Helicobacter pylori upregulates matrilysin (MMP-7) in epithelial cells in vivo and in vitro in a Cag dependent manner
Background and aims: Matrix metalloproteinase-7 (MMP-7) is important in normal and pathological remodelling of epithelial-matrix interactions, and is upregulated in gastric cancer. Helicobacter pylori infection is the first stage in gastric carcinogenesis, and therefore our aim was to determine if H...
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| Veröffentlicht in: | Gut 2003-10, Vol.52 (10), p.1408-1413 |
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| description | Background and aims: Matrix metalloproteinase-7 (MMP-7) is important in normal and pathological remodelling of epithelial-matrix interactions, and is upregulated in gastric cancer. Helicobacter pylori infection is the first stage in gastric carcinogenesis, and therefore our aim was to determine if H pylori upregulated gastric MMP-7 expression and if this was affected by strain virulence. Methods: We took gastric biopsy specimens at endoscopy from H pylori infected (n = 17) and uninfected (n = 18) patients and assessed MMP-7 expression by ELISA, real time polymerase chain reaction (PCR), and immunohistochemistry (concentrating on epithelial cells in the proliferative zone). We PCR typed H pylori for cagE and vacA. We performed H pylori/cell line coculture studies with wild-type pathogenic and non-pathogenic H pylori strains and with CagE− and VacA− isogenic mutants. Results: Gastric biopsy specimens from H pylori+ patients expressed higher levels of MMP-7 at the protein and mRNA levels in the antrum and corpus (for example, by ELISA: H pylori+ 0.182 OD units vH pylori− 0.059; p = 0.009 antrum). Epithelial cells from H pylori+ patients stained more intensely for MMP-7 than those from uninfected patients, including in the proliferative zone containing pluripotent cells (p |
| doi_str_mv | 10.1136/gut.52.10.1408 |
| format | Article |
| fullrecord | <record><control><sourceid>gale_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1773843</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A108720905</galeid><sourcerecordid>A108720905</sourcerecordid><originalsourceid>FETCH-LOGICAL-b622t-74b2611b2ea67a491b5531f9a598817796a79990e6f1cde49a12e5368c1d47c43</originalsourceid><addsrcrecordid>eNqFkk2P0zAQhiMEYsvClSOKhJDYQ4rtxLF9QVrKx4K6gMTX0XKcSdZd1w52UtF_j0urLUgI5IPHnmdezauZLHuI0Rzjsn7WT-OckvnuWSF-K5vhquZFSTi_nc0QwqygrBIn2b0YVwghzgW-m51gIhjCJZ5l0wVYo32j9AghH7bWB5NPQ4B-smqEmK_VGIzdRuPyp5eXHwt2lqcQBjNepUplcw3Wxt3fxmx8rly7j8fgd4HKF6rPWxjAteDGJOcchPvZnU7ZCA8O92n25fWrz4uLYvnhzdvF-bJoakLGglUNqTFuCKiaqUrghtISd0JRwTlmTNSKCSEQ1B3WLVRCYQK0rLnGbcV0VZ5mz_e6w9SsodWpg6CsHIJZq7CVXhn5Z8aZK9n7jUziJa_KJPD4IBD89wniKFd-Ci71vENESZAgdaKKPdUrC9K4zicx3UNyqqx30Jn0fY4RZ4lHNPHzv_DptLBOw_hHgQ4-xgDdjQWM5G4PZNoDScmvZ9qDVPDod-NH_DD4BDw5ACpqZbugnDbxyFGMebJ3tGbiCD9u8ipcy5qVjMr3Xxfy27uXL-gnROUy8Wd7vlmv_tfkT7TM1tw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1779320926</pqid></control><display><type>article</type><title>Helicobacter pylori upregulates matrilysin (MMP-7) in epithelial cells in vivo and in vitro in a Cag dependent manner</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Bebb, J R ; Letley, D P ; Thomas, R J ; Aviles, F ; Collins, H M ; Watson, S A ; Hand, N M ; Zaitoun, A ; Atherton, J C</creator><creatorcontrib>Bebb, J R ; Letley, D P ; Thomas, R J ; Aviles, F ; Collins, H M ; Watson, S A ; Hand, N M ; Zaitoun, A ; Atherton, J C</creatorcontrib><description>Background and aims: Matrix metalloproteinase-7 (MMP-7) is important in normal and pathological remodelling of epithelial-matrix interactions, and is upregulated in gastric cancer. Helicobacter pylori infection is the first stage in gastric carcinogenesis, and therefore our aim was to determine if H pylori upregulated gastric MMP-7 expression and if this was affected by strain virulence. Methods: We took gastric biopsy specimens at endoscopy from H pylori infected (n = 17) and uninfected (n = 18) patients and assessed MMP-7 expression by ELISA, real time polymerase chain reaction (PCR), and immunohistochemistry (concentrating on epithelial cells in the proliferative zone). We PCR typed H pylori for cagE and vacA. We performed H pylori/cell line coculture studies with wild-type pathogenic and non-pathogenic H pylori strains and with CagE− and VacA− isogenic mutants. Results: Gastric biopsy specimens from H pylori+ patients expressed higher levels of MMP-7 at the protein and mRNA levels in the antrum and corpus (for example, by ELISA: H pylori+ 0.182 OD units vH pylori− 0.059; p = 0.009 antrum). Epithelial cells from H pylori+ patients stained more intensely for MMP-7 than those from uninfected patients, including in the proliferative zone containing pluripotent cells (p<0.03 antrum, p<0.04 body). Upregulation of MMP-7 in epithelial cells was confirmed at the protein and mRNA levels by H pylori/cell line coculture. These experiments also showed that MMP-7 upregulation was dependent on an intact H pyloricag pathogenicity island but not on the vacuolating cytotoxin. Conclusion: We speculate that increased expression of MMP-7 in H pylori gastritis may contribute to gastric carcinogenesis.</description><identifier>ISSN: 0017-5749</identifier><identifier>EISSN: 1468-3288</identifier><identifier>EISSN: 1458-3288</identifier><identifier>DOI: 10.1136/gut.52.10.1408</identifier><identifier>PMID: 12970131</identifier><identifier>CODEN: GUTTAK</identifier><language>eng</language><publisher>London: BMJ Publishing Group Ltd and British Society of Gastroenterology</publisher><subject>Aged ; Apoptosis ; Bacterial Proteins - analysis ; Biological and medical sciences ; Biopsy ; cag pathogenicity island ; Causes of ; Cells, Cultured ; Cytokines ; ELISA ; Enzyme Activation ; enzyme linked immunosorbent assay ; Enzyme-Linked Immunosorbent Assay - methods ; Enzymes ; Epithelial Cells - enzymology ; FCS ; Female ; fetal calf serum ; GAPDH ; Gastric cancer ; Gastric Mucosa - enzymology ; Gastroenterology. Liver. Pancreas. Abdomen ; Gene expression ; Genetic aspects ; glyceraldehyde-3-phosphate dehydrogenase ; Helicobacter infections ; Helicobacter Infections - enzymology ; Helicobacter pylori ; Helicobacter pylori - metabolism ; Humans ; Immunohistochemistry ; Influence ; Kinases ; Ligands ; Male ; Matrix Metalloproteinase 7 - metabolism ; matrix metalloproteinase-7 ; matrix metalloproteinase-7 (matrilysin) ; matrix metalloproteinases ; Medical research ; Medical sciences ; Metalloproteins ; Middle Aged ; MMP-7 ; MMPs ; Nuclear Proteins - analysis ; Patients ; PCR ; Physiological aspects ; polymerase chain reaction ; Regulation ; Reverse Transcriptase Polymerase Chain Reaction ; Scholarships & fellowships ; SDS-PAGE ; sodium dodecyl sulphate-polyacrylamide gel electrophoresis ; Stomach ; Stomach cancer ; Stomach. Duodenum. Small intestine. Colon. Rectum. Anus ; threshold cycle ; TNF-α ; Tumor necrosis factor-TNF ; Tumors ; tumour necrosis factor α ; Ulcers ; Up-Regulation</subject><ispartof>Gut, 2003-10, Vol.52 (10), p.1408-1413</ispartof><rights>Copyright 2003 by Gut</rights><rights>2004 INIST-CNRS</rights><rights>COPYRIGHT 2003 BMJ Publishing Group Ltd.</rights><rights>Copyright: 2003 Copyright 2003 by Gut</rights><rights>Copyright © Copyright 2003 by Gut 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b622t-74b2611b2ea67a491b5531f9a598817796a79990e6f1cde49a12e5368c1d47c43</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1773843/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1773843/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15118932$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12970131$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bebb, J R</creatorcontrib><creatorcontrib>Letley, D P</creatorcontrib><creatorcontrib>Thomas, R J</creatorcontrib><creatorcontrib>Aviles, F</creatorcontrib><creatorcontrib>Collins, H M</creatorcontrib><creatorcontrib>Watson, S A</creatorcontrib><creatorcontrib>Hand, N M</creatorcontrib><creatorcontrib>Zaitoun, A</creatorcontrib><creatorcontrib>Atherton, J C</creatorcontrib><title>Helicobacter pylori upregulates matrilysin (MMP-7) in epithelial cells in vivo and in vitro in a Cag dependent manner</title><title>Gut</title><addtitle>Gut</addtitle><description>Background and aims: Matrix metalloproteinase-7 (MMP-7) is important in normal and pathological remodelling of epithelial-matrix interactions, and is upregulated in gastric cancer. Helicobacter pylori infection is the first stage in gastric carcinogenesis, and therefore our aim was to determine if H pylori upregulated gastric MMP-7 expression and if this was affected by strain virulence. Methods: We took gastric biopsy specimens at endoscopy from H pylori infected (n = 17) and uninfected (n = 18) patients and assessed MMP-7 expression by ELISA, real time polymerase chain reaction (PCR), and immunohistochemistry (concentrating on epithelial cells in the proliferative zone). We PCR typed H pylori for cagE and vacA. We performed H pylori/cell line coculture studies with wild-type pathogenic and non-pathogenic H pylori strains and with CagE− and VacA− isogenic mutants. Results: Gastric biopsy specimens from H pylori+ patients expressed higher levels of MMP-7 at the protein and mRNA levels in the antrum and corpus (for example, by ELISA: H pylori+ 0.182 OD units vH pylori− 0.059; p = 0.009 antrum). Epithelial cells from H pylori+ patients stained more intensely for MMP-7 than those from uninfected patients, including in the proliferative zone containing pluripotent cells (p<0.03 antrum, p<0.04 body). Upregulation of MMP-7 in epithelial cells was confirmed at the protein and mRNA levels by H pylori/cell line coculture. These experiments also showed that MMP-7 upregulation was dependent on an intact H pyloricag pathogenicity island but not on the vacuolating cytotoxin. Conclusion: We speculate that increased expression of MMP-7 in H pylori gastritis may contribute to gastric carcinogenesis.</description><subject>Aged</subject><subject>Apoptosis</subject><subject>Bacterial Proteins - analysis</subject><subject>Biological and medical sciences</subject><subject>Biopsy</subject><subject>cag pathogenicity island</subject><subject>Causes of</subject><subject>Cells, Cultured</subject><subject>Cytokines</subject><subject>ELISA</subject><subject>Enzyme Activation</subject><subject>enzyme linked immunosorbent assay</subject><subject>Enzyme-Linked Immunosorbent Assay - methods</subject><subject>Enzymes</subject><subject>Epithelial Cells - enzymology</subject><subject>FCS</subject><subject>Female</subject><subject>fetal calf serum</subject><subject>GAPDH</subject><subject>Gastric cancer</subject><subject>Gastric Mucosa - enzymology</subject><subject>Gastroenterology. Liver. Pancreas. Abdomen</subject><subject>Gene expression</subject><subject>Genetic aspects</subject><subject>glyceraldehyde-3-phosphate dehydrogenase</subject><subject>Helicobacter infections</subject><subject>Helicobacter Infections - enzymology</subject><subject>Helicobacter pylori</subject><subject>Helicobacter pylori - metabolism</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Influence</subject><subject>Kinases</subject><subject>Ligands</subject><subject>Male</subject><subject>Matrix Metalloproteinase 7 - metabolism</subject><subject>matrix metalloproteinase-7</subject><subject>matrix metalloproteinase-7 (matrilysin)</subject><subject>matrix metalloproteinases</subject><subject>Medical research</subject><subject>Medical sciences</subject><subject>Metalloproteins</subject><subject>Middle Aged</subject><subject>MMP-7</subject><subject>MMPs</subject><subject>Nuclear Proteins - analysis</subject><subject>Patients</subject><subject>PCR</subject><subject>Physiological aspects</subject><subject>polymerase chain reaction</subject><subject>Regulation</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Scholarships & fellowships</subject><subject>SDS-PAGE</subject><subject>sodium dodecyl sulphate-polyacrylamide gel electrophoresis</subject><subject>Stomach</subject><subject>Stomach cancer</subject><subject>Stomach. Duodenum. Small intestine. Colon. Rectum. Anus</subject><subject>threshold cycle</subject><subject>TNF-α</subject><subject>Tumor necrosis factor-TNF</subject><subject>Tumors</subject><subject>tumour necrosis factor α</subject><subject>Ulcers</subject><subject>Up-Regulation</subject><issn>0017-5749</issn><issn>1468-3288</issn><issn>1458-3288</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkk2P0zAQhiMEYsvClSOKhJDYQ4rtxLF9QVrKx4K6gMTX0XKcSdZd1w52UtF_j0urLUgI5IPHnmdezauZLHuI0Rzjsn7WT-OckvnuWSF-K5vhquZFSTi_nc0QwqygrBIn2b0YVwghzgW-m51gIhjCJZ5l0wVYo32j9AghH7bWB5NPQ4B-smqEmK_VGIzdRuPyp5eXHwt2lqcQBjNepUplcw3Wxt3fxmx8rly7j8fgd4HKF6rPWxjAteDGJOcchPvZnU7ZCA8O92n25fWrz4uLYvnhzdvF-bJoakLGglUNqTFuCKiaqUrghtISd0JRwTlmTNSKCSEQ1B3WLVRCYQK0rLnGbcV0VZ5mz_e6w9SsodWpg6CsHIJZq7CVXhn5Z8aZK9n7jUziJa_KJPD4IBD89wniKFd-Ci71vENESZAgdaKKPdUrC9K4zicx3UNyqqx30Jn0fY4RZ4lHNPHzv_DptLBOw_hHgQ4-xgDdjQWM5G4PZNoDScmvZ9qDVPDod-NH_DD4BDw5ACpqZbugnDbxyFGMebJ3tGbiCD9u8ipcy5qVjMr3Xxfy27uXL-gnROUy8Wd7vlmv_tfkT7TM1tw</recordid><startdate>20031001</startdate><enddate>20031001</enddate><creator>Bebb, J R</creator><creator>Letley, D P</creator><creator>Thomas, R J</creator><creator>Aviles, F</creator><creator>Collins, H M</creator><creator>Watson, S A</creator><creator>Hand, N M</creator><creator>Zaitoun, A</creator><creator>Atherton, J C</creator><general>BMJ Publishing Group Ltd and British Society of Gastroenterology</general><general>BMJ</general><general>BMJ Publishing Group Ltd</general><general>BMJ Publishing Group LTD</general><general>Copyright 2003 by Gut</general><scope>BSCLL</scope><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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BTHHO</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>5PM</scope></search><sort><creationdate>20031001</creationdate><title>Helicobacter pylori upregulates matrilysin (MMP-7) in epithelial cells in vivo and in vitro in a Cag dependent manner</title><author>Bebb, J R ; Letley, D P ; Thomas, R J ; Aviles, F ; Collins, H M ; Watson, S A ; Hand, N M ; Zaitoun, A ; Atherton, J C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b622t-74b2611b2ea67a491b5531f9a598817796a79990e6f1cde49a12e5368c1d47c43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Aged</topic><topic>Apoptosis</topic><topic>Bacterial Proteins - analysis</topic><topic>Biological and medical sciences</topic><topic>Biopsy</topic><topic>cag pathogenicity island</topic><topic>Causes of</topic><topic>Cells, Cultured</topic><topic>Cytokines</topic><topic>ELISA</topic><topic>Enzyme Activation</topic><topic>enzyme linked immunosorbent assay</topic><topic>Enzyme-Linked Immunosorbent Assay - methods</topic><topic>Enzymes</topic><topic>Epithelial Cells - enzymology</topic><topic>FCS</topic><topic>Female</topic><topic>fetal calf serum</topic><topic>GAPDH</topic><topic>Gastric cancer</topic><topic>Gastric Mucosa - enzymology</topic><topic>Gastroenterology. Liver. Pancreas. Abdomen</topic><topic>Gene expression</topic><topic>Genetic aspects</topic><topic>glyceraldehyde-3-phosphate dehydrogenase</topic><topic>Helicobacter infections</topic><topic>Helicobacter Infections - enzymology</topic><topic>Helicobacter pylori</topic><topic>Helicobacter pylori - metabolism</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Influence</topic><topic>Kinases</topic><topic>Ligands</topic><topic>Male</topic><topic>Matrix Metalloproteinase 7 - metabolism</topic><topic>matrix metalloproteinase-7</topic><topic>matrix metalloproteinase-7 (matrilysin)</topic><topic>matrix metalloproteinases</topic><topic>Medical research</topic><topic>Medical sciences</topic><topic>Metalloproteins</topic><topic>Middle Aged</topic><topic>MMP-7</topic><topic>MMPs</topic><topic>Nuclear Proteins - analysis</topic><topic>Patients</topic><topic>PCR</topic><topic>Physiological aspects</topic><topic>polymerase chain reaction</topic><topic>Regulation</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Scholarships & fellowships</topic><topic>SDS-PAGE</topic><topic>sodium dodecyl sulphate-polyacrylamide gel electrophoresis</topic><topic>Stomach</topic><topic>Stomach cancer</topic><topic>Stomach. Duodenum. Small intestine. Colon. Rectum. Anus</topic><topic>threshold cycle</topic><topic>TNF-α</topic><topic>Tumor necrosis factor-TNF</topic><topic>Tumors</topic><topic>tumour necrosis factor α</topic><topic>Ulcers</topic><topic>Up-Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bebb, J R</creatorcontrib><creatorcontrib>Letley, D P</creatorcontrib><creatorcontrib>Thomas, R J</creatorcontrib><creatorcontrib>Aviles, F</creatorcontrib><creatorcontrib>Collins, H M</creatorcontrib><creatorcontrib>Watson, S A</creatorcontrib><creatorcontrib>Hand, N M</creatorcontrib><creatorcontrib>Zaitoun, A</creatorcontrib><creatorcontrib>Atherton, J C</creatorcontrib><collection>Istex</collection><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>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</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>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>BMJ Journals</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Gut</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bebb, J R</au><au>Letley, D P</au><au>Thomas, R J</au><au>Aviles, F</au><au>Collins, H M</au><au>Watson, S A</au><au>Hand, N M</au><au>Zaitoun, A</au><au>Atherton, J C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Helicobacter pylori upregulates matrilysin (MMP-7) in epithelial cells in vivo and in vitro in a Cag dependent manner</atitle><jtitle>Gut</jtitle><addtitle>Gut</addtitle><date>2003-10-01</date><risdate>2003</risdate><volume>52</volume><issue>10</issue><spage>1408</spage><epage>1413</epage><pages>1408-1413</pages><issn>0017-5749</issn><eissn>1468-3288</eissn><eissn>1458-3288</eissn><coden>GUTTAK</coden><abstract>Background and aims: Matrix metalloproteinase-7 (MMP-7) is important in normal and pathological remodelling of epithelial-matrix interactions, and is upregulated in gastric cancer. Helicobacter pylori infection is the first stage in gastric carcinogenesis, and therefore our aim was to determine if H pylori upregulated gastric MMP-7 expression and if this was affected by strain virulence. Methods: We took gastric biopsy specimens at endoscopy from H pylori infected (n = 17) and uninfected (n = 18) patients and assessed MMP-7 expression by ELISA, real time polymerase chain reaction (PCR), and immunohistochemistry (concentrating on epithelial cells in the proliferative zone). We PCR typed H pylori for cagE and vacA. We performed H pylori/cell line coculture studies with wild-type pathogenic and non-pathogenic H pylori strains and with CagE− and VacA− isogenic mutants. Results: Gastric biopsy specimens from H pylori+ patients expressed higher levels of MMP-7 at the protein and mRNA levels in the antrum and corpus (for example, by ELISA: H pylori+ 0.182 OD units vH pylori− 0.059; p = 0.009 antrum). Epithelial cells from H pylori+ patients stained more intensely for MMP-7 than those from uninfected patients, including in the proliferative zone containing pluripotent cells (p<0.03 antrum, p<0.04 body). Upregulation of MMP-7 in epithelial cells was confirmed at the protein and mRNA levels by H pylori/cell line coculture. These experiments also showed that MMP-7 upregulation was dependent on an intact H pyloricag pathogenicity island but not on the vacuolating cytotoxin. Conclusion: We speculate that increased expression of MMP-7 in H pylori gastritis may contribute to gastric carcinogenesis.</abstract><cop>London</cop><pub>BMJ Publishing Group Ltd and British Society of Gastroenterology</pub><pmid>12970131</pmid><doi>10.1136/gut.52.10.1408</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Gut, 2003-10, Vol.52 (10), p.1408-1413 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Aged Apoptosis Bacterial Proteins - analysis Biological and medical sciences Biopsy cag pathogenicity island Causes of Cells, Cultured Cytokines ELISA Enzyme Activation enzyme linked immunosorbent assay Enzyme-Linked Immunosorbent Assay - methods Enzymes Epithelial Cells - enzymology FCS Female fetal calf serum GAPDH Gastric cancer Gastric Mucosa - enzymology Gastroenterology. Liver. Pancreas. Abdomen Gene expression Genetic aspects glyceraldehyde-3-phosphate dehydrogenase Helicobacter infections Helicobacter Infections - enzymology Helicobacter pylori Helicobacter pylori - metabolism Humans Immunohistochemistry Influence Kinases Ligands Male Matrix Metalloproteinase 7 - metabolism matrix metalloproteinase-7 matrix metalloproteinase-7 (matrilysin) matrix metalloproteinases Medical research Medical sciences Metalloproteins Middle Aged MMP-7 MMPs Nuclear Proteins - analysis Patients PCR Physiological aspects polymerase chain reaction Regulation Reverse Transcriptase Polymerase Chain Reaction Scholarships & fellowships SDS-PAGE sodium dodecyl sulphate-polyacrylamide gel electrophoresis Stomach Stomach cancer Stomach. Duodenum. Small intestine. Colon. Rectum. Anus threshold cycle TNF-α Tumor necrosis factor-TNF Tumors tumour necrosis factor α Ulcers Up-Regulation |
| title | Helicobacter pylori upregulates matrilysin (MMP-7) in epithelial cells in vivo and in vitro in a Cag dependent manner |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-21T17%3A21%3A23IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Helicobacter%20pylori%20upregulates%20matrilysin%20(MMP-7)%20in%20epithelial%20cells%20in%20vivo%20and%20in%20vitro%20in%20a%20Cag%20dependent%20manner&rft.jtitle=Gut&rft.au=Bebb,%20J%20R&rft.date=2003-10-01&rft.volume=52&rft.issue=10&rft.spage=1408&rft.epage=1413&rft.pages=1408-1413&rft.issn=0017-5749&rft.eissn=1468-3288&rft.coden=GUTTAK&rft_id=info:doi/10.1136/gut.52.10.1408&rft_dat=%3Cgale_pubme%3EA108720905%3C/gale_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1779320926&rft_id=info:pmid/12970131&rft_galeid=A108720905&rfr_iscdi=true |