AustralieFrV1, PubMed, Checkpoint, bibRecord, 001557

The NLRP3 inflammasome functions as a driver of the myelodysplastic syndrome phenotype.

Identifieur interne : 001557 ( PubMed/Checkpoint ); précédent : 001556; suivant : 001558

The NLRP3 inflammasome functions as a driver of the myelodysplastic syndrome phenotype.

Auteurs : Ashley A. Basiorka ; Kathy L. Mcgraw ; Erika A. Eksioglu ; Xianghong Chen ; Joseph Johnson ; Ling Zhang [États-Unis] ; Qing Zhang ; Brittany A. Irvine ; Thomas Cluzeau [France] ; David A. Sallman ; Eric Padron ; Rami Komrokji ; Lubomir Sokol ; Rebecca C. Coll [Australie] ; Avril A B. Robertson [Australie] ; Matthew A. Cooper [Australie] ; John L. Cleveland ; Luke A. O'Neill [Irlande (pays)] ; Sheng Wei ; Alan F. List

Source :

Blood [ 1528-0020 ] ; 2016.

RBID : pubmed:27737891

Descripteurs français

English descriptors

KwdEn :
- Animals, Calgranulin B (metabolism), Cell Size, Colony-Forming Units Assay, Hematopoiesis, Hematopoietic Stem Cells (metabolism), Hematopoietic Stem Cells (pathology), Humans, Inflammasomes (metabolism), Ion Channel Gating, Ion Channels (metabolism), Mice, Transgenic, Mutation (genetics), Myelodysplastic Syndromes (metabolism), Myelodysplastic Syndromes (pathology), NADPH Oxidase (metabolism), NLR Family, Pyrin Domain-Containing 3 Protein (metabolism), Phenotype, Pyroptosis, Reactive Oxygen Species (metabolism), beta Catenin (metabolism).
MESH :
- chemical , metabolism : Calgranulin B, Inflammasomes, Ion Channels, NADPH Oxidase, NLR Family, Pyrin Domain-Containing 3 Protein, Reactive Oxygen Species, beta Catenin.
- genetics : Mutation.
- metabolism : Hematopoietic Stem Cells, Myelodysplastic Syndromes.
- pathology : Hematopoietic Stem Cells, Myelodysplastic Syndromes.
- Animals, Cell Size, Colony-Forming Units Assay, Hematopoiesis, Humans, Ion Channel Gating, Mice, Transgenic, Phenotype, Pyroptosis.

Abstract

Despite genetic heterogeneity, myelodysplastic syndromes (MDSs) share features of cytological dysplasia and ineffective hematopoiesis. We report that a hallmark of MDSs is activation of the NLRP3 inflammasome, which drives clonal expansion and pyroptotic cell death. Independent of genotype, MDS hematopoietic stem and progenitor cells (HSPCs) overexpress inflammasome proteins and manifest activated NLRP3 complexes that direct activation of caspase-1, generation of interleukin-1β (IL-1β) and IL-18, and pyroptotic cell death. Mechanistically, pyroptosis is triggered by the alarmin S100A9 that is found in excess in MDS HSPCs and bone marrow plasma. Further, like somatic gene mutations, S100A9-induced signaling activates NADPH oxidase (NOX), increasing levels of reactive oxygen species (ROS) that initiate cation influx, cell swelling, and β-catenin activation. Notably, knockdown of NLRP3 or caspase-1, neutralization of S100A9, and pharmacologic inhibition of NLRP3 or NOX suppress pyroptosis, ROS generation, and nuclear β-catenin in MDSs and are sufficient to restore effective hematopoiesis. Thus, alarmins and founder gene mutations in MDSs license a common redox-sensitive inflammasome circuit, which suggests new avenues for therapeutic intervention.

DOI: 10.1182/blood-2016-07-730556
PubMed: 27737891

Affiliations:

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<author><name sortKey="O Neill, Luke A" sort="O Neill, Luke A" uniqKey="O Neill L" first="Luke A" last="O'Neill">Luke A. O'Neill</name>
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<author><name sortKey="Wei, Sheng" sort="Wei, Sheng" uniqKey="Wei S" first="Sheng" last="Wei">Sheng Wei</name>
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<wicri:noCountry code="no comma">Department of Immunology.</wicri:noCountry>
</affiliation>
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<author><name sortKey="List, Alan F" sort="List, Alan F" uniqKey="List A" first="Alan F" last="List">Alan F. List</name>
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</affiliation>
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<author><name sortKey="Eksioglu, Erika A" sort="Eksioglu, Erika A" uniqKey="Eksioglu E" first="Erika A" last="Eksioglu">Erika A. Eksioglu</name>
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</affiliation>
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<author><name sortKey="Padron, Eric" sort="Padron, Eric" uniqKey="Padron E" first="Eric" last="Padron">Eric Padron</name>
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<wicri:noCountry code="no comma">Department of Malignant Hematology.</wicri:noCountry>
</affiliation>
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<author><name sortKey="Komrokji, Rami" sort="Komrokji, Rami" uniqKey="Komrokji R" first="Rami" last="Komrokji">Rami Komrokji</name>
<affiliation><nlm:affiliation>Department of Malignant Hematology.</nlm:affiliation>
<wicri:noCountry code="no comma">Department of Malignant Hematology.</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Sokol, Lubomir" sort="Sokol, Lubomir" uniqKey="Sokol L" first="Lubomir" last="Sokol">Lubomir Sokol</name>
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<wicri:noCountry code="no comma">Department of Malignant Hematology.</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Coll, Rebecca C" sort="Coll, Rebecca C" uniqKey="Coll R" first="Rebecca C" last="Coll">Rebecca C. Coll</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia.</nlm:affiliation>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Institute for Molecular Bioscience, University of Queensland, Brisbane</wicri:regionArea>
<wicri:noRegion>Brisbane</wicri:noRegion>
</affiliation>
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<author><name sortKey="Robertson, Avril A B" sort="Robertson, Avril A B" uniqKey="Robertson A" first="Avril A B" last="Robertson">Avril A B. Robertson</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia.</nlm:affiliation>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Institute for Molecular Bioscience, University of Queensland, Brisbane</wicri:regionArea>
<wicri:noRegion>Brisbane</wicri:noRegion>
</affiliation>
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<author><name sortKey="Cooper, Matthew A" sort="Cooper, Matthew A" uniqKey="Cooper M" first="Matthew A" last="Cooper">Matthew A. Cooper</name>
<affiliation wicri:level="1"><nlm:affiliation>Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia.</nlm:affiliation>
<country xml:lang="fr">Australie</country>
<wicri:regionArea>Institute for Molecular Bioscience, University of Queensland, Brisbane</wicri:regionArea>
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<author><name sortKey="Cleveland, John L" sort="Cleveland, John L" uniqKey="Cleveland J" first="John L" last="Cleveland">John L. Cleveland</name>
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<wicri:noCountry code="subField">FL; and</wicri:noCountry>
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<author><name sortKey="O Neill, Luke A" sort="O Neill, Luke A" uniqKey="O Neill L" first="Luke A" last="O'Neill">Luke A. O'Neill</name>
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<country xml:lang="fr">Irlande (pays)</country>
<wicri:regionArea>Trinity Biomedical Sciences Institute, School of Biochemistry and Immunology, Trinity College Dublin, Dublin</wicri:regionArea>
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</affiliation>
</author>
<author><name sortKey="Wei, Sheng" sort="Wei, Sheng" uniqKey="Wei S" first="Sheng" last="Wei">Sheng Wei</name>
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</affiliation>
</author>
<author><name sortKey="List, Alan F" sort="List, Alan F" uniqKey="List A" first="Alan F" last="List">Alan F. List</name>
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<wicri:noCountry code="no comma">Department of Malignant Hematology.</wicri:noCountry>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Calgranulin B (metabolism)</term>
<term>Cell Size</term>
<term>Colony-Forming Units Assay</term>
<term>Hematopoiesis</term>
<term>Hematopoietic Stem Cells (metabolism)</term>
<term>Hematopoietic Stem Cells (pathology)</term>
<term>Humans</term>
<term>Inflammasomes (metabolism)</term>
<term>Ion Channel Gating</term>
<term>Ion Channels (metabolism)</term>
<term>Mice, Transgenic</term>
<term>Mutation (genetics)</term>
<term>Myelodysplastic Syndromes (metabolism)</term>
<term>Myelodysplastic Syndromes (pathology)</term>
<term>NADPH Oxidase (metabolism)</term>
<term>NLR Family, Pyrin Domain-Containing 3 Protein (metabolism)</term>
<term>Phenotype</term>
<term>Pyroptosis</term>
<term>Reactive Oxygen Species (metabolism)</term>
<term>beta Catenin (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term>
<term>Calgranuline B (métabolisme)</term>
<term>Canaux ioniques (métabolisme)</term>
<term>Cellules souches hématopoïétiques (anatomopathologie)</term>
<term>Cellules souches hématopoïétiques (métabolisme)</term>
<term>Espèces réactives de l'oxygène (métabolisme)</term>
<term>Humains</term>
<term>Hématopoïèse</term>
<term>Inflammasomes (métabolisme)</term>
<term>Mutation (génétique)</term>
<term>NADPH oxidase (métabolisme)</term>
<term>Ouverture et fermeture des portes des canaux ioniques</term>
<term>Phénotype</term>
<term>Protéine-3 de la famille des NLR contenant un domaine pyrine (métabolisme)</term>
<term>Pyroptose</term>
<term>Souris transgéniques</term>
<term>Syndromes myélodysplasiques (anatomopathologie)</term>
<term>Syndromes myélodysplasiques (métabolisme)</term>
<term>Taille de la cellule</term>
<term>Test clonogénique</term>
<term>bêta-Caténine (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calgranulin B</term>
<term>Inflammasomes</term>
<term>Ion Channels</term>
<term>NADPH Oxidase</term>
<term>NLR Family, Pyrin Domain-Containing 3 Protein</term>
<term>Reactive Oxygen Species</term>
<term>beta Catenin</term>
</keywords>
<keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Cellules souches hématopoïétiques</term>
<term>Syndromes myélodysplasiques</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Mutation</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Hematopoietic Stem Cells</term>
<term>Myelodysplastic Syndromes</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Calgranuline B</term>
<term>Canaux ioniques</term>
<term>Cellules souches hématopoïétiques</term>
<term>Espèces réactives de l'oxygène</term>
<term>Inflammasomes</term>
<term>NADPH oxidase</term>
<term>Protéine-3 de la famille des NLR contenant un domaine pyrine</term>
<term>Syndromes myélodysplasiques</term>
<term>bêta-Caténine</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Hematopoietic Stem Cells</term>
<term>Myelodysplastic Syndromes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Size</term>
<term>Colony-Forming Units Assay</term>
<term>Hematopoiesis</term>
<term>Humans</term>
<term>Ion Channel Gating</term>
<term>Mice, Transgenic</term>
<term>Phenotype</term>
<term>Pyroptosis</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Humains</term>
<term>Hématopoïèse</term>
<term>Ouverture et fermeture des portes des canaux ioniques</term>
<term>Phénotype</term>
<term>Pyroptose</term>
<term>Souris transgéniques</term>
<term>Taille de la cellule</term>
<term>Test clonogénique</term>
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<front><div type="abstract" xml:lang="en">Despite genetic heterogeneity, myelodysplastic syndromes (MDSs) share features of cytological dysplasia and ineffective hematopoiesis. We report that a hallmark of MDSs is activation of the NLRP3 inflammasome, which drives clonal expansion and pyroptotic cell death. Independent of genotype, MDS hematopoietic stem and progenitor cells (HSPCs) overexpress inflammasome proteins and manifest activated NLRP3 complexes that direct activation of caspase-1, generation of interleukin-1β (IL-1β) and IL-18, and pyroptotic cell death. Mechanistically, pyroptosis is triggered by the alarmin S100A9 that is found in excess in MDS HSPCs and bone marrow plasma. Further, like somatic gene mutations, S100A9-induced signaling activates NADPH oxidase (NOX), increasing levels of reactive oxygen species (ROS) that initiate cation influx, cell swelling, and β-catenin activation. Notably, knockdown of NLRP3 or caspase-1, neutralization of S100A9, and pharmacologic inhibition of NLRP3 or NOX suppress pyroptosis, ROS generation, and nuclear β-catenin in MDSs and are sufficient to restore effective hematopoiesis. Thus, alarmins and founder gene mutations in MDSs license a common redox-sensitive inflammasome circuit, which suggests new avenues for therapeutic intervention.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27737891</PMID>
<DateCreated><Year>2016</Year>
<Month>10</Month>
<Day>14</Day>
</DateCreated>
<DateCompleted><Year>2017</Year>
<Month>07</Month>
<Day>31</Day>
</DateCompleted>
<DateRevised><Year>2017</Year>
<Month>11</Month>
<Day>16</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1528-0020</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>128</Volume>
<Issue>25</Issue>
<PubDate><Year>2016</Year>
<Month>Dec</Month>
<Day>22</Day>
</PubDate>
</JournalIssue>
<Title>Blood</Title>
<ISOAbbreviation>Blood</ISOAbbreviation>
</Journal>
<ArticleTitle>The NLRP3 inflammasome functions as a driver of the myelodysplastic syndrome phenotype.</ArticleTitle>
<Pagination><MedlinePgn>2960-2975</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1182/blood-2016-07-730556</ELocationID>
<Abstract><AbstractText>Despite genetic heterogeneity, myelodysplastic syndromes (MDSs) share features of cytological dysplasia and ineffective hematopoiesis. We report that a hallmark of MDSs is activation of the NLRP3 inflammasome, which drives clonal expansion and pyroptotic cell death. Independent of genotype, MDS hematopoietic stem and progenitor cells (HSPCs) overexpress inflammasome proteins and manifest activated NLRP3 complexes that direct activation of caspase-1, generation of interleukin-1β (IL-1β) and IL-18, and pyroptotic cell death. Mechanistically, pyroptosis is triggered by the alarmin S100A9 that is found in excess in MDS HSPCs and bone marrow plasma. Further, like somatic gene mutations, S100A9-induced signaling activates NADPH oxidase (NOX), increasing levels of reactive oxygen species (ROS) that initiate cation influx, cell swelling, and β-catenin activation. Notably, knockdown of NLRP3 or caspase-1, neutralization of S100A9, and pharmacologic inhibition of NLRP3 or NOX suppress pyroptosis, ROS generation, and nuclear β-catenin in MDSs and are sufficient to restore effective hematopoiesis. Thus, alarmins and founder gene mutations in MDSs license a common redox-sensitive inflammasome circuit, which suggests new avenues for therapeutic intervention.</AbstractText>
<CopyrightInformation>© 2016 by The American Society of Hematology.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Basiorka</LastName>
<ForeName>Ashley A</ForeName>
<Initials>AA</Initials>
<AffiliationInfo><Affiliation>Cancer Biology Ph.D. Program, Department of Malignant Hematology.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>McGraw</LastName>
<ForeName>Kathy L</ForeName>
<Initials>KL</Initials>
<AffiliationInfo><Affiliation>Department of Malignant Hematology.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Eksioglu</LastName>
<ForeName>Erika A</ForeName>
<Initials>EA</Initials>
<AffiliationInfo><Affiliation>Department of Immunology.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Xianghong</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>Department of Immunology.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Johnson</LastName>
<ForeName>Joseph</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Analytic Microscopy Core Facility, and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Ling</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Department of Hematopathology, H. Lee Moffitt Cancer Center, Tampa, FL.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Qing</ForeName>
<Initials>Q</Initials>
<AffiliationInfo><Affiliation>Department of Malignant Hematology.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Irvine</LastName>
<ForeName>Brittany A</ForeName>
<Initials>BA</Initials>
<AffiliationInfo><Affiliation>Department of Malignant Hematology.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cluzeau</LastName>
<ForeName>Thomas</ForeName>
<Initials>T</Initials>
<AffiliationInfo><Affiliation>Department of Hematology, Centre Hospitalier Universitaire de Nice, Nice, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Faculty of Medicine, University Nice Sophia Antipolis, Nice, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>INSERM U1065, Mediterranean Center of Molecular Medicine, Nice, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>French Group of Myelodysplasia, Paris, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sallman</LastName>
<ForeName>David A</ForeName>
<Initials>DA</Initials>
<AffiliationInfo><Affiliation>Department of Malignant Hematology.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Padron</LastName>
<ForeName>Eric</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>Department of Malignant Hematology.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Komrokji</LastName>
<ForeName>Rami</ForeName>
<Initials>R</Initials>
<AffiliationInfo><Affiliation>Department of Malignant Hematology.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sokol</LastName>
<ForeName>Lubomir</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Department of Malignant Hematology.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Coll</LastName>
<ForeName>Rebecca C</ForeName>
<Initials>RC</Initials>
<AffiliationInfo><Affiliation>Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Robertson</LastName>
<ForeName>Avril A B</ForeName>
<Initials>AA</Initials>
<AffiliationInfo><Affiliation>Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cooper</LastName>
<ForeName>Matthew A</ForeName>
<Initials>MA</Initials>
<AffiliationInfo><Affiliation>Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cleveland</LastName>
<ForeName>John L</ForeName>
<Initials>JL</Initials>
<AffiliationInfo><Affiliation>Department of Tumor Biology, H. Lee Moffitt Cancer Center, Tampa, FL; and.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>O'Neill</LastName>
<ForeName>Luke A</ForeName>
<Initials>LA</Initials>
<AffiliationInfo><Affiliation>Trinity Biomedical Sciences Institute, School of Biochemistry and Immunology, Trinity College Dublin, Dublin, Ireland.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wei</LastName>
<ForeName>Sheng</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Immunology.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>List</LastName>
<ForeName>Alan F</ForeName>
<Initials>AF</Initials>
<AffiliationInfo><Affiliation>Department of Malignant Hematology.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>K01 CA187020</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>P30 CA076292</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>T32 CA115308</GrantID>
<Acronym>CA</Acronym>
<Agency>NCI NIH HHS</Agency>
<Country>United States</Country>
</Grant>
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<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2016</Year>
<Month>10</Month>
<Day>13</Day>
</ArticleDate>
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<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Blood</MedlineTA>
<NlmUniqueID>7603509</NlmUniqueID>
<ISSNLinking>0006-4971</ISSNLinking>
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<NameOfSubstance UI="D040502">Calgranulin B</NameOfSubstance>
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<CitationSubset>IM</CitationSubset>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D040502" MajorTopicYN="N">Calgranulin B</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D048429" MajorTopicYN="N">Cell Size</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003114" MajorTopicYN="N">Colony-Forming Units Assay</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006410" MajorTopicYN="N">Hematopoiesis</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006412" MajorTopicYN="N">Hematopoietic Stem Cells</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D058847" MajorTopicYN="N">Inflammasomes</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015640" MajorTopicYN="N">Ion Channel Gating</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007473" MajorTopicYN="N">Ion Channels</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
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<MeshHeading><DescriptorName UI="D008822" MajorTopicYN="N">Mice, Transgenic</DescriptorName>
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<MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
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<MeshHeading><DescriptorName UI="D009190" MajorTopicYN="N">Myelodysplastic Syndromes</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
<QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019255" MajorTopicYN="N">NADPH Oxidase</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000071199" MajorTopicYN="N">NLR Family, Pyrin Domain-Containing 3 Protein</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000069292" MajorTopicYN="N">Pyroptosis</DescriptorName>
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<MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051176" MajorTopicYN="N">beta Catenin</DescriptorName>
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<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year>
<Month>07</Month>
<Day>28</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2016</Year>
<Month>10</Month>
<Day>03</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pmc-release"><Year>2017</Year>
<Month>12</Month>
<Day>22</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2016</Year>
<Month>10</Month>
<Day>16</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2017</Year>
<Month>8</Month>
<Day>2</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2016</Year>
<Month>10</Month>
<Day>15</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">27737891</ArticleId>
<ArticleId IdType="pii">blood-2016-07-730556</ArticleId>
<ArticleId IdType="doi">10.1182/blood-2016-07-730556</ArticleId>
<ArticleId IdType="pmc">PMC5179338</ArticleId>
</ArticleIdList>
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</pubmed>
<affiliations><list><country><li>Australie</li>
<li>France</li>
<li>Irlande (pays)</li>
<li>États-Unis</li>
</country>
<region><li>Floride</li>
<li>Provence-Alpes-Côte d'Azur</li>
</region>
<settlement><li>Nice</li>
</settlement>
</list>
<tree><noCountry><name sortKey="Basiorka, Ashley A" sort="Basiorka, Ashley A" uniqKey="Basiorka A" first="Ashley A" last="Basiorka">Ashley A. Basiorka</name>
<name sortKey="Chen, Xianghong" sort="Chen, Xianghong" uniqKey="Chen X" first="Xianghong" last="Chen">Xianghong Chen</name>
<name sortKey="Cleveland, John L" sort="Cleveland, John L" uniqKey="Cleveland J" first="John L" last="Cleveland">John L. Cleveland</name>
<name sortKey="Eksioglu, Erika A" sort="Eksioglu, Erika A" uniqKey="Eksioglu E" first="Erika A" last="Eksioglu">Erika A. Eksioglu</name>
<name sortKey="Irvine, Brittany A" sort="Irvine, Brittany A" uniqKey="Irvine B" first="Brittany A" last="Irvine">Brittany A. Irvine</name>
<name sortKey="Johnson, Joseph" sort="Johnson, Joseph" uniqKey="Johnson J" first="Joseph" last="Johnson">Joseph Johnson</name>
<name sortKey="Komrokji, Rami" sort="Komrokji, Rami" uniqKey="Komrokji R" first="Rami" last="Komrokji">Rami Komrokji</name>
<name sortKey="List, Alan F" sort="List, Alan F" uniqKey="List A" first="Alan F" last="List">Alan F. List</name>
<name sortKey="Mcgraw, Kathy L" sort="Mcgraw, Kathy L" uniqKey="Mcgraw K" first="Kathy L" last="Mcgraw">Kathy L. Mcgraw</name>
<name sortKey="Padron, Eric" sort="Padron, Eric" uniqKey="Padron E" first="Eric" last="Padron">Eric Padron</name>
<name sortKey="Sallman, David A" sort="Sallman, David A" uniqKey="Sallman D" first="David A" last="Sallman">David A. Sallman</name>
<name sortKey="Sokol, Lubomir" sort="Sokol, Lubomir" uniqKey="Sokol L" first="Lubomir" last="Sokol">Lubomir Sokol</name>
<name sortKey="Wei, Sheng" sort="Wei, Sheng" uniqKey="Wei S" first="Sheng" last="Wei">Sheng Wei</name>
<name sortKey="Zhang, Qing" sort="Zhang, Qing" uniqKey="Zhang Q" first="Qing" last="Zhang">Qing Zhang</name>
</noCountry>
<country name="États-Unis"><region name="Floride"><name sortKey="Zhang, Ling" sort="Zhang, Ling" uniqKey="Zhang L" first="Ling" last="Zhang">Ling Zhang</name>
</region>
</country>
<country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Cluzeau, Thomas" sort="Cluzeau, Thomas" uniqKey="Cluzeau T" first="Thomas" last="Cluzeau">Thomas Cluzeau</name>
</region>
</country>
<country name="Australie"><noRegion><name sortKey="Coll, Rebecca C" sort="Coll, Rebecca C" uniqKey="Coll R" first="Rebecca C" last="Coll">Rebecca C. Coll</name>
</noRegion>
<name sortKey="Cooper, Matthew A" sort="Cooper, Matthew A" uniqKey="Cooper M" first="Matthew A" last="Cooper">Matthew A. Cooper</name>
<name sortKey="Robertson, Avril A B" sort="Robertson, Avril A B" uniqKey="Robertson A" first="Avril A B" last="Robertson">Avril A B. Robertson</name>
</country>
<country name="Irlande (pays)"><noRegion><name sortKey="O Neill, Luke A" sort="O Neill, Luke A" uniqKey="O Neill L" first="Luke A" last="O'Neill">Luke A. O'Neill</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

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   |clé=     pubmed:27737891
   |texte=   The NLRP3 inflammasome functions as a driver of the myelodysplastic syndrome phenotype.
}}

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	Serveur d'exploration sur les relations entre la France et l'Australie
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The NLRP3 inflammasome functions as a driver of the myelodysplastic syndrome phenotype.

The NLRP3 inflammasome functions as a driver of the myelodysplastic syndrome phenotype.

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Abstract

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