β-Catenin and p120 Mediate PPARδ-Dependent Proliferation Induced by Helicobacter pylori in Human and Rodent Epithelia
Background & Aims Colonization of gastric mucosa by Helicobacter pylori leads to epithelial hyperproliferation, which increases the risk for gastric adenocarcinoma. One H pylori virulence locus associated with cancer risk, cag , encodes a secretion system that transports effectors into host cell...
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| Veröffentlicht in: | Gastroenterology (New York, N.Y. 1943) N.Y. 1943), 2011-08, Vol.141 (2), p.553-564 |
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| creator | Nagy, Toni A Wroblewski, Lydia E Wang, Dingzhi Piazuelo, M. Blanca Delgado, Alberto Romero–Gallo, Judith Noto, Jennifer Israel, Dawn A Ogden, Seth R Correa, Pelayo Cover, Timothy L Peek, Richard M |
| description | Background & Aims Colonization of gastric mucosa by Helicobacter pylori leads to epithelial hyperproliferation, which increases the risk for gastric adenocarcinoma. One H pylori virulence locus associated with cancer risk, cag , encodes a secretion system that transports effectors into host cells and leads to aberrant activation of β-catenin and p120-catenin (p120). Peroxisome proliferator-activated receptor (PPAR)δ is a ligand-activated transcription factor that affects oncogenesis in conjunction with β-catenin. We used a carcinogenic H pylori strain to define the role of microbial virulence constituents and PPARδ in regulating epithelial responses that mediate development of adenocarcinoma. Methods Gastric epithelial cells or colonies were co-cultured with the H pylori cag + strain 7.13 or cagE− , cagA − , soluble lytic transglycosylase − , or cagA − /soluble lytic transglycosylase − mutants. Levels of PPARδ and cyclin E1 were determined by real-time, reverse-transcription polymerase chain reaction, immunoblot analysis, or immunofluorescence microscopy; proliferation was measured in 3-dimensional culture. PPARδ and Ki67 expression were determined by immunohistochemical analysis of human biopsies and rodent gastric mucosa. Results H pylori induced β-catenin– and p120-dependent expression and activation of PPARδ in gastric epithelial cells, which were mediated by the cag secretion system substrates CagA and peptidoglycan. H pylori stimulated proliferation in vitro, which required PPARδ-mediated activation of cyclin E1; H pylori did not induce expression of cyclin E1 in a genetic model of PPARδ deficiency. PPARδ expression and proliferation in rodent and human gastric tissue was selectively induced by cag + strains and PPARδ levels normalized after eradication of H pylori. Conclusions The H pylori cag secretion system activates β-catenin, p120, and PPARδ, which promote gastric epithelial cell proliferation via activation of cyclin E1. PPARδ might contribute to gastric adenocarcinoma development in humans. |
| doi_str_mv | 10.1053/j.gastro.2011.05.004 |
| format | Article |
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Blanca ; Delgado, Alberto ; Romero–Gallo, Judith ; Noto, Jennifer ; Israel, Dawn A ; Ogden, Seth R ; Correa, Pelayo ; Cover, Timothy L ; Peek, Richard M</creator><creatorcontrib>Nagy, Toni A ; Wroblewski, Lydia E ; Wang, Dingzhi ; Piazuelo, M. Blanca ; Delgado, Alberto ; Romero–Gallo, Judith ; Noto, Jennifer ; Israel, Dawn A ; Ogden, Seth R ; Correa, Pelayo ; Cover, Timothy L ; Peek, Richard M</creatorcontrib><description>Background & Aims Colonization of gastric mucosa by Helicobacter pylori leads to epithelial hyperproliferation, which increases the risk for gastric adenocarcinoma. One H pylori virulence locus associated with cancer risk, cag , encodes a secretion system that transports effectors into host cells and leads to aberrant activation of β-catenin and p120-catenin (p120). Peroxisome proliferator-activated receptor (PPAR)δ is a ligand-activated transcription factor that affects oncogenesis in conjunction with β-catenin. We used a carcinogenic H pylori strain to define the role of microbial virulence constituents and PPARδ in regulating epithelial responses that mediate development of adenocarcinoma. Methods Gastric epithelial cells or colonies were co-cultured with the H pylori cag + strain 7.13 or cagE− , cagA − , soluble lytic transglycosylase − , or cagA − /soluble lytic transglycosylase − mutants. Levels of PPARδ and cyclin E1 were determined by real-time, reverse-transcription polymerase chain reaction, immunoblot analysis, or immunofluorescence microscopy; proliferation was measured in 3-dimensional culture. PPARδ and Ki67 expression were determined by immunohistochemical analysis of human biopsies and rodent gastric mucosa. Results H pylori induced β-catenin– and p120-dependent expression and activation of PPARδ in gastric epithelial cells, which were mediated by the cag secretion system substrates CagA and peptidoglycan. H pylori stimulated proliferation in vitro, which required PPARδ-mediated activation of cyclin E1; H pylori did not induce expression of cyclin E1 in a genetic model of PPARδ deficiency. PPARδ expression and proliferation in rodent and human gastric tissue was selectively induced by cag + strains and PPARδ levels normalized after eradication of H pylori. Conclusions The H pylori cag secretion system activates β-catenin, p120, and PPARδ, which promote gastric epithelial cell proliferation via activation of cyclin E1. PPARδ might contribute to gastric adenocarcinoma development in humans.</description><identifier>ISSN: 0016-5085</identifier><identifier>EISSN: 1528-0012</identifier><identifier>DOI: 10.1053/j.gastro.2011.05.004</identifier><identifier>PMID: 21704622</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenocarcinoma - microbiology ; Adenocarcinoma - pathology ; Animals ; Antigens, Bacterial - genetics ; Antigens, Bacterial - metabolism ; Bacteria ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; beta Catenin - metabolism ; Catenins - metabolism ; Cell Proliferation ; Cell Transformation, Neoplastic ; Cells, Cultured ; Cyclin E - metabolism ; Epithelial Cells - metabolism ; Epithelial Cells - microbiology ; Gastric Mucosa - metabolism ; Gastric Mucosa - pathology ; Gastroenterology and Hepatology ; Gerbillinae ; Helicobacter Infections - metabolism ; Helicobacter pylori - genetics ; Helicobacter pylori - metabolism ; Humans ; Ki-67 Antigen - metabolism ; Mongolian Gerbils ; Oncogene Proteins - metabolism ; PPAR delta - metabolism ; Signal Transduction ; Signaling ; Stomach Cancer ; Stomach Neoplasms - microbiology ; Stomach Neoplasms - pathology</subject><ispartof>Gastroenterology (New York, N.Y. 1943), 2011-08, Vol.141 (2), p.553-564</ispartof><rights>AGA Institute</rights><rights>2011 AGA Institute</rights><rights>Copyright © 2011 AGA Institute. Published by Elsevier Inc. All rights reserved.</rights><rights>2011 The American Gastroenterological Association. Published by Elsevier Inc. All rights reserved. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c517t-7627f4bf4b1dd07f700accb5fee09135733adb91bb2a84bd17dfa32431fdcf123</citedby><cites>FETCH-LOGICAL-c517t-7627f4bf4b1dd07f700accb5fee09135733adb91bb2a84bd17dfa32431fdcf123</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0016508511006214$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21704622$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nagy, Toni A</creatorcontrib><creatorcontrib>Wroblewski, Lydia E</creatorcontrib><creatorcontrib>Wang, Dingzhi</creatorcontrib><creatorcontrib>Piazuelo, M. Blanca</creatorcontrib><creatorcontrib>Delgado, Alberto</creatorcontrib><creatorcontrib>Romero–Gallo, Judith</creatorcontrib><creatorcontrib>Noto, Jennifer</creatorcontrib><creatorcontrib>Israel, Dawn A</creatorcontrib><creatorcontrib>Ogden, Seth R</creatorcontrib><creatorcontrib>Correa, Pelayo</creatorcontrib><creatorcontrib>Cover, Timothy L</creatorcontrib><creatorcontrib>Peek, Richard M</creatorcontrib><title>β-Catenin and p120 Mediate PPARδ-Dependent Proliferation Induced by Helicobacter pylori in Human and Rodent Epithelia</title><title>Gastroenterology (New York, N.Y. 1943)</title><addtitle>Gastroenterology</addtitle><description>Background & Aims Colonization of gastric mucosa by Helicobacter pylori leads to epithelial hyperproliferation, which increases the risk for gastric adenocarcinoma. One H pylori virulence locus associated with cancer risk, cag , encodes a secretion system that transports effectors into host cells and leads to aberrant activation of β-catenin and p120-catenin (p120). Peroxisome proliferator-activated receptor (PPAR)δ is a ligand-activated transcription factor that affects oncogenesis in conjunction with β-catenin. We used a carcinogenic H pylori strain to define the role of microbial virulence constituents and PPARδ in regulating epithelial responses that mediate development of adenocarcinoma. Methods Gastric epithelial cells or colonies were co-cultured with the H pylori cag + strain 7.13 or cagE− , cagA − , soluble lytic transglycosylase − , or cagA − /soluble lytic transglycosylase − mutants. Levels of PPARδ and cyclin E1 were determined by real-time, reverse-transcription polymerase chain reaction, immunoblot analysis, or immunofluorescence microscopy; proliferation was measured in 3-dimensional culture. PPARδ and Ki67 expression were determined by immunohistochemical analysis of human biopsies and rodent gastric mucosa. Results H pylori induced β-catenin– and p120-dependent expression and activation of PPARδ in gastric epithelial cells, which were mediated by the cag secretion system substrates CagA and peptidoglycan. H pylori stimulated proliferation in vitro, which required PPARδ-mediated activation of cyclin E1; H pylori did not induce expression of cyclin E1 in a genetic model of PPARδ deficiency. PPARδ expression and proliferation in rodent and human gastric tissue was selectively induced by cag + strains and PPARδ levels normalized after eradication of H pylori. Conclusions The H pylori cag secretion system activates β-catenin, p120, and PPARδ, which promote gastric epithelial cell proliferation via activation of cyclin E1. PPARδ might contribute to gastric adenocarcinoma development in humans.</description><subject>Adenocarcinoma - microbiology</subject><subject>Adenocarcinoma - pathology</subject><subject>Animals</subject><subject>Antigens, Bacterial - genetics</subject><subject>Antigens, Bacterial - metabolism</subject><subject>Bacteria</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>beta Catenin - metabolism</subject><subject>Catenins - metabolism</subject><subject>Cell Proliferation</subject><subject>Cell Transformation, Neoplastic</subject><subject>Cells, Cultured</subject><subject>Cyclin E - metabolism</subject><subject>Epithelial Cells - metabolism</subject><subject>Epithelial Cells - microbiology</subject><subject>Gastric Mucosa - metabolism</subject><subject>Gastric Mucosa - pathology</subject><subject>Gastroenterology and Hepatology</subject><subject>Gerbillinae</subject><subject>Helicobacter Infections - metabolism</subject><subject>Helicobacter pylori - genetics</subject><subject>Helicobacter pylori - metabolism</subject><subject>Humans</subject><subject>Ki-67 Antigen - metabolism</subject><subject>Mongolian Gerbils</subject><subject>Oncogene Proteins - metabolism</subject><subject>PPAR delta - metabolism</subject><subject>Signal Transduction</subject><subject>Signaling</subject><subject>Stomach Cancer</subject><subject>Stomach Neoplasms - microbiology</subject><subject>Stomach Neoplasms - pathology</subject><issn>0016-5085</issn><issn>1528-0012</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkttuEzEQhi0EoqHwBgj5BXaZsfeQ3CBVoZBKRUQFri0fZluHjb3yboryWojn6DPhECiHGyRLI3k834z_fxh7jlAi1PLlprzW45RiKQCxhLoEqB6wGdZiXgCgeMhmOTRFDfP6hD0Zxw0ALOQcH7MTgS1UjRAz9uXua7HUEwUfuA6ODyiAvyPn8x1fr8-u7r4Vr2mg4ChMfJ1i7ztKevIx8IvgdpYcN3u-ot7baLSdKPFh38fkeSaudlt95F7FH4DzwU83-a1-yh51uh_p2c94yj69Of-4XBWX799eLM8uC1tjOxVtI9quMvmgc9B2LYC21tQdESxQ1q2U2pkFGiP0vDIOW9dpKSqJnbMdCnnKXh25w85sydk8RNK9GpLf6rRXUXv1dyb4G3Udb5XMQjYgM6A6AmyK45iou69FUAcj1EYdjVAHIxTUKhuRy1782fe-6Jfyvwej_PtbT0mN1lPIevpEdlIu-v91-Bdgex-81f1n2tO4ibsUsrIK1SgUqA-HZTjsAiJAI7CS3wHomrRK</recordid><startdate>20110801</startdate><enddate>20110801</enddate><creator>Nagy, Toni A</creator><creator>Wroblewski, Lydia E</creator><creator>Wang, Dingzhi</creator><creator>Piazuelo, M. Blanca</creator><creator>Delgado, Alberto</creator><creator>Romero–Gallo, Judith</creator><creator>Noto, Jennifer</creator><creator>Israel, Dawn A</creator><creator>Ogden, Seth R</creator><creator>Correa, Pelayo</creator><creator>Cover, Timothy L</creator><creator>Peek, Richard M</creator><general>Elsevier Inc</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>5PM</scope></search><sort><creationdate>20110801</creationdate><title>β-Catenin and p120 Mediate PPARδ-Dependent Proliferation Induced by Helicobacter pylori in Human and Rodent Epithelia</title><author>Nagy, Toni A ; Wroblewski, Lydia E ; Wang, Dingzhi ; Piazuelo, M. 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Blanca</creatorcontrib><creatorcontrib>Delgado, Alberto</creatorcontrib><creatorcontrib>Romero–Gallo, Judith</creatorcontrib><creatorcontrib>Noto, Jennifer</creatorcontrib><creatorcontrib>Israel, Dawn A</creatorcontrib><creatorcontrib>Ogden, Seth R</creatorcontrib><creatorcontrib>Correa, Pelayo</creatorcontrib><creatorcontrib>Cover, Timothy L</creatorcontrib><creatorcontrib>Peek, Richard M</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Gastroenterology (New York, N.Y. 1943)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nagy, Toni A</au><au>Wroblewski, Lydia E</au><au>Wang, Dingzhi</au><au>Piazuelo, M. Blanca</au><au>Delgado, Alberto</au><au>Romero–Gallo, Judith</au><au>Noto, Jennifer</au><au>Israel, Dawn A</au><au>Ogden, Seth R</au><au>Correa, Pelayo</au><au>Cover, Timothy L</au><au>Peek, Richard M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>β-Catenin and p120 Mediate PPARδ-Dependent Proliferation Induced by Helicobacter pylori in Human and Rodent Epithelia</atitle><jtitle>Gastroenterology (New York, N.Y. 1943)</jtitle><addtitle>Gastroenterology</addtitle><date>2011-08-01</date><risdate>2011</risdate><volume>141</volume><issue>2</issue><spage>553</spage><epage>564</epage><pages>553-564</pages><issn>0016-5085</issn><eissn>1528-0012</eissn><abstract>Background & Aims Colonization of gastric mucosa by Helicobacter pylori leads to epithelial hyperproliferation, which increases the risk for gastric adenocarcinoma. One H pylori virulence locus associated with cancer risk, cag , encodes a secretion system that transports effectors into host cells and leads to aberrant activation of β-catenin and p120-catenin (p120). Peroxisome proliferator-activated receptor (PPAR)δ is a ligand-activated transcription factor that affects oncogenesis in conjunction with β-catenin. We used a carcinogenic H pylori strain to define the role of microbial virulence constituents and PPARδ in regulating epithelial responses that mediate development of adenocarcinoma. Methods Gastric epithelial cells or colonies were co-cultured with the H pylori cag + strain 7.13 or cagE− , cagA − , soluble lytic transglycosylase − , or cagA − /soluble lytic transglycosylase − mutants. Levels of PPARδ and cyclin E1 were determined by real-time, reverse-transcription polymerase chain reaction, immunoblot analysis, or immunofluorescence microscopy; proliferation was measured in 3-dimensional culture. PPARδ and Ki67 expression were determined by immunohistochemical analysis of human biopsies and rodent gastric mucosa. Results H pylori induced β-catenin– and p120-dependent expression and activation of PPARδ in gastric epithelial cells, which were mediated by the cag secretion system substrates CagA and peptidoglycan. H pylori stimulated proliferation in vitro, which required PPARδ-mediated activation of cyclin E1; H pylori did not induce expression of cyclin E1 in a genetic model of PPARδ deficiency. PPARδ expression and proliferation in rodent and human gastric tissue was selectively induced by cag + strains and PPARδ levels normalized after eradication of H pylori. Conclusions The H pylori cag secretion system activates β-catenin, p120, and PPARδ, which promote gastric epithelial cell proliferation via activation of cyclin E1. PPARδ might contribute to gastric adenocarcinoma development in humans.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>21704622</pmid><doi>10.1053/j.gastro.2011.05.004</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenocarcinoma - microbiology Adenocarcinoma - pathology Animals Antigens, Bacterial - genetics Antigens, Bacterial - metabolism Bacteria Bacterial Proteins - genetics Bacterial Proteins - metabolism beta Catenin - metabolism Catenins - metabolism Cell Proliferation Cell Transformation, Neoplastic Cells, Cultured Cyclin E - metabolism Epithelial Cells - metabolism Epithelial Cells - microbiology Gastric Mucosa - metabolism Gastric Mucosa - pathology Gastroenterology and Hepatology Gerbillinae Helicobacter Infections - metabolism Helicobacter pylori - genetics Helicobacter pylori - metabolism Humans Ki-67 Antigen - metabolism Mongolian Gerbils Oncogene Proteins - metabolism PPAR delta - metabolism Signal Transduction Signaling Stomach Cancer Stomach Neoplasms - microbiology Stomach Neoplasms - pathology |
| title | β-Catenin and p120 Mediate PPARδ-Dependent Proliferation Induced by Helicobacter pylori in Human and Rodent Epithelia |
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