Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-9517
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dc.contributor.authorMüller-Calleja, Nadine-
dc.contributor.authorHollerbach, Anne-
dc.contributor.authorCanisius, Antje-
dc.contributor.authorOrning, Carolin-
dc.contributor.authorStrand, Susanne-
dc.contributor.authorLackner, Karl J.-
dc.date.accessioned2023-09-11T10:20:54Z-
dc.date.available2023-09-11T10:20:54Z-
dc.date.issued2023-
dc.identifier.urihttps://openscience.ub.uni-mainz.de/handle/20.500.12030/9535-
dc.description.abstractEndosomal toll-like receptors (TLRs) must be translocated from the endoplasmic reticulum (ER) to the endosome and proteolytically cleaved within the endosome before they can induce cellular signals. As ligands for these TLRs are also liberated from apoptotic or necrotic cells, this process is controlled by several mechanisms which shall ensure that there is no inadvertent activation. We have shown previously that antiphospholipid antibodies induce endosomal NADPH-oxidase (NOX) followed by the translocation of TLR7/8 to the endosome. We show now that endosomal NOX is required for the rapid translocation of TLR3, TLR7/8, and TLR9. Deficiency of gp91phox, the catalytic subunit of NOX2, or inhibition of endosomal NOX by the chloride channel blocker niflumic acid both prevent immediate (i.e., within 30 min) translocation of these TLRs as shown by confocal laser scanning microscopy. Under these conditions, the induction of mRNA synthesis for TNF-α and secretion of TNF-α is delayed by approx. 6–9 h. However, maximal expression of TNF-α mRNA or secretion of TNF-α is not significantly reduced. In conclusion, these data add NOX2 as another component involved in the orchestration of cellular responses to ligands of endosomal TLRs.en_GB
dc.language.isoengde
dc.rightsCC BY-NC-ND*
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subject.ddc610 Medizinde_DE
dc.subject.ddc610 Medical sciencesen_GB
dc.titleRapid translocation of intracellular toll-like receptors depends on endosomal NADPH oxidaseen_GB
dc.typeZeitschriftenaufsatzde
dc.identifier.doihttp://doi.org/10.25358/openscience-9517-
jgu.type.dinitypearticleen_GB
jgu.type.versionPublished versionde
jgu.type.resourceTextde
jgu.organisation.departmentFB 04 Medizinde
jgu.organisation.number2700-
jgu.organisation.nameJohannes Gutenberg-Universität Mainz-
jgu.rights.accessrightsopenAccess-
jgu.journal.titleEuropean journal of immunologyde
jgu.journal.volume53de
jgu.journal.issue9de
jgu.pages.alternative2250271de
jgu.publisher.year2023-
jgu.publisher.nameWiley-VCHde
jgu.publisher.placeWeinheimde
jgu.publisher.issn1521-4141de
jgu.organisation.placeMainz-
jgu.subject.ddccode610de
jgu.publisher.doi10.1002/eji.202250271de
jgu.organisation.rorhttps://ror.org/023b0x485-
Appears in collections:DFG-491381577-H

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