Inositol polyphosphates promote T cell-independent humoral immunity via the regulation of Bruton's tyrosine kinase

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dc.contributor.authorKim, Wooseobko
dc.contributor.authorKim, Eunhako
dc.contributor.authorMin, Hyungyuko
dc.contributor.authorKim, Min Gyuko
dc.contributor.authorEisenbeis, Verena B.ko
dc.contributor.authorDutta, Amit K.ko
dc.contributor.authorPavlovic, Igorko
dc.contributor.authorJessen, Henning J.ko
dc.contributor.authorKim, Seyunko
dc.contributor.authorSeong, Rho Hyunko
dc.date.accessioned2019-07-18T05:31:40Z-
dc.date.available2019-07-18T05:31:40Z-
dc.date.created2019-07-15-
dc.date.issued2019-06-
dc.identifier.citationPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v.116, no.26, pp.12952 - 12957-
dc.identifier.issn0027-8424-
dc.identifier.urihttp://hdl.handle.net/10203/263303-
dc.description.abstractT cell-independent (TI) B cell response is critical for the early protection against pathogen invasion. The regulation and activation of Bruton's tyrosine kinase (Btk) is known as a pivotal step of B cell antigen receptor (BCR) signaling in TI humoral immunity, as observed in patients with X-linked agammaglobulinemia (XLA) experiencing a high incidence of encapsulated bacterial infections. However, key questions remain as towhether a well-established canonical BCR signaling pathway is sufficient to regulate the activity of Btk. Here, we find that inositol hexakisphosphate (InsP6) acts as a physiological regulator of Btk in BCR signaling. Absence of higher order inositol phosphates (InsPs), inositol polyphosphates, leads to an inability to mount immune response against TI antigens. Interestingly, the significance of InsP6-mediated Btk regulation ismore prominent in IgM(+) plasma cells. Hence, the present study identifies higher order InsPs as principal components of B cell activation upon TI antigen stimulation and presents a mechanism for InsP-mediated regulation of the BCR signaling.-
dc.languageEnglish-
dc.publisherNATL ACAD SCIENCES-
dc.titleInositol polyphosphates promote T cell-independent humoral immunity via the regulation of Bruton's tyrosine kinase-
dc.typeArticle-
dc.identifier.wosid000472719100065-
dc.identifier.scopusid2-s2.0-85068183344-
dc.type.rimsART-
dc.citation.volume116-
dc.citation.issue26-
dc.citation.beginningpage12952-
dc.citation.endingpage12957-
dc.citation.publicationnamePROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-
dc.identifier.doi10.1073/pnas.1821552116-
dc.contributor.localauthorKim, Seyun-
dc.contributor.nonIdAuthorKim, Wooseob-
dc.contributor.nonIdAuthorMin, Hyungyu-
dc.contributor.nonIdAuthorEisenbeis, Verena B.-
dc.contributor.nonIdAuthorDutta, Amit K.-
dc.contributor.nonIdAuthorPavlovic, Igor-
dc.contributor.nonIdAuthorJessen, Henning J.-
dc.contributor.nonIdAuthorSeong, Rho Hyun-
dc.description.isOpenAccessN-
dc.type.journalArticleArticle-
dc.subject.keywordAuthorT cell-independent immune response-
dc.subject.keywordAuthorB cell antigen receptor-
dc.subject.keywordAuthorBruton&apos-
dc.subject.keywordAuthors tyrosine kinase-
dc.subject.keywordAuthorinositol phosphate-
dc.subject.keywordAuthorinositol polyphosphate multikinase-
dc.subject.keywordPlusX-LINKED AGAMMAGLOBULINEMIA-
dc.subject.keywordPlusPLECKSTRIN HOMOLOGY DOMAIN-
dc.subject.keywordPlusB-CELL-
dc.subject.keywordPlusANTIGEN RECEPTOR-
dc.subject.keywordPlusMARGINAL ZONE-
dc.subject.keywordPlusLYMPHOCYTES-
dc.subject.keywordPlusCALCIUM-
dc.subject.keywordPlusACTIVATION-
dc.subject.keywordPlus1,3,4,5-TETRAKISPHOSPHATE-
dc.subject.keywordPlusPENTAKISPHOSPHATE-
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