Thioredoxin-interacting protein promotes phagosomal acidification upon exposure to Escherichia coli through inflammasome-mediated caspase-1 activation in macrophages

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dc.contributor.authorSung Jin Yoon-
dc.contributor.authorD H Jo-
dc.contributor.authorSeung-Ho Park-
dc.contributor.authorJun-Young Park-
dc.contributor.authorYoo Kyung Lee-
dc.contributor.authorMoo-Seung Lee-
dc.contributor.authorJeong Ki Min-
dc.contributor.authorHaiyoung Jung-
dc.contributor.authorTae-Don Kim-
dc.contributor.authorSuk Ran Yoon-
dc.contributor.authorS W Chung-
dc.contributor.authorJ H Kim-
dc.contributor.authorIn Pyo Choi-
dc.contributor.authorYoung-Jun Park-
dc.date.accessioned2020-02-07T16:30:39Z-
dc.date.available2020-02-07T16:30:39Z-
dc.date.issued2019-
dc.identifier.issn1664-3224-
dc.identifier.uri10.3389/fimmu.2019.02636ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/19173-
dc.description.abstractIn host defense, it is crucial to maintain the acidity of the macrophage phagosome for effective bacterial clearance. However, the mechanisms governing phagosomal acidification upon exposure to gram-negative bacteria have not been fully elucidated. In this study, we demonstrate that in macrophages exposed to Escherichia coli, the thioredoxin-interacting protein (TXNIP)-associated inflammasome plays a role in pH modulation through the activated caspase-1-mediated inhibition of NADPH oxidase. While there was no difference in early-phase bacterial engulfment between Txnip knockout (KO) macrophages and wild-type (WT) macrophages, Txnip KO macrophages were less efficient at destroying intracellular bacteria in the late phase, and their phagosomes failed to undergo appropriate acidification. These phenomena were associated with reactive oxygen species production and were reversed by treatment with an NADPH oxidase inhibitor or a caspase inhibitor. In line with these results, Txnip KO mice were more susceptible to both intraperitoneally administered E. coli and sepsis induced by cecum ligation and puncture than WT mice. Taken together, this study suggests that the TXNIP-associated inflammasome-caspase-1 axis regulates NADPH oxidase to modulate the pH of the phagosome, controlling bacterial clearance by macrophages.-
dc.publisherFrontiers Media Sa-
dc.titleThioredoxin-interacting protein promotes phagosomal acidification upon exposure to Escherichia coli through inflammasome-mediated caspase-1 activation in macrophages-
dc.title.alternativeThioredoxin-interacting protein promotes phagosomal acidification upon exposure to Escherichia coli through inflammasome-mediated caspase-1 activation in macrophages-
dc.typeArticle-
dc.citation.titleFrontiers in Immunology-
dc.citation.number0-
dc.citation.endPage2636-
dc.citation.startPage2636-
dc.citation.volume10-
dc.contributor.affiliatedAuthorSung Jin Yoon-
dc.contributor.affiliatedAuthorSeung-Ho Park-
dc.contributor.affiliatedAuthorJun-Young Park-
dc.contributor.affiliatedAuthorYoo Kyung Lee-
dc.contributor.affiliatedAuthorMoo-Seung Lee-
dc.contributor.affiliatedAuthorJeong Ki Min-
dc.contributor.affiliatedAuthorHaiyoung Jung-
dc.contributor.affiliatedAuthorTae-Don Kim-
dc.contributor.affiliatedAuthorSuk Ran Yoon-
dc.contributor.affiliatedAuthorIn Pyo Choi-
dc.contributor.affiliatedAuthorYoung-Jun Park-
dc.contributor.alternativeName윤성진-
dc.contributor.alternativeName조동현-
dc.contributor.alternativeName박승호-
dc.contributor.alternativeName박준영-
dc.contributor.alternativeName이유경-
dc.contributor.alternativeName이무승-
dc.contributor.alternativeName민정기-
dc.contributor.alternativeName정해용-
dc.contributor.alternativeName김태돈-
dc.contributor.alternativeName윤석란-
dc.contributor.alternativeName정수월-
dc.contributor.alternativeName김정훈-
dc.contributor.alternativeName최인표-
dc.contributor.alternativeName박영준-
dc.identifier.bibliographicCitationFrontiers in Immunology, vol. 10, pp. 2636-2636-
dc.identifier.doi10.3389/fimmu.2019.02636-
dc.subject.keywordEscherichia coli-
dc.subject.keywordcaspase-
dc.subject.keywordmacrophage-
dc.subject.keywordphagosome-
dc.subject.keywordthioredoxin-interacting protein-
dc.subject.localE. Coli-
dc.subject.localE. coli-
dc.subject.localE.coli-
dc.subject.localEscherichia Coli-
dc.subject.localEscherichia coli-
dc.subject.localEscherichia coli.-
dc.subject.localescherichia coil-
dc.subject.localescherichia coli-
dc.subject.localCaspase-
dc.subject.localCaspases-
dc.subject.localcaspase-
dc.subject.localmacrophage-
dc.subject.localmacrophages-
dc.subject.localMacrophage-
dc.subject.localMacrophages-
dc.subject.localphagosome-
dc.subject.localThioredoxin-interacting protein-
dc.subject.localthioredoxin-interacting protein-
dc.subject.localthioredoxin interacting protein-
dc.description.journalClassY-
Appears in Collections:
Division of Research on National Challenges > Environmental diseases research center > 1. Journal Articles
Division of Biomedical Research > Biotherapeutics Translational Research Center > 1. Journal Articles
Aging Convergence Research Center > 1. Journal Articles
Division of Biomedical Research > Immunotherapy Research Center > 1. Journal Articles
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