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Microaerophilic conditions permit to mimic in vitro events occurring during in vivo Helicobacter pylori infection and to identify Rho/Ras-associated proteins in cellular signaling.

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Τίτλος: Microaerophilic conditions permit to mimic in vitro events occurring during in vivo Helicobacter pylori infection and to identify Rho/Ras-associated proteins in cellular signaling.
Συγγραφείς: Cottet, S., Corthésy-Theulaz, I., Spertini, F., Corthésy, B.
Έτος έκδοσης: 2002
Συλλογή: Université de Lausanne (UNIL): Serval - Serveur académique lausannois
Θεματικοί όροι: Caco-2 Cells, Cell Polarity, Chemokines/secretion, Cortactin, DNA-Binding Proteins/metabolism, Epithelial Cells/metabolism, GTPase-Activating Proteins, Gastric Mucosa/secretion, Guanine Nucleotide Exchange Factors/metabolism, Helicobacter Infections/metabolism, Helicobacter pylori/enzymology, Helicobacter pylori/growth & development, Humans, Microfilament Proteins/metabolism, NF-kappa B/metabolism, Nuclear Proteins/metabolism, Phosphoproteins/metabolism, Phosphorylation, RNA-Binding Proteins/metabolism, Repressor Proteins, Urease/biosynthesis, p120 GTPase Activating Protein/metabolism, ras-GRF1
Περιγραφή: Molecular dissection of the mechanisms underlying Helicobacter pylori infection suffers from the lack of in vitro systems mimicking in vivo observations. A system was developed whereby human epithelial cells (Caco-2) grown as polarized monolayers and bacteria can communicate with each other under culture conditions optimal for each partner. Caco-2 cells grown on filter supports were inserted in a vertical position into diffusion chambers equilibrated with air and 5% CO(2) at their basolateral surface (aerophilic conditions) and 5% CO(2), 5% O(2), 90% N(2) (microaerophilic conditions) in the apical compartment. Remarkably, the epithelial polarized layer was stable under these asymmetric culture conditions for at least 24 h, and the presence of Caco-2 cells was necessary to maintain H. pylori growth. In contrast to previous studies conducted with non-polarized Caco-2 cells and other cell lines kept under aerophilic conditions, we found H. pylori-dependent stimulation of cytokine secretion (MCP-1 (monocyte chemoattractant protein-1), GRO-alpha (growth-regulated oncogene-alpha), RANTES (regulated on activation normal T cell expressed and secreted)). This correlated with nuclear translocation of NF-kappaB p50 and p65 subunits. Tyrosine phosphorylation of nine cellular proteins was induced or enhanced; we identified p120(RasGAP), p190(RhoGAP), p62dok (downstream of tyrosine kinases), and cortactin as H. pylori-inducible targets. Moreover, reduction of H. pylori urease expression was observed in adherent bacteria as compared with bacteria in suspension. In addition to mimicking several observations seen in the inflamed gastric mucosa, the novel in vitro system was allowed to underscore complex cellular events not seen in classical in vitro analyses of microaerophilic bacteria-epithelial cell cross-talk.
Τύπος εγγράφου: article in journal/newspaper
Γλώσσα: English
ISBN: 978-0-00-177959-4
0-00-177959-1
ISSN: 0021-9258
Relation: Journal of Biological Chemistry; https://iris.unil.ch/handle/iris/248444; serval:BIB_DADA8E1BE436; 000177959100061
DOI: 10.1074/jbc.M201726200
Διαθεσιμότητα: https://iris.unil.ch/handle/iris/248444
https://doi.org/10.1074/jbc.M201726200
Αριθμός Καταχώρησης: edsbas.D18EB310
Βάση Δεδομένων: BASE
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  Data: Microaerophilic conditions permit to mimic in vitro events occurring during in vivo Helicobacter pylori infection and to identify Rho/Ras-associated proteins in cellular signaling.
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  Data: <searchLink fieldCode="AR" term="%22Cottet%2C+S%2E%22">Cottet, S.</searchLink><br /><searchLink fieldCode="AR" term="%22Corthésy-Theulaz%2C+I%2E%22">Corthésy-Theulaz, I.</searchLink><br /><searchLink fieldCode="AR" term="%22Spertini%2C+F%2E%22">Spertini, F.</searchLink><br /><searchLink fieldCode="AR" term="%22Corthésy%2C+B%2E%22">Corthésy, B.</searchLink>
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  Data: 2002
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  Data: Université de Lausanne (UNIL): Serval - Serveur académique lausannois
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  Data: <searchLink fieldCode="DE" term="%22Caco-2+Cells%22">Caco-2 Cells</searchLink><br /><searchLink fieldCode="DE" term="%22Cell+Polarity%22">Cell Polarity</searchLink><br /><searchLink fieldCode="DE" term="%22Chemokines%2Fsecretion%22">Chemokines/secretion</searchLink><br /><searchLink fieldCode="DE" term="%22Cortactin%22">Cortactin</searchLink><br /><searchLink fieldCode="DE" term="%22DNA-Binding+Proteins%2Fmetabolism%22">DNA-Binding Proteins/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Epithelial+Cells%2Fmetabolism%22">Epithelial Cells/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22GTPase-Activating+Proteins%22">GTPase-Activating Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Gastric+Mucosa%2Fsecretion%22">Gastric Mucosa/secretion</searchLink><br /><searchLink fieldCode="DE" term="%22Guanine+Nucleotide+Exchange+Factors%2Fmetabolism%22">Guanine Nucleotide Exchange Factors/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Helicobacter+Infections%2Fmetabolism%22">Helicobacter Infections/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Helicobacter+pylori%2Fenzymology%22">Helicobacter pylori/enzymology</searchLink><br /><searchLink fieldCode="DE" term="%22Helicobacter+pylori%2Fgrowth+%26+development%22">Helicobacter pylori/growth & development</searchLink><br /><searchLink fieldCode="DE" term="%22Humans%22">Humans</searchLink><br /><searchLink fieldCode="DE" term="%22Microfilament+Proteins%2Fmetabolism%22">Microfilament Proteins/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22NF-kappa+B%2Fmetabolism%22">NF-kappa B/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Nuclear+Proteins%2Fmetabolism%22">Nuclear Proteins/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Phosphoproteins%2Fmetabolism%22">Phosphoproteins/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Phosphorylation%22">Phosphorylation</searchLink><br /><searchLink fieldCode="DE" term="%22RNA-Binding+Proteins%2Fmetabolism%22">RNA-Binding Proteins/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22Repressor+Proteins%22">Repressor Proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Urease%2Fbiosynthesis%22">Urease/biosynthesis</searchLink><br /><searchLink fieldCode="DE" term="%22p120+GTPase+Activating+Protein%2Fmetabolism%22">p120 GTPase Activating Protein/metabolism</searchLink><br /><searchLink fieldCode="DE" term="%22ras-GRF1%22">ras-GRF1</searchLink>
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  Data: Molecular dissection of the mechanisms underlying Helicobacter pylori infection suffers from the lack of in vitro systems mimicking in vivo observations. A system was developed whereby human epithelial cells (Caco-2) grown as polarized monolayers and bacteria can communicate with each other under culture conditions optimal for each partner. Caco-2 cells grown on filter supports were inserted in a vertical position into diffusion chambers equilibrated with air and 5% CO(2) at their basolateral surface (aerophilic conditions) and 5% CO(2), 5% O(2), 90% N(2) (microaerophilic conditions) in the apical compartment. Remarkably, the epithelial polarized layer was stable under these asymmetric culture conditions for at least 24 h, and the presence of Caco-2 cells was necessary to maintain H. pylori growth. In contrast to previous studies conducted with non-polarized Caco-2 cells and other cell lines kept under aerophilic conditions, we found H. pylori-dependent stimulation of cytokine secretion (MCP-1 (monocyte chemoattractant protein-1), GRO-alpha (growth-regulated oncogene-alpha), RANTES (regulated on activation normal T cell expressed and secreted)). This correlated with nuclear translocation of NF-kappaB p50 and p65 subunits. Tyrosine phosphorylation of nine cellular proteins was induced or enhanced; we identified p120(RasGAP), p190(RhoGAP), p62dok (downstream of tyrosine kinases), and cortactin as H. pylori-inducible targets. Moreover, reduction of H. pylori urease expression was observed in adherent bacteria as compared with bacteria in suspension. In addition to mimicking several observations seen in the inflamed gastric mucosa, the novel in vitro system was allowed to underscore complex cellular events not seen in classical in vitro analyses of microaerophilic bacteria-epithelial cell cross-talk.
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  Data: Journal of Biological Chemistry; https://iris.unil.ch/handle/iris/248444; serval:BIB_DADA8E1BE436; 000177959100061
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  Data: 10.1074/jbc.M201726200
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        Value: 10.1074/jbc.M201726200
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      – Text: English
    Subjects:
      – SubjectFull: Caco-2 Cells
        Type: general
      – SubjectFull: Cell Polarity
        Type: general
      – SubjectFull: Chemokines/secretion
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      – SubjectFull: Cortactin
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      – SubjectFull: GTPase-Activating Proteins
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      – SubjectFull: Gastric Mucosa/secretion
        Type: general
      – SubjectFull: Guanine Nucleotide Exchange Factors/metabolism
        Type: general
      – SubjectFull: Helicobacter Infections/metabolism
        Type: general
      – SubjectFull: Helicobacter pylori/enzymology
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      – SubjectFull: Humans
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      – SubjectFull: Microfilament Proteins/metabolism
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      – SubjectFull: RNA-Binding Proteins/metabolism
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      – SubjectFull: Repressor Proteins
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      – SubjectFull: Urease/biosynthesis
        Type: general
      – SubjectFull: p120 GTPase Activating Protein/metabolism
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      – SubjectFull: ras-GRF1
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      – TitleFull: Microaerophilic conditions permit to mimic in vitro events occurring during in vivo Helicobacter pylori infection and to identify Rho/Ras-associated proteins in cellular signaling.
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