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Rise and fall of Kir2.2 current by TLR4 signaling in human monocytes: PKC-dependent trafficking and PI3K-mediated PIP2 decrease

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dc.contributor.authorKim, Kyung Soo-
dc.contributor.authorJang, Ji Hyun-
dc.contributor.authorLin, Haiyue-
dc.contributor.authorChoi, Seong Woo-
dc.contributor.authorKim, Hang Rae-
dc.contributor.authorShin, Dong Hoon-
dc.contributor.authorNam, Joo Hyun-
dc.contributor.authorZhang, Yin Hua-
dc.contributor.authorKim, Sung Joon-
dc.date.accessioned2024-05-16T01:31:31Z-
dc.date.available2024-05-16T01:31:31Z-
dc.date.created2018-11-05-
dc.date.created2018-11-05-
dc.date.issued2015-10-
dc.identifier.citationJournal of Immunology, Vol.195 No.7, pp.3345-3354-
dc.identifier.issn0022-1767-
dc.identifier.urihttps://hdl.handle.net/10371/202623-
dc.description.abstractLPSs are widely used to stimulate TLR4, but their effects on ion channels in immune cells are poorly known. In THP-1 cells and human blood monocytes treated with LPS, inwardly rectifying K+ channel current (I-Kir,I-LPS) newly emerged at 1 h, peaked at 4 h (-119 +/- 8.6 pA/pF), and decayed afterward (-32 +/- 6.7 pA/pF at 24 h). Whereas both the Kir2.1 and Kir2.2 mRNAs and proteins were observed, single-channel conductance (38 pS) of I-Kir,(LPS) and small interfering RNA-induced knockdown commonly indicated Kir2.2 than Kir2.1. LPS-induced cytokine release and store-operated Ca2+ entry were commonly decreased by ML-133, a Kir2 inhibitor. Immunoblot, confocal microscopy, and the effects of vesicular trafficking inhibitors commonly suggested plasma membrane translocation of Kir2.2 by LPS. Both I-Kir,I-LPS and membrane translocation of Kir2.2 were inhibited by GF109203X (protein kinase C [PKC] inhibitor) or by transfection with small interfering RNA-specific PKC epsilon. Interestingly, pharmacological activation of PKC by PMA induced both Kir2.1 and Kir2.2 currents. The spontaneously decayed I-Kir,I-LPS at 24 h was recovered by PI3K inhibitors but further suppressed by an inhibitor of phosphatidylinositol(3,4,5)-trisphosphate (PIP3) phosphatase (phosphatase and tensin homolog). However, I-Kir,I-LPS at 24 h was not affected by Akt inhibitors, suggesting that the decreased phosphatidylinositol(4,5)-bisphosphate availability, that is, conversion into PIP3 by PI3K, per se accounts for the decay of I-Kir,I-LPS. Taken together, to our knowledge these data are the first demonstrations that I-Kir is newly induced by TLR4 stimulation via PKC-dependent membrane trafficking of Kir2.2, and that conversion of phosphatidylinositol(4,5)-bisphosphate to PIP3 modulates Kir2.2. The augmentation of Ca2+ influx and cytokine release suggests a physiological role for Kir2.2 in TLR4-stimulated monocytes.-
dc.language영어-
dc.publisherAmerican Association of Immunologists-
dc.titleRise and fall of Kir2.2 current by TLR4 signaling in human monocytes: PKC-dependent trafficking and PI3K-mediated PIP2 decrease-
dc.typeArticle-
dc.identifier.doi10.4049/jimmunol.1500056-
dc.citation.journaltitleJournal of Immunology-
dc.identifier.wosid000361741200040-
dc.identifier.scopusid2-s2.0-84942474597-
dc.citation.endpage3354-
dc.citation.number7-
dc.citation.startpage3345-
dc.citation.volume195-
dc.description.isOpenAccessN-
dc.contributor.affiliatedAuthorKim, Hang Rae-
dc.contributor.affiliatedAuthorZhang, Yin Hua-
dc.contributor.affiliatedAuthorKim, Sung Joon-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.subject.keywordPlusPROTEIN-KINASE-C-
dc.subject.keywordPlusRECTIFYING POTASSIUM CHANNELS-
dc.subject.keywordPlusK+ CHANNELS-
dc.subject.keywordPlusTYROSINE KINASE-
dc.subject.keywordPlusCA2+ ENTRY-
dc.subject.keywordPlusACTIVATION-
dc.subject.keywordPlusCELLS-
dc.subject.keywordPlusDIFFERENTIATION-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordPlusEPSILON-
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