Eintrag weiter verarbeiten
Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells
Gespeichert in:
| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | Proceedings of the National Academy of Sciences, 102, 2005, 45, S. 16339-16344 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
|
| Schlagwörter: |
| author_facet |
Bagnoli, Fabio Buti, Ludovico Tompkins, Lucy Covacci, Antonello Amieva, Manuel R. Bagnoli, Fabio Buti, Ludovico Tompkins, Lucy Covacci, Antonello Amieva, Manuel R. |
|---|---|
| author |
Bagnoli, Fabio Buti, Ludovico Tompkins, Lucy Covacci, Antonello Amieva, Manuel R. |
| spellingShingle |
Bagnoli, Fabio Buti, Ludovico Tompkins, Lucy Covacci, Antonello Amieva, Manuel R. Proceedings of the National Academy of Sciences Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells Multidisciplinary |
| author_sort |
bagnoli, fabio |
| spelling |
Bagnoli, Fabio Buti, Ludovico Tompkins, Lucy Covacci, Antonello Amieva, Manuel R. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0502598102 <jats:p> CagA is a bacterial effector protein of <jats:italic>Helicobacter pylori</jats:italic> that is translocated via a type IV secretion system into gastric epithelial cells. We previously described that <jats:italic>H. pylori</jats:italic> require CagA to disrupt the organization and assembly of apical junctions in polarized epithelial cells. In this study, we provide evidence that CagA expression is not only sufficient to disrupt the apical junctions but also perturbs epithelial differentiation. CagA-expressing cells lose apicobasal polarity and cell–cell adhesion, extend migratory pseudopodia, and degrade basement membranes, acquiring an invasive phenotype. Expression of the CagA C-terminal domain, which contains the tyrosine phosphorylated EPIYA motifs, induces pseudopodial activity but is not sufficient to induce cell migration. Conversely, the N terminus targets CagA to the cell–cell junctions. Neither domain is sufficient to disrupt cell adhesion or cell polarity, but coexpressed <jats:italic>in trans</jats:italic> , the N terminus determines the localization of both polypeptides. We show that CagA induces a morphogenetic program in polarized Madin–Darby canine kidney cells resembling an epithelial-to-mesenchymal transition. We propose that altered cell–cell and cell matrix interactions may serve as an early event in <jats:italic>H. pylori</jats:italic> -induced carcinogenesis. </jats:p> <i>Helicobacter pylori</i> CagA induces a transition from polarized to invasive phenotypes in MDCK cells Proceedings of the National Academy of Sciences |
| doi_str_mv |
10.1073/pnas.0502598102 |
| facet_avail |
Online Free |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA3My9wbmFzLjA1MDI1OTgxMDI |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA3My9wbmFzLjA1MDI1OTgxMDI |
| institution |
DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 DE-Gla1 DE-Zi4 DE-15 DE-Rs1 DE-Pl11 DE-105 DE-14 DE-Ch1 DE-L229 |
| imprint |
Proceedings of the National Academy of Sciences, 2005 |
| imprint_str_mv |
Proceedings of the National Academy of Sciences, 2005 |
| issn |
0027-8424 1091-6490 |
| issn_str_mv |
0027-8424 1091-6490 |
| language |
English |
| mega_collection |
Proceedings of the National Academy of Sciences (CrossRef) |
| match_str |
bagnoli2005helicobacterpyloricagainducesatransitionfrompolarizedtoinvasivephenotypesinmdckcells |
| publishDateSort |
2005 |
| publisher |
Proceedings of the National Academy of Sciences |
| recordtype |
ai |
| record_format |
ai |
| series |
Proceedings of the National Academy of Sciences |
| source_id |
49 |
| title |
Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| title_unstemmed |
Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| title_full |
Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| title_fullStr |
Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| title_full_unstemmed |
Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| title_short |
Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| title_sort |
<i>helicobacter pylori</i>
caga induces a transition from polarized to invasive phenotypes in mdck cells |
| topic |
Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.0502598102 |
| publishDate |
2005 |
| physical |
16339-16344 |
| description |
<jats:p>
CagA is a bacterial effector protein of
<jats:italic>Helicobacter pylori</jats:italic>
that is translocated via a type IV secretion system into gastric epithelial cells. We previously described that
<jats:italic>H. pylori</jats:italic>
require CagA to disrupt the organization and assembly of apical junctions in polarized epithelial cells. In this study, we provide evidence that CagA expression is not only sufficient to disrupt the apical junctions but also perturbs epithelial differentiation. CagA-expressing cells lose apicobasal polarity and cell–cell adhesion, extend migratory pseudopodia, and degrade basement membranes, acquiring an invasive phenotype. Expression of the CagA C-terminal domain, which contains the tyrosine phosphorylated EPIYA motifs, induces pseudopodial activity but is not sufficient to induce cell migration. Conversely, the N terminus targets CagA to the cell–cell junctions. Neither domain is sufficient to disrupt cell adhesion or cell polarity, but coexpressed
<jats:italic>in trans</jats:italic>
, the N terminus determines the localization of both polypeptides. We show that CagA induces a morphogenetic program in polarized Madin–Darby canine kidney cells resembling an epithelial-to-mesenchymal transition. We propose that altered cell–cell and cell matrix interactions may serve as an early event in
<jats:italic>H. pylori</jats:italic>
-induced carcinogenesis.
</jats:p> |
| container_issue |
45 |
| container_start_page |
16339 |
| container_title |
Proceedings of the National Academy of Sciences |
| container_volume |
102 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792348239988523017 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T18:08:02.121Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Helicobacter+pylori++++++++++++CagA+induces+a+transition+from+polarized+to+invasive+phenotypes+in+MDCK+cells&rft.date=2005-11-08&genre=article&issn=1091-6490&volume=102&issue=45&spage=16339&epage=16344&pages=16339-16344&jtitle=Proceedings+of+the+National+Academy+of+Sciences&atitle=%3Ci%3EHelicobacter+pylori%3C%2Fi%3E%0A++++++++++++CagA+induces+a+transition+from+polarized+to+invasive+phenotypes+in+MDCK+cells&aulast=Amieva&aufirst=Manuel+R.&rft_id=info%3Adoi%2F10.1073%2Fpnas.0502598102&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792348239988523017 |
| author | Bagnoli, Fabio, Buti, Ludovico, Tompkins, Lucy, Covacci, Antonello, Amieva, Manuel R. |
| author_facet | Bagnoli, Fabio, Buti, Ludovico, Tompkins, Lucy, Covacci, Antonello, Amieva, Manuel R., Bagnoli, Fabio, Buti, Ludovico, Tompkins, Lucy, Covacci, Antonello, Amieva, Manuel R. |
| author_sort | bagnoli, fabio |
| container_issue | 45 |
| container_start_page | 16339 |
| container_title | Proceedings of the National Academy of Sciences |
| container_volume | 102 |
| description | <jats:p> CagA is a bacterial effector protein of <jats:italic>Helicobacter pylori</jats:italic> that is translocated via a type IV secretion system into gastric epithelial cells. We previously described that <jats:italic>H. pylori</jats:italic> require CagA to disrupt the organization and assembly of apical junctions in polarized epithelial cells. In this study, we provide evidence that CagA expression is not only sufficient to disrupt the apical junctions but also perturbs epithelial differentiation. CagA-expressing cells lose apicobasal polarity and cell–cell adhesion, extend migratory pseudopodia, and degrade basement membranes, acquiring an invasive phenotype. Expression of the CagA C-terminal domain, which contains the tyrosine phosphorylated EPIYA motifs, induces pseudopodial activity but is not sufficient to induce cell migration. Conversely, the N terminus targets CagA to the cell–cell junctions. Neither domain is sufficient to disrupt cell adhesion or cell polarity, but coexpressed <jats:italic>in trans</jats:italic> , the N terminus determines the localization of both polypeptides. We show that CagA induces a morphogenetic program in polarized Madin–Darby canine kidney cells resembling an epithelial-to-mesenchymal transition. We propose that altered cell–cell and cell matrix interactions may serve as an early event in <jats:italic>H. pylori</jats:italic> -induced carcinogenesis. </jats:p> |
| doi_str_mv | 10.1073/pnas.0502598102 |
| facet_avail | Online, Free |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA3My9wbmFzLjA1MDI1OTgxMDI |
| imprint | Proceedings of the National Academy of Sciences, 2005 |
| imprint_str_mv | Proceedings of the National Academy of Sciences, 2005 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Rs1, DE-Pl11, DE-105, DE-14, DE-Ch1, DE-L229 |
| issn | 0027-8424, 1091-6490 |
| issn_str_mv | 0027-8424, 1091-6490 |
| language | English |
| last_indexed | 2024-03-01T18:08:02.121Z |
| match_str | bagnoli2005helicobacterpyloricagainducesatransitionfrompolarizedtoinvasivephenotypesinmdckcells |
| mega_collection | Proceedings of the National Academy of Sciences (CrossRef) |
| physical | 16339-16344 |
| publishDate | 2005 |
| publishDateSort | 2005 |
| publisher | Proceedings of the National Academy of Sciences |
| record_format | ai |
| recordtype | ai |
| series | Proceedings of the National Academy of Sciences |
| source_id | 49 |
| spelling | Bagnoli, Fabio Buti, Ludovico Tompkins, Lucy Covacci, Antonello Amieva, Manuel R. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0502598102 <jats:p> CagA is a bacterial effector protein of <jats:italic>Helicobacter pylori</jats:italic> that is translocated via a type IV secretion system into gastric epithelial cells. We previously described that <jats:italic>H. pylori</jats:italic> require CagA to disrupt the organization and assembly of apical junctions in polarized epithelial cells. In this study, we provide evidence that CagA expression is not only sufficient to disrupt the apical junctions but also perturbs epithelial differentiation. CagA-expressing cells lose apicobasal polarity and cell–cell adhesion, extend migratory pseudopodia, and degrade basement membranes, acquiring an invasive phenotype. Expression of the CagA C-terminal domain, which contains the tyrosine phosphorylated EPIYA motifs, induces pseudopodial activity but is not sufficient to induce cell migration. Conversely, the N terminus targets CagA to the cell–cell junctions. Neither domain is sufficient to disrupt cell adhesion or cell polarity, but coexpressed <jats:italic>in trans</jats:italic> , the N terminus determines the localization of both polypeptides. We show that CagA induces a morphogenetic program in polarized Madin–Darby canine kidney cells resembling an epithelial-to-mesenchymal transition. We propose that altered cell–cell and cell matrix interactions may serve as an early event in <jats:italic>H. pylori</jats:italic> -induced carcinogenesis. </jats:p> <i>Helicobacter pylori</i> CagA induces a transition from polarized to invasive phenotypes in MDCK cells Proceedings of the National Academy of Sciences |
| spellingShingle | Bagnoli, Fabio, Buti, Ludovico, Tompkins, Lucy, Covacci, Antonello, Amieva, Manuel R., Proceedings of the National Academy of Sciences, Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells, Multidisciplinary |
| title | Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| title_full | Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| title_fullStr | Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| title_full_unstemmed | Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| title_short | Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| title_sort | <i>helicobacter pylori</i> caga induces a transition from polarized to invasive phenotypes in mdck cells |
| title_unstemmed | Helicobacter pylori CagA induces a transition from polarized to invasive phenotypes in MDCK cells |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.0502598102 |