Serveur d'exploration sur le suicide chez les dentistes

Attention, ce site est en cours de développement !
Attention, site généré par des moyens informatiques à partir de corpus bruts.
Les informations ne sont donc pas validées.

Porphyromonas gingivalis Cell Wall Components Induce Programmed Death Ligand 1 (PD-L1) Expression on Human Oral Carcinoma Cells by a Receptor-Interacting Protein Kinase 2 (RIP2)-Dependent Mechanism.

Identifieur interne : 000032 ( Main/Exploration ); précédent : 000031; suivant : 000033

Porphyromonas gingivalis Cell Wall Components Induce Programmed Death Ligand 1 (PD-L1) Expression on Human Oral Carcinoma Cells by a Receptor-Interacting Protein Kinase 2 (RIP2)-Dependent Mechanism.

Auteurs : S. Groeger [Allemagne] ; F. Denter [Allemagne] ; G. Lochnit [Allemagne] ; M L Schmitz [Allemagne] ; J. Meyle [Allemagne]

Source :

RBID : pubmed:32041789

Descripteurs français

English descriptors

Abstract

Programmed death-ligand 1 (PD-L1/B7-H1) serves as a cosignaling molecule in cell-mediated immune responses and contributes to chronicity of inflammation and the escape of tumor cells from immunosurveillance. Here, we investigated the molecular mechanisms leading to PD-L1 upregulation in human oral carcinoma cells and in primary human gingival keratinocytes in response to infection with Porphyromonas gingivalis (P. gingivalis), a keystone pathogen for the development of periodontitis. The bacterial cell wall component peptidoglycan uses bacterial outer membrane vesicles to be taken up by cells. Internalized peptidoglycan triggers cytosolic receptors to induce PD-L1 expression in a myeloid differentiation primary response 88 (Myd88)-independent and receptor-interacting serine/threonine-protein kinase 2 (RIP2)-dependent fashion. Interference with the kinase activity of RIP2 or mitogen-activated protein (MAP) kinases interferes with inducible PD-L1 expression.

DOI: 10.1128/IAI.00051-20
PubMed: 32041789
PubMed Central: PMC7171240


Affiliations:


Links toward previous steps (curation, corpus...)


Le document en format XML

<record>
<TEI>
<teiHeader>
<fileDesc>
<titleStmt>
<title xml:lang="en">Porphyromonas gingivalis Cell Wall Components Induce Programmed Death Ligand 1 (PD-L1) Expression on Human Oral Carcinoma Cells by a Receptor-Interacting Protein Kinase 2 (RIP2)-Dependent Mechanism.</title>
<author>
<name sortKey="Groeger, S" sort="Groeger, S" uniqKey="Groeger S" first="S" last="Groeger">S. Groeger</name>
<affiliation wicri:level="1">
<nlm:affiliation>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen, Germany Sabine.E.Groeger@dentist.med.uni-giessen.de.</nlm:affiliation>
<country wicri:rule="url">Allemagne</country>
<wicri:regionArea>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen</wicri:regionArea>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Denter, F" sort="Denter, F" uniqKey="Denter F" first="F" last="Denter">F. Denter</name>
<affiliation wicri:level="1">
<nlm:affiliation>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen</wicri:regionArea>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Lochnit, G" sort="Lochnit, G" uniqKey="Lochnit G" first="G" last="Lochnit">G. Lochnit</name>
<affiliation wicri:level="1">
<nlm:affiliation>Institute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen</wicri:regionArea>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Schmitz, M L" sort="Schmitz, M L" uniqKey="Schmitz M" first="M L" last="Schmitz">M L Schmitz</name>
<affiliation wicri:level="1">
<nlm:affiliation>Institute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen</wicri:regionArea>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Meyle, J" sort="Meyle, J" uniqKey="Meyle J" first="J" last="Meyle">J. Meyle</name>
<affiliation wicri:level="1">
<nlm:affiliation>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen</wicri:regionArea>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
</affiliation>
</author>
</titleStmt>
<publicationStmt>
<idno type="wicri:source">PubMed</idno>
<date when="2020">2020</date>
<idno type="RBID">pubmed:32041789</idno>
<idno type="pmid">32041789</idno>
<idno type="doi">10.1128/IAI.00051-20</idno>
<idno type="pmc">PMC7171240</idno>
<idno type="wicri:Area/Main/Corpus">000047</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000047</idno>
<idno type="wicri:Area/Main/Curation">000047</idno>
<idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000047</idno>
<idno type="wicri:Area/Main/Exploration">000047</idno>
</publicationStmt>
<sourceDesc>
<biblStruct>
<analytic>
<title xml:lang="en">Porphyromonas gingivalis Cell Wall Components Induce Programmed Death Ligand 1 (PD-L1) Expression on Human Oral Carcinoma Cells by a Receptor-Interacting Protein Kinase 2 (RIP2)-Dependent Mechanism.</title>
<author>
<name sortKey="Groeger, S" sort="Groeger, S" uniqKey="Groeger S" first="S" last="Groeger">S. Groeger</name>
<affiliation wicri:level="1">
<nlm:affiliation>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen, Germany Sabine.E.Groeger@dentist.med.uni-giessen.de.</nlm:affiliation>
<country wicri:rule="url">Allemagne</country>
<wicri:regionArea>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen</wicri:regionArea>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Denter, F" sort="Denter, F" uniqKey="Denter F" first="F" last="Denter">F. Denter</name>
<affiliation wicri:level="1">
<nlm:affiliation>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen</wicri:regionArea>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Lochnit, G" sort="Lochnit, G" uniqKey="Lochnit G" first="G" last="Lochnit">G. Lochnit</name>
<affiliation wicri:level="1">
<nlm:affiliation>Institute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen</wicri:regionArea>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Schmitz, M L" sort="Schmitz, M L" uniqKey="Schmitz M" first="M L" last="Schmitz">M L Schmitz</name>
<affiliation wicri:level="1">
<nlm:affiliation>Institute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Institute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen</wicri:regionArea>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
</affiliation>
</author>
<author>
<name sortKey="Meyle, J" sort="Meyle, J" uniqKey="Meyle J" first="J" last="Meyle">J. Meyle</name>
<affiliation wicri:level="1">
<nlm:affiliation>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen, Germany.</nlm:affiliation>
<country xml:lang="fr">Allemagne</country>
<wicri:regionArea>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen</wicri:regionArea>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
<wicri:noRegion>Giessen</wicri:noRegion>
</affiliation>
</author>
</analytic>
<series>
<title level="j">Infection and immunity</title>
<idno type="eISSN">1098-5522</idno>
<imprint>
<date when="2020" type="published">2020</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc>
<textClass>
<keywords scheme="KwdEn" xml:lang="en">
<term>Adaptor Proteins, Signal Transducing (metabolism)</term>
<term>B7-H1 Antigen (metabolism)</term>
<term>Bacteroidaceae Infections (metabolism)</term>
<term>Bacteroidaceae Infections (microbiology)</term>
<term>Carcinoma (metabolism)</term>
<term>Carcinoma (microbiology)</term>
<term>Cell Line, Tumor (MeSH)</term>
<term>Cell Wall (metabolism)</term>
<term>Gingiva (metabolism)</term>
<term>Gingiva (microbiology)</term>
<term>Humans (MeSH)</term>
<term>Keratinocytes (metabolism)</term>
<term>Keratinocytes (microbiology)</term>
<term>Mitogen-Activated Protein Kinases (metabolism)</term>
<term>Mouth Neoplasms (metabolism)</term>
<term>Mouth Neoplasms (microbiology)</term>
<term>Periodontitis (metabolism)</term>
<term>Periodontitis (microbiology)</term>
<term>Porphyromonas gingivalis (metabolism)</term>
<term>Receptor-Interacting Protein Serine-Threonine Kinase 2 (metabolism)</term>
<term>Up-Regulation (physiology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Antigène CD274 (métabolisme)</term>
<term>Carcinomes (microbiologie)</term>
<term>Carcinomes (métabolisme)</term>
<term>Gencive (microbiologie)</term>
<term>Gencive (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Infections à Bacteroidaceae (microbiologie)</term>
<term>Infections à Bacteroidaceae (métabolisme)</term>
<term>Kératinocytes (microbiologie)</term>
<term>Kératinocytes (métabolisme)</term>
<term>Lignée cellulaire tumorale (MeSH)</term>
<term>Mitogen-Activated Protein Kinases (métabolisme)</term>
<term>Parodontite (microbiologie)</term>
<term>Parodontite (métabolisme)</term>
<term>Paroi cellulaire (métabolisme)</term>
<term>Porphyromonas gingivalis (métabolisme)</term>
<term>Protéines adaptatrices de la transduction du signal (métabolisme)</term>
<term>Receptor-Interacting Protein Serine-Threonine Kinase 2 (métabolisme)</term>
<term>Régulation positive (physiologie)</term>
<term>Tumeurs de la bouche (microbiologie)</term>
<term>Tumeurs de la bouche (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en">
<term>Adaptor Proteins, Signal Transducing</term>
<term>B7-H1 Antigen</term>
<term>Mitogen-Activated Protein Kinases</term>
<term>Receptor-Interacting Protein Serine-Threonine Kinase 2</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Bacteroidaceae Infections</term>
<term>Carcinoma</term>
<term>Cell Wall</term>
<term>Gingiva</term>
<term>Keratinocytes</term>
<term>Mouth Neoplasms</term>
<term>Periodontitis</term>
<term>Porphyromonas gingivalis</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr">
<term>Carcinomes</term>
<term>Gencive</term>
<term>Infections à Bacteroidaceae</term>
<term>Kératinocytes</term>
<term>Parodontite</term>
<term>Tumeurs de la bouche</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en">
<term>Bacteroidaceae Infections</term>
<term>Carcinoma</term>
<term>Gingiva</term>
<term>Keratinocytes</term>
<term>Mouth Neoplasms</term>
<term>Periodontitis</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Antigène CD274</term>
<term>Carcinomes</term>
<term>Gencive</term>
<term>Infections à Bacteroidaceae</term>
<term>Kératinocytes</term>
<term>Mitogen-Activated Protein Kinases</term>
<term>Parodontite</term>
<term>Paroi cellulaire</term>
<term>Porphyromonas gingivalis</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Receptor-Interacting Protein Serine-Threonine Kinase 2</term>
<term>Tumeurs de la bouche</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr">
<term>Régulation positive</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en">
<term>Up-Regulation</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Cell Line, Tumor</term>
<term>Humans</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr">
<term>Humains</term>
<term>Lignée cellulaire tumorale</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front>
<div type="abstract" xml:lang="en">Programmed death-ligand 1 (PD-L1/B7-H1) serves as a cosignaling molecule in cell-mediated immune responses and contributes to chronicity of inflammation and the escape of tumor cells from immunosurveillance. Here, we investigated the molecular mechanisms leading to PD-L1 upregulation in human oral carcinoma cells and in primary human gingival keratinocytes in response to infection with
<i>Porphyromonas gingivalis</i>
(
<i>P. gingivalis</i>
), a keystone pathogen for the development of periodontitis. The bacterial cell wall component peptidoglycan uses bacterial outer membrane vesicles to be taken up by cells. Internalized peptidoglycan triggers cytosolic receptors to induce PD-L1 expression in a myeloid differentiation primary response 88 (Myd88)-independent and receptor-interacting serine/threonine-protein kinase 2 (RIP2)-dependent fashion. Interference with the kinase activity of RIP2 or mitogen-activated protein (MAP) kinases interferes with inducible PD-L1 expression.</div>
</front>
</TEI>
<pubmed>
<MedlineCitation Status="MEDLINE" Owner="NLM">
<PMID Version="1">32041789</PMID>
<DateCompleted>
<Year>2020</Year>
<Month>10</Month>
<Day>13</Day>
</DateCompleted>
<DateRevised>
<Year>2020</Year>
<Month>10</Month>
<Day>20</Day>
</DateRevised>
<Article PubModel="Electronic-Print">
<Journal>
<ISSN IssnType="Electronic">1098-5522</ISSN>
<JournalIssue CitedMedium="Internet">
<Volume>88</Volume>
<Issue>5</Issue>
<PubDate>
<Year>2020</Year>
<Month>04</Month>
<Day>20</Day>
</PubDate>
</JournalIssue>
<Title>Infection and immunity</Title>
<ISOAbbreviation>Infect Immun</ISOAbbreviation>
</Journal>
<ArticleTitle>Porphyromonas gingivalis Cell Wall Components Induce Programmed Death Ligand 1 (PD-L1) Expression on Human Oral Carcinoma Cells by a Receptor-Interacting Protein Kinase 2 (RIP2)-Dependent Mechanism.</ArticleTitle>
<ELocationID EIdType="pii" ValidYN="Y">e00051-20</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1128/IAI.00051-20</ELocationID>
<Abstract>
<AbstractText>Programmed death-ligand 1 (PD-L1/B7-H1) serves as a cosignaling molecule in cell-mediated immune responses and contributes to chronicity of inflammation and the escape of tumor cells from immunosurveillance. Here, we investigated the molecular mechanisms leading to PD-L1 upregulation in human oral carcinoma cells and in primary human gingival keratinocytes in response to infection with
<i>Porphyromonas gingivalis</i>
(
<i>P. gingivalis</i>
), a keystone pathogen for the development of periodontitis. The bacterial cell wall component peptidoglycan uses bacterial outer membrane vesicles to be taken up by cells. Internalized peptidoglycan triggers cytosolic receptors to induce PD-L1 expression in a myeloid differentiation primary response 88 (Myd88)-independent and receptor-interacting serine/threonine-protein kinase 2 (RIP2)-dependent fashion. Interference with the kinase activity of RIP2 or mitogen-activated protein (MAP) kinases interferes with inducible PD-L1 expression.</AbstractText>
<CopyrightInformation>Copyright © 2020 American Society for Microbiology.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y">
<Author ValidYN="Y">
<LastName>Groeger</LastName>
<ForeName>S</ForeName>
<Initials>S</Initials>
<AffiliationInfo>
<Affiliation>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen, Germany Sabine.E.Groeger@dentist.med.uni-giessen.de.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Denter</LastName>
<ForeName>F</ForeName>
<Initials>F</Initials>
<AffiliationInfo>
<Affiliation>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Lochnit</LastName>
<ForeName>G</ForeName>
<Initials>G</Initials>
<AffiliationInfo>
<Affiliation>Institute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Schmitz</LastName>
<ForeName>M L</ForeName>
<Initials>ML</Initials>
<AffiliationInfo>
<Affiliation>Institute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y">
<LastName>Meyle</LastName>
<ForeName>J</ForeName>
<Initials>J</Initials>
<AffiliationInfo>
<Affiliation>Department of Periodontology, Justus-Liebig-University of Giessen, Giessen, Germany.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList>
<PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic">
<Year>2020</Year>
<Month>04</Month>
<Day>20</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo>
<Country>United States</Country>
<MedlineTA>Infect Immun</MedlineTA>
<NlmUniqueID>0246127</NlmUniqueID>
<ISSNLinking>0019-9567</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D048868">Adaptor Proteins, Signal Transducing</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D060890">B7-H1 Antigen</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C423236">CD274 protein, human</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="C506253">RIPK2 protein, human</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D053475">Receptor-Interacting Protein Serine-Threonine Kinase 2</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>EC 2.7.11.24</RegistryNumber>
<NameOfSubstance UI="D020928">Mitogen-Activated Protein Kinases</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList>
<MeshHeading>
<DescriptorName UI="D048868" MajorTopicYN="N">Adaptor Proteins, Signal Transducing</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D060890" MajorTopicYN="N">B7-H1 Antigen</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D016866" MajorTopicYN="N">Bacteroidaceae Infections</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D002277" MajorTopicYN="N">Carcinoma</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D045744" MajorTopicYN="N">Cell Line, Tumor</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D002473" MajorTopicYN="N">Cell Wall</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D005881" MajorTopicYN="N">Gingiva</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D015603" MajorTopicYN="N">Keratinocytes</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D020928" MajorTopicYN="N">Mitogen-Activated Protein Kinases</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D009062" MajorTopicYN="N">Mouth Neoplasms</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010518" MajorTopicYN="N">Periodontitis</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D016966" MajorTopicYN="N">Porphyromonas gingivalis</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D053475" MajorTopicYN="N">Receptor-Interacting Protein Serine-Threonine Kinase 2</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D015854" MajorTopicYN="N">Up-Regulation</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM">
<Keyword MajorTopicYN="Y">B7-H1</Keyword>
<Keyword MajorTopicYN="Y">PD-L1</Keyword>
<Keyword MajorTopicYN="Y">Porphyromonas gingivalis</Keyword>
<Keyword MajorTopicYN="Y">immune evasion</Keyword>
<Keyword MajorTopicYN="Y">immune suppression</Keyword>
<Keyword MajorTopicYN="Y">signaling pathway</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData>
<History>
<PubMedPubDate PubStatus="received">
<Year>2020</Year>
<Month>01</Month>
<Day>22</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted">
<Year>2020</Year>
<Month>02</Month>
<Day>06</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed">
<Year>2020</Year>
<Month>2</Month>
<Day>12</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline">
<Year>2020</Year>
<Month>10</Month>
<Day>21</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez">
<Year>2020</Year>
<Month>2</Month>
<Day>12</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>epublish</PublicationStatus>
<ArticleIdList>
<ArticleId IdType="pubmed">32041789</ArticleId>
<ArticleId IdType="pii">IAI.00051-20</ArticleId>
<ArticleId IdType="doi">10.1128/IAI.00051-20</ArticleId>
<ArticleId IdType="pmc">PMC7171240</ArticleId>
</ArticleIdList>
<ReferenceList>
<Reference>
<Citation>Oncoimmunology. 2012 Nov 1;1(8):1223-1225</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">23243584</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Endocrinol. 1992 Sep;134(3):505-11</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">1357069</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Nature. 2002 Mar 14;416(6877):194-9</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">11894098</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Mol Immunol. 2009 Jan;46(3):375-83</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">19081139</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Microbiol Mol Biol Rev. 2010 Mar;74(1):81-94</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">20197500</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>World J Gastroenterol. 2006 Jan 21;12(3):457-9</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">16489649</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Int J Clin Exp Pathol. 2014 Mar 15;7(4):1677-86</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">24817964</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Vis Exp. 2014 Jan 15;(83):e51183</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">24457605</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Mol Microbiol. 2014 Mar;91(5):862-74</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">24405365</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>FEBS Lett. 1989 Nov 20;258(1):156-8</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">2591531</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Nat Commun. 2018 Oct 2;9(1):4043</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">30279485</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Periodontal Res. 2008 Dec;43(6):604-14</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">18771458</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Nat Rev Immunol. 2004 Aug;4(8):641-8</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">15286730</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Front Immunol. 2012 Nov 08;3:328</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">23162548</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Immunol. 2002 Nov 15;169(10):5538-45</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">12421930</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Pathol Oncol Res. 2017 Jan;23(1):99-110</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">27498988</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Immunobiology. 2011 Dec;216(12):1302-10</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">21723642</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Future Microbiol. 2015;10(9):1517-27</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">26343879</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Proteome Res. 2014 May 2;13(5):2420-32</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">24620993</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Clin Periodontol. 2012 May;39(5):425-33</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">22417294</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Int J Oncol. 2017 Jan;50(1):41-48</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">27922697</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>PLoS Pathog. 2014 Mar 27;10(3):e1003933</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">24676390</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>EMBO J. 1992 Nov;11(11):3887-95</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">1396582</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Immunol. 2014 Sep 1;193(5):2218-29</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">25070848</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Exp Med. 2000 Oct 2;192(7):1027-34</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">11015443</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Cell Host Microbe. 2014 May 14;15(5):623-35</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">24746552</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Infect Immun. 2007 Sep;75(9):4334-41</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">17562772</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Immunol Rev. 2000 Feb;173:89-97</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">10719670</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Mol Immunol. 2018 Sep;101:167-175</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">29944986</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Xenobiotica. 2004 Oct;34(10):901-15</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">15764410</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 1998 Jul 3;273(27):16968-75</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">9642260</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Mol Cancer Ther. 2015 Apr;14(4):847-56</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">25695955</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Anal Biochem. 1988 Aug 1;172(2):451-64</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">3056100</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Infect Immun. 2016 Mar 24;84(4):1194-1204</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">26857578</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Nat Rev Immunol. 2015 Jan;15(1):30-44</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">25534621</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Nat Rev Microbiol. 2012 Oct;10(10):717-25</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">22941505</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Anticancer Res. 2019 Jun;39(6):3039-3046</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">31177146</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Prostate. 1993;22(1):75-89</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">7678932</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Clin Immunol. 2012 May;143(2):162-9</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">22397822</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Biol Chem. 2003 Mar 14;278(11):8869-72</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">12527755</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Cell Mol Immunol. 2004 Feb;1(1):37-42</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">16212919</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Immunobiology. 2017 Feb;222(2):137-147</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">28164807</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Immunol. 2002 Oct 1;169(7):3581-8</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">12244148</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Cell Death Differ. 2015 Feb;22(2):225-36</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">25146926</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Nat Med. 2002 Aug;8(8):793-800</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">12091876</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Immunol. 2014 Feb 1;192(3):1079-90</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">24353266</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Trends Microbiol. 2000 Oct;8(10):452-6</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">11044679</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Blood. 2007 Jul 1;110(1):296-304</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">17363736</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>FEMS Microbiol Rev. 2008 Mar;32(2):287-306</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">18070068</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Trends Mol Med. 2015 Mar;21(3):172-83</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">25498392</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Proc Natl Acad Sci U S A. 2003 Apr 29;100(9):5336-41</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">12697896</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Oral Oncol. 2015 Mar;51(3):221-8</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">25500094</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Nat Immunol. 2004 Nov;5(11):1166-74</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">15489856</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>PLoS One. 2016 Apr 01;11(4):e0151967</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">27035339</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Immunol Lett. 2004 Jul 15;94(3):215-22</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">15275969</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Nat Protoc. 2013 Nov;8(11):2281-2308</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">24157548</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Sci Rep. 2016 Sep 14;6:33346</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">27624143</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Immunol. 2006 Mar 1;176(5):3000-9</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">16493058</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Arch Otolaryngol Head Neck Surg. 2007 May;133(5):450-4</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">17515503</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Immunol. 2007 Feb 15;178(4):2380-6</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">17277144</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Xenobiotica. 2004 Nov-Dec;34(11-12):983-1000</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">15801543</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Microbiol Mol Biol Rev. 2004 Jun;68(2):320-44</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">15187187</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>Oral Oncol. 2013 Sep;49(9):887-892</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">23910564</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>J Periodontol. 2005 Mar;76(3):406-10</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">15857075</ArticleId>
</ArticleIdList>
</Reference>
<Reference>
<Citation>mBio. 2012 Dec 04;3(6):e00409-12</Citation>
<ArticleIdList>
<ArticleId IdType="pubmed">23221800</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
<affiliations>
<list>
<country>
<li>Allemagne</li>
</country>
</list>
<tree>
<country name="Allemagne">
<noRegion>
<name sortKey="Groeger, S" sort="Groeger, S" uniqKey="Groeger S" first="S" last="Groeger">S. Groeger</name>
</noRegion>
<name sortKey="Denter, F" sort="Denter, F" uniqKey="Denter F" first="F" last="Denter">F. Denter</name>
<name sortKey="Lochnit, G" sort="Lochnit, G" uniqKey="Lochnit G" first="G" last="Lochnit">G. Lochnit</name>
<name sortKey="Meyle, J" sort="Meyle, J" uniqKey="Meyle J" first="J" last="Meyle">J. Meyle</name>
<name sortKey="Schmitz, M L" sort="Schmitz, M L" uniqKey="Schmitz M" first="M L" last="Schmitz">M L Schmitz</name>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SuicidDentistV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000032 | SxmlIndent | more

Ou

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000032 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    SuicidDentistV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:32041789
   |texte=   Porphyromonas gingivalis Cell Wall Components Induce Programmed Death Ligand 1 (PD-L1) Expression on Human Oral Carcinoma Cells by a Receptor-Interacting Protein Kinase 2 (RIP2)-Dependent Mechanism.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:32041789" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a SuicidDentistV1 

Wicri

This area was generated with Dilib version V0.6.39.
Data generation: Sun Oct 3 17:04:29 2021. Site generation: Sun Oct 3 17:05:17 2021