Stimulation of MMP-7 (matrilysin) by Helicobacter pylori in human gastric epithelial cells: role in epithelial cell migration
Epithelial cell responses to bacterial infection include induction of matrix metalloproteinase 7 (MMP-7). Here, we identify increased MMP-7 expression in the gastric epithelium in response to the oncogenic bacterium Helicobacter pylori, and report on the mechanisms and consequences for gastric epith...
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| Veröffentlicht in: | Journal of cell science 2003-07, Vol.116 (Pt 14), p.3017-3026 |
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| container_title | Journal of cell science |
| container_volume | 116 |
| creator | Wroblewski, Lydia E Noble, P-J M Pagliocca, Adelina Pritchard, D Mark Hart, C Anthony Campbell, Fiona Dodson, Andrew R Dockray, Graham J Varro, Andrea |
| description | Epithelial cell responses to bacterial infection include induction of matrix metalloproteinase 7 (MMP-7). Here, we identify increased MMP-7 expression in the gastric epithelium in response to the oncogenic bacterium Helicobacter pylori, and report on the mechanisms and consequences for gastric epithelial cell migration. In patients infected with H. pylori, there was increased MMP-7 in gastric biopsies detected by western blot. MMP-7 was localized to the advancing edge of migrating gastric epithelial cell colonies, including lamellipodia. Rates of spreading of gastric gland cells were higher in H. pylori-infected cultures compared with control, and this was inhibited by antisense oligonucleotides to MMP-7. Complementary data were obtained in a gastric cancer cell line (AGS cells). In the latter, H. pylori induced expression of an MMP-7-luciferase promoter/reporter vector through mechanisms that involved activation of Rho and Rac. RhoA acted through activation of both NF-kappaB and AP-1, whereas Rac activated NF-kappaB but not AP-1. MMP-7 is commonly upregulated in gastric cancer; since H. pylori is a recognized gastric carcinogen, the data suggest a new mechanism by which the bacterium might predispose towards gastric neoplasia. |
| doi_str_mv | 10.1242/jcs.00518 |
| format | Article |
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Here, we identify increased MMP-7 expression in the gastric epithelium in response to the oncogenic bacterium Helicobacter pylori, and report on the mechanisms and consequences for gastric epithelial cell migration. In patients infected with H. pylori, there was increased MMP-7 in gastric biopsies detected by western blot. MMP-7 was localized to the advancing edge of migrating gastric epithelial cell colonies, including lamellipodia. Rates of spreading of gastric gland cells were higher in H. pylori-infected cultures compared with control, and this was inhibited by antisense oligonucleotides to MMP-7. Complementary data were obtained in a gastric cancer cell line (AGS cells). In the latter, H. pylori induced expression of an MMP-7-luciferase promoter/reporter vector through mechanisms that involved activation of Rho and Rac. RhoA acted through activation of both NF-kappaB and AP-1, whereas Rac activated NF-kappaB but not AP-1. MMP-7 is commonly upregulated in gastric cancer; since H. pylori is a recognized gastric carcinogen, the data suggest a new mechanism by which the bacterium might predispose towards gastric neoplasia.</description><identifier>ISSN: 0021-9533</identifier><identifier>EISSN: 1477-9137</identifier><identifier>DOI: 10.1242/jcs.00518</identifier><identifier>PMID: 12808021</identifier><language>eng</language><publisher>England</publisher><subject>Blotting, Western ; Cell Line, Tumor ; Cell Movement ; Cells, Cultured ; Epithelial Cells - cytology ; Epithelial Cells - enzymology ; Genes, Reporter ; Genetic Vectors ; Helicobacter pylori ; Helicobacter pylori - metabolism ; Humans ; Immunohistochemistry ; Luciferases - metabolism ; Matrix Metalloproteinase 7 - metabolism ; Matrix Metalloproteinase 7 - physiology ; Neoplasm Invasiveness ; NF-kappa B - metabolism ; Oligonucleotides, Antisense - chemistry ; Plasmids - metabolism ; Promoter Regions, Genetic ; rac GTP-Binding Proteins - metabolism ; Rac protein ; Radioimmunoassay ; rhoA GTP-Binding Protein - physiology ; RhoA protein ; Signal Transduction ; Stomach - metabolism ; Time Factors ; Transcription Factor AP-1 - metabolism ; Transcription Factors - metabolism ; Transfection ; Up-Regulation</subject><ispartof>Journal of cell science, 2003-07, Vol.116 (Pt 14), p.3017-3026</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c349t-59574472ad937a6acff97289e287403bf4ceb169384c8e842d8598cef00261833</citedby><cites>FETCH-LOGICAL-c349t-59574472ad937a6acff97289e287403bf4ceb169384c8e842d8598cef00261833</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,3665,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12808021$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wroblewski, Lydia E</creatorcontrib><creatorcontrib>Noble, P-J M</creatorcontrib><creatorcontrib>Pagliocca, Adelina</creatorcontrib><creatorcontrib>Pritchard, D Mark</creatorcontrib><creatorcontrib>Hart, C Anthony</creatorcontrib><creatorcontrib>Campbell, Fiona</creatorcontrib><creatorcontrib>Dodson, Andrew R</creatorcontrib><creatorcontrib>Dockray, Graham J</creatorcontrib><creatorcontrib>Varro, Andrea</creatorcontrib><title>Stimulation of MMP-7 (matrilysin) by Helicobacter pylori in human gastric epithelial cells: role in epithelial cell migration</title><title>Journal of cell science</title><addtitle>J Cell Sci</addtitle><description>Epithelial cell responses to bacterial infection include induction of matrix metalloproteinase 7 (MMP-7). Here, we identify increased MMP-7 expression in the gastric epithelium in response to the oncogenic bacterium Helicobacter pylori, and report on the mechanisms and consequences for gastric epithelial cell migration. In patients infected with H. pylori, there was increased MMP-7 in gastric biopsies detected by western blot. MMP-7 was localized to the advancing edge of migrating gastric epithelial cell colonies, including lamellipodia. Rates of spreading of gastric gland cells were higher in H. pylori-infected cultures compared with control, and this was inhibited by antisense oligonucleotides to MMP-7. Complementary data were obtained in a gastric cancer cell line (AGS cells). In the latter, H. pylori induced expression of an MMP-7-luciferase promoter/reporter vector through mechanisms that involved activation of Rho and Rac. RhoA acted through activation of both NF-kappaB and AP-1, whereas Rac activated NF-kappaB but not AP-1. MMP-7 is commonly upregulated in gastric cancer; since H. pylori is a recognized gastric carcinogen, the data suggest a new mechanism by which the bacterium might predispose towards gastric neoplasia.</description><subject>Blotting, Western</subject><subject>Cell Line, Tumor</subject><subject>Cell Movement</subject><subject>Cells, Cultured</subject><subject>Epithelial Cells - cytology</subject><subject>Epithelial Cells - enzymology</subject><subject>Genes, Reporter</subject><subject>Genetic Vectors</subject><subject>Helicobacter pylori</subject><subject>Helicobacter pylori - metabolism</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Luciferases - metabolism</subject><subject>Matrix Metalloproteinase 7 - metabolism</subject><subject>Matrix Metalloproteinase 7 - physiology</subject><subject>Neoplasm Invasiveness</subject><subject>NF-kappa B - metabolism</subject><subject>Oligonucleotides, Antisense - chemistry</subject><subject>Plasmids - metabolism</subject><subject>Promoter Regions, Genetic</subject><subject>rac GTP-Binding Proteins - metabolism</subject><subject>Rac protein</subject><subject>Radioimmunoassay</subject><subject>rhoA GTP-Binding Protein - physiology</subject><subject>RhoA protein</subject><subject>Signal Transduction</subject><subject>Stomach - metabolism</subject><subject>Time Factors</subject><subject>Transcription Factor AP-1 - metabolism</subject><subject>Transcription Factors - metabolism</subject><subject>Transfection</subject><subject>Up-Regulation</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkL1OwzAYRS0EoqUw8ALIE6JDiv9S22yoAorUCiRgjhzXaV05cbCTIQPvTvojITF9wz2699MB4BqjCSaM3G91nCCUYnEChphxnkhM-SkYIkRwIlNKB-Aixi1CiBPJz8EAE4FEHw7Bz0djy9apxvoK-gIul-8Jh3elaoJ1XbTVGOYdnBtntc-VbkyAded8sNBWcNOWqoJrFXtYQ1PbZtODykFtnIsPMHhndty_BJZ2HfaLl-CsUC6aq-Mdga_np8_ZPFm8vbzOHheJpkw2SSpTzhgnaiUpV1Oli0JyIqQhgjNE84Jpk-OppIJpYQQjK5FKoU3RC5hiQekI3B566-C_WxObrLRx94qqjG9jhiXmKcGsB8cHUAcfYzBFVgdbqtBlGGU711nvOtu77tmbY2mbl2b1Rx7l0l-UtXpU</recordid><startdate>20030715</startdate><enddate>20030715</enddate><creator>Wroblewski, Lydia E</creator><creator>Noble, P-J M</creator><creator>Pagliocca, Adelina</creator><creator>Pritchard, D Mark</creator><creator>Hart, C Anthony</creator><creator>Campbell, Fiona</creator><creator>Dodson, Andrew R</creator><creator>Dockray, Graham J</creator><creator>Varro, Andrea</creator><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>C1K</scope></search><sort><creationdate>20030715</creationdate><title>Stimulation of MMP-7 (matrilysin) by Helicobacter pylori in human gastric epithelial cells: role in epithelial cell migration</title><author>Wroblewski, Lydia E ; Noble, P-J M ; Pagliocca, Adelina ; Pritchard, D Mark ; Hart, C Anthony ; Campbell, Fiona ; Dodson, Andrew R ; Dockray, Graham J ; Varro, Andrea</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c349t-59574472ad937a6acff97289e287403bf4ceb169384c8e842d8598cef00261833</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Blotting, Western</topic><topic>Cell Line, Tumor</topic><topic>Cell Movement</topic><topic>Cells, Cultured</topic><topic>Epithelial Cells - cytology</topic><topic>Epithelial Cells - enzymology</topic><topic>Genes, Reporter</topic><topic>Genetic Vectors</topic><topic>Helicobacter pylori</topic><topic>Helicobacter pylori - metabolism</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Luciferases - metabolism</topic><topic>Matrix Metalloproteinase 7 - metabolism</topic><topic>Matrix Metalloproteinase 7 - physiology</topic><topic>Neoplasm Invasiveness</topic><topic>NF-kappa B - metabolism</topic><topic>Oligonucleotides, Antisense - chemistry</topic><topic>Plasmids - metabolism</topic><topic>Promoter Regions, Genetic</topic><topic>rac GTP-Binding Proteins - metabolism</topic><topic>Rac protein</topic><topic>Radioimmunoassay</topic><topic>rhoA GTP-Binding Protein - physiology</topic><topic>RhoA protein</topic><topic>Signal Transduction</topic><topic>Stomach - metabolism</topic><topic>Time Factors</topic><topic>Transcription Factor AP-1 - metabolism</topic><topic>Transcription Factors - metabolism</topic><topic>Transfection</topic><topic>Up-Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wroblewski, Lydia E</creatorcontrib><creatorcontrib>Noble, P-J M</creatorcontrib><creatorcontrib>Pagliocca, Adelina</creatorcontrib><creatorcontrib>Pritchard, D Mark</creatorcontrib><creatorcontrib>Hart, C Anthony</creatorcontrib><creatorcontrib>Campbell, Fiona</creatorcontrib><creatorcontrib>Dodson, Andrew R</creatorcontrib><creatorcontrib>Dockray, Graham J</creatorcontrib><creatorcontrib>Varro, Andrea</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>Environmental Sciences and Pollution Management</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wroblewski, Lydia E</au><au>Noble, P-J M</au><au>Pagliocca, Adelina</au><au>Pritchard, D Mark</au><au>Hart, C Anthony</au><au>Campbell, Fiona</au><au>Dodson, Andrew R</au><au>Dockray, Graham J</au><au>Varro, Andrea</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Stimulation of MMP-7 (matrilysin) by Helicobacter pylori in human gastric epithelial cells: role in epithelial cell migration</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2003-07-15</date><risdate>2003</risdate><volume>116</volume><issue>Pt 14</issue><spage>3017</spage><epage>3026</epage><pages>3017-3026</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>Epithelial cell responses to bacterial infection include induction of matrix metalloproteinase 7 (MMP-7). Here, we identify increased MMP-7 expression in the gastric epithelium in response to the oncogenic bacterium Helicobacter pylori, and report on the mechanisms and consequences for gastric epithelial cell migration. In patients infected with H. pylori, there was increased MMP-7 in gastric biopsies detected by western blot. MMP-7 was localized to the advancing edge of migrating gastric epithelial cell colonies, including lamellipodia. Rates of spreading of gastric gland cells were higher in H. pylori-infected cultures compared with control, and this was inhibited by antisense oligonucleotides to MMP-7. Complementary data were obtained in a gastric cancer cell line (AGS cells). In the latter, H. pylori induced expression of an MMP-7-luciferase promoter/reporter vector through mechanisms that involved activation of Rho and Rac. RhoA acted through activation of both NF-kappaB and AP-1, whereas Rac activated NF-kappaB but not AP-1. MMP-7 is commonly upregulated in gastric cancer; since H. pylori is a recognized gastric carcinogen, the data suggest a new mechanism by which the bacterium might predispose towards gastric neoplasia.</abstract><cop>England</cop><pmid>12808021</pmid><doi>10.1242/jcs.00518</doi><tpages>10</tpages></addata></record> |
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| ispartof | Journal of cell science, 2003-07, Vol.116 (Pt 14), p.3017-3026 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Company of Biologists |
| subjects | Blotting, Western Cell Line, Tumor Cell Movement Cells, Cultured Epithelial Cells - cytology Epithelial Cells - enzymology Genes, Reporter Genetic Vectors Helicobacter pylori Helicobacter pylori - metabolism Humans Immunohistochemistry Luciferases - metabolism Matrix Metalloproteinase 7 - metabolism Matrix Metalloproteinase 7 - physiology Neoplasm Invasiveness NF-kappa B - metabolism Oligonucleotides, Antisense - chemistry Plasmids - metabolism Promoter Regions, Genetic rac GTP-Binding Proteins - metabolism Rac protein Radioimmunoassay rhoA GTP-Binding Protein - physiology RhoA protein Signal Transduction Stomach - metabolism Time Factors Transcription Factor AP-1 - metabolism Transcription Factors - metabolism Transfection Up-Regulation |
| title | Stimulation of MMP-7 (matrilysin) by Helicobacter pylori in human gastric epithelial cells: role in epithelial cell migration |
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