biochemistry, biophysics & molecular biology ; Biochimie, biophysique & biologie moléculaire ; Breast Neoplasms ; Cancer ; Carcinogenicity Tests ; Carcinogens ; Carcinoma ; Cells ; Cellular Biology ; Cloning, Molecular ; DNA ; Epithelial cells ; Epithelial Cells - enzymology ; Extracellular Matrix - physiology ; Female ; Fibroblasts ; Fibroblasts - cytology ; Fibroblasts - enzymology ; Genes ; Human growth ; Humans ; Life Sciences ; Limb Buds - cytology ; Male ; Mammary glands ; Matrix Metalloproteinase 11 ; Metalloendopeptidases - genetics ; Metalloendopeptidases - metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Mutant Strains ; Mice, Nude ; Neoplasm Transplantation ; Paracrine Communication - physiology ; Phenotype ; Pregnancy ; Proteins ; Recombination, Genetic ; Sciences du vivant ; Tumor Cells, Cultured - cytology ; Tumor Cells, Cultured - enzymology ; Tumors</subject><ispartof>The Journal of cell biology, 1998-03, Vol.140 (6), p.1535-1541</ispartof><rights>Copyright 1998 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Mar 23, 1998</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>1998</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c541t-bce80abd2cafcdef651a310100d429273a6908706cb744d0704ccd76c49c889b3</citedby><cites>FETCH-LOGICAL-c541t-bce80abd2cafcdef651a310100d429273a6908706cb744d0704ccd76c49c889b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9508784$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-04033191$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Masson, Régis</creatorcontrib><creatorcontrib>Lefebvre, Olivier</creatorcontrib><creatorcontrib>Noël, Agnès</creatorcontrib><creatorcontrib>El Fahime, Mostapha</creatorcontrib><creatorcontrib>Chenard, Marie-Pierre</creatorcontrib><creatorcontrib>Wendling, Corinne</creatorcontrib><creatorcontrib>Kebers, Florence</creatorcontrib><creatorcontrib>LeMeur, Marianne</creatorcontrib><creatorcontrib>Dierich, Andrée</creatorcontrib><creatorcontrib>Foidart, Jean-Michel</creatorcontrib><creatorcontrib>Basset, Paul</creatorcontrib><creatorcontrib>Rio, Marie-Christine</creatorcontrib><title>In vivo Evidence That the Stromelysin-3 Metalloproteinase Contributes in a Paracrine Manner to Epithelial Cell Malignancy</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>Stromelysin-3 (ST3; Basset, P., J.P. Bellocq, C. Wolf, I. Stoll, P. Hutin, J.M. Limacher, O.L. Podhajcer, M.P. Chenard, M.C. Rio, P. Chambon. 1990. Nature. 348:699-704) is a matrix metalloproteinase (MMP) expressed in mesenchymal cells located close to epithelial cells, during physiological and pathological tissue remodeling processes. In human carcinomas, high ST3 levels are associated with a poor clinical outcome, suggesting that ST3 plays a role during malignant processes. In this study we report the ST3 gene inactivation by homologous recombination. Although ST3 null mice ( ST3-/-) were fertile and did not exhibit obvious alterations in appearance and behavior, the lack of ST3 altered malignant processes. Thus, the suppression of ST3 results in a decreased 7,12-dimethylbenzan-thracene-induced tumorigenesis in ST3-/- mice. Moreover, ST3-/- fibroblasts have lost the capacity to promote implantation of MCF7 human malignant epithelial cells in nude mice (P < 0.008). Finally, we show that this ST3 paracrine function requires extracellular matrix (ECM)-associated growth factors. Altogether, these findings give evidence that ST3 promotes, in a paracrine manner, homing of malignant epithelial cells, a key process for both primary tumors and metastases. Therefore, ST3 represents an appropriate target for specific MMP inhibitor(s) in future therapeutical approaches directed against the stromal compartment of human carcinomas.</description><subject>9,10-Dimethyl-1,2-benzanthracene</subject><subject>Animals</subject><subject>Biochemistry, biophysics & molecular biology</subject><subject>Biochimie, biophysique & biologie moléculaire</subject><subject>Breast Neoplasms</subject><subject>Cancer</subject><subject>Carcinogenicity Tests</subject><subject>Carcinogens</subject><subject>Carcinoma</subject><subject>Cells</subject><subject>Cellular Biology</subject><subject>Cloning, Molecular</subject><subject>DNA</subject><subject>Epithelial cells</subject><subject>Epithelial Cells - enzymology</subject><subject>Extracellular Matrix - physiology</subject><subject>Female</subject><subject>Fibroblasts</subject><subject>Fibroblasts - cytology</subject><subject>Fibroblasts - enzymology</subject><subject>Genes</subject><subject>Human growth</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Limb Buds - cytology</subject><subject>Male</subject><subject>Mammary glands</subject><subject>Matrix Metalloproteinase 11</subject><subject>Metalloendopeptidases - genetics</subject><subject>Metalloendopeptidases - metabolism</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Mutant Strains</subject><subject>Mice, Nude</subject><subject>Neoplasm Transplantation</subject><subject>Paracrine Communication - physiology</subject><subject>Phenotype</subject><subject>Pregnancy</subject><subject>Proteins</subject><subject>Recombination, Genetic</subject><subject>Sciences du vivant</subject><subject>Tumor Cells, Cultured - cytology</subject><subject>Tumor Cells, Cultured - enzymology</subject><subject>Tumors</subject><issn>0021-9525</issn><issn>1540-8140</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdUk1vEzEUtBCohMCVE0gWByQOG54_1rt7QaqiQiu1AolytrxeJ3Hk2MH2rpR_j9NEBXqy9WbevOfxIPSWwIJAyz5vdb8gHBZiQWpWP0MzUnOo2lJ6jmYAlFRdTeuX6FVKWwDgDWcX6KKroW1aPkOHG48nOwV8NdnBeG3w_UZlnDcG_8wx7Iw7JOsrhu9MVs6FfQzZWK-Swcvgc7T9mE3C1mOFf6iodLTe4DvlvYk4F9m9LVrOKoeXxrmCOLv2yuvDa_RipVwyb87nHP36enW_vK5uv3-7WV7eVrrmJFe9Ni2ofqBarfRgVqImihEgAAOnHW2YEl15CwjdN5wP0ADXemiE5p1u265nc_TlpLsf-50ZtClbKyf30e5UPMigrPwf8XYj12GSlDAqmq4I0JOAs2ZtZIi9lRN9aHy4j24tlZa9kZSKVtYNA1qaPp2aNk9mXV_eymMNODBGOjKRwv143jCG36NJWe5s0sUt5U0YkySCQyPKZ8_RhyfEbRijL-6VZYsFHSdHtcWJpGNIKZrV43gC8hgZWSIjSz6kkMfIlIb3_xr0SD9npODvTvg25RD_qgnS1lywPzczxpk</recordid><startdate>19980323</startdate><enddate>19980323</enddate><creator>Masson, Régis</creator><creator>Lefebvre, Olivier</creator><creator>Noël, Agnès</creator><creator>El Fahime, Mostapha</creator><creator>Chenard, Marie-Pierre</creator><creator>Wendling, Corinne</creator><creator>Kebers, Florence</creator><creator>LeMeur, Marianne</creator><creator>Dierich, Andrée</creator><creator>Foidart, Jean-Michel</creator><creator>Basset, Paul</creator><creator>Rio, Marie-Christine</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>1XC</scope><scope>Q33</scope><scope>5PM</scope></search><sort><creationdate>19980323</creationdate><title>In vivo Evidence That the Stromelysin-3 Metalloproteinase Contributes in a Paracrine Manner to Epithelial Cell Malignancy</title><author>Masson, Régis ; Lefebvre, Olivier ; Noël, Agnès ; El Fahime, Mostapha ; Chenard, Marie-Pierre ; Wendling, Corinne ; Kebers, Florence ; LeMeur, Marianne ; Dierich, Andrée ; Foidart, Jean-Michel ; Basset, Paul ; Rio, Marie-Christine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c541t-bce80abd2cafcdef651a310100d429273a6908706cb744d0704ccd76c49c889b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>9,10-Dimethyl-1,2-benzanthracene</topic><topic>Animals</topic><topic>Biochemistry, biophysics & molecular biology</topic><topic>Biochimie, biophysique & biologie moléculaire</topic><topic>Breast Neoplasms</topic><topic>Cancer</topic><topic>Carcinogenicity Tests</topic><topic>Carcinogens</topic><topic>Carcinoma</topic><topic>Cells</topic><topic>Cellular Biology</topic><topic>Cloning, Molecular</topic><topic>DNA</topic><topic>Epithelial cells</topic><topic>Epithelial Cells - enzymology</topic><topic>Extracellular Matrix - physiology</topic><topic>Female</topic><topic>Fibroblasts</topic><topic>Fibroblasts - cytology</topic><topic>Fibroblasts - enzymology</topic><topic>Genes</topic><topic>Human growth</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Limb Buds - cytology</topic><topic>Male</topic><topic>Mammary glands</topic><topic>Matrix Metalloproteinase 11</topic><topic>Metalloendopeptidases - genetics</topic><topic>Metalloendopeptidases - metabolism</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Mutant Strains</topic><topic>Mice, Nude</topic><topic>Neoplasm Transplantation</topic><topic>Paracrine Communication - physiology</topic><topic>Phenotype</topic><topic>Pregnancy</topic><topic>Proteins</topic><topic>Recombination, Genetic</topic><topic>Sciences du vivant</topic><topic>Tumor Cells, Cultured - cytology</topic><topic>Tumor Cells, Cultured - enzymology</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Masson, Régis</creatorcontrib><creatorcontrib>Lefebvre, Olivier</creatorcontrib><creatorcontrib>Noël, Agnès</creatorcontrib><creatorcontrib>El Fahime, Mostapha</creatorcontrib><creatorcontrib>Chenard, Marie-Pierre</creatorcontrib><creatorcontrib>Wendling, Corinne</creatorcontrib><creatorcontrib>Kebers, Florence</creatorcontrib><creatorcontrib>LeMeur, Marianne</creatorcontrib><creatorcontrib>Dierich, Andrée</creatorcontrib><creatorcontrib>Foidart, Jean-Michel</creatorcontrib><creatorcontrib>Basset, Paul</creatorcontrib><creatorcontrib>Rio, Marie-Christine</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Université de Liège - Open Repository and Bibliography (ORBI)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Masson, Régis</au><au>Lefebvre, Olivier</au><au>Noël, Agnès</au><au>El Fahime, Mostapha</au><au>Chenard, Marie-Pierre</au><au>Wendling, Corinne</au><au>Kebers, Florence</au><au>LeMeur, Marianne</au><au>Dierich, Andrée</au><au>Foidart, Jean-Michel</au><au>Basset, Paul</au><au>Rio, Marie-Christine</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>In vivo Evidence That the Stromelysin-3 Metalloproteinase Contributes in a Paracrine Manner to Epithelial Cell Malignancy</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1998-03-23</date><risdate>1998</risdate><volume>140</volume><issue>6</issue><spage>1535</spage><epage>1541</epage><pages>1535-1541</pages><issn>0021-9525</issn><issn>1540-8140</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>Stromelysin-3 (ST3; Basset, P., J.P. Bellocq, C. Wolf, I. Stoll, P. Hutin, J.M. Limacher, O.L. Podhajcer, M.P. Chenard, M.C. Rio, P. Chambon. 1990. Nature. 348:699-704) is a matrix metalloproteinase (MMP) expressed in mesenchymal cells located close to epithelial cells, during physiological and pathological tissue remodeling processes. In human carcinomas, high ST3 levels are associated with a poor clinical outcome, suggesting that ST3 plays a role during malignant processes. In this study we report the ST3 gene inactivation by homologous recombination. Although ST3 null mice ( ST3-/-) were fertile and did not exhibit obvious alterations in appearance and behavior, the lack of ST3 altered malignant processes. Thus, the suppression of ST3 results in a decreased 7,12-dimethylbenzan-thracene-induced tumorigenesis in ST3-/- mice. Moreover, ST3-/- fibroblasts have lost the capacity to promote implantation of MCF7 human malignant epithelial cells in nude mice (P < 0.008). Finally, we show that this ST3 paracrine function requires extracellular matrix (ECM)-associated growth factors. Altogether, these findings give evidence that ST3 promotes, in a paracrine manner, homing of malignant epithelial cells, a key process for both primary tumors and metastases. Therefore, ST3 represents an appropriate target for specific MMP inhibitor(s) in future therapeutical approaches directed against the stromal compartment of human carcinomas.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>9508784</pmid><doi>10.1083/jcb.140.6.1535</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of cell biology, 1998-03, Vol.140 (6), p.1535-1541 |
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| subjects | 9,10-Dimethyl-1,2-benzanthracene Animals Biochemistry, biophysics & molecular biology Biochimie, biophysique & biologie moléculaire Breast Neoplasms Cancer Carcinogenicity Tests Carcinogens Carcinoma Cells Cellular Biology Cloning, Molecular DNA Epithelial cells Epithelial Cells - enzymology Extracellular Matrix - physiology Female Fibroblasts Fibroblasts - cytology Fibroblasts - enzymology Genes Human growth Humans Life Sciences Limb Buds - cytology Male Mammary glands Matrix Metalloproteinase 11 Metalloendopeptidases - genetics Metalloendopeptidases - metabolism Mice Mice, Inbred C57BL Mice, Mutant Strains Mice, Nude Neoplasm Transplantation Paracrine Communication - physiology Phenotype Pregnancy Proteins Recombination, Genetic Sciences du vivant Tumor Cells, Cultured - cytology Tumor Cells, Cultured - enzymology Tumors |
| title | In vivo Evidence That the Stromelysin-3 Metalloproteinase Contributes in a Paracrine Manner to Epithelial Cell Malignancy |
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