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Kwon, Hyug Moo
Immunometabolism and Cancer Lab.
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dc.citation.endPage 28105 -
dc.citation.number 42 -
dc.citation.startPage 28095 -
dc.citation.title JOURNAL OF BIOLOGICAL CHEMISTRY -
dc.citation.volume 283 -
dc.contributor.author Hasler, Udo -
dc.contributor.author Leroy, Valeeie -
dc.contributor.author Jeon, Un Sil -
dc.contributor.author Bouley, Richard -
dc.contributor.author Dimitrov, Mitko -
dc.contributor.author Kim, Jeong Ah -
dc.contributor.author Brown, Dennis -
dc.contributor.author Kwon, H. Moo -
dc.contributor.author Martin, Pierre-Yves -
dc.contributor.author Feraille, Eric -
dc.date.accessioned 2023-12-22T08:36:40Z -
dc.date.available 2023-12-22T08:36:40Z -
dc.date.created 2014-06-02 -
dc.date.issued 2008-10 -
dc.description.abstract Renal tubulo-interstitial inflammation is frequently associated with polyuria and urine concentration defects. This led us to investigate the effects of the major pro-inflammatory nuclear factor kappa B (NF-kappa B) pathway on aquaporin 2 (AQP2) expression by the collecting duct. Using immortalized collecting duct principal cells (mpkCCD(c14)), we found that, acting independently of vasopressin, activation of NF-kappa B by lipopolysaccharide (LPS) decreased AQP2 mRNA and protein levels in a time-and dose-dependent manner but did not decrease AQP2 mRNA stability. Consistently, constitutively active I kappa B kinase beta decreased AQP2 expression. The LPS-induced decrease in AQP2 mRNA levels was confirmed in rat kidney slices and was reproduced both under conditions of elevated cAMP concentration and V-2 receptor antagonism. Computer analysis of the AQP2 promoter revealed two putative kappa B elements. Mutation of either kappa B element abolished the LPS-induced decrease of luciferase activity in cells expressing AQP2 promoter-luciferase plasmid constructs. Chromatin immunoprecipitation revealed that LPS challenge decreased p65, increased p50 and p52, and had no effect on RelB and c-Rel binding to kappa B elements of the AQP2 promoter. RNA-mediated interference silencing of p65, p50, and p52 confirmed controlled AQP2 transcription by these NF-kappa B subunits. We additionally found that hypertonicity activated NF-kappa B in mpkCCD(c14) cells, an effect that may counteract the Tonicity-responsive enhancer binding protein (TonEBP)-dependent increase in AQP2 gene transcription. Taken together, these findings indicate that NF-kappa B is an important physiological regulator of AQP2 transcription. -
dc.identifier.bibliographicCitation JOURNAL OF BIOLOGICAL CHEMISTRY, v.283, no.42, pp.28095 - 28105 -
dc.identifier.doi 10.1074/jbc.M708350200 -
dc.identifier.issn 0021-9258 -
dc.identifier.scopusid 2-s2.0-57649136392 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/4847 -
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=57649136392 -
dc.identifier.wosid 000259969300012 -
dc.language 영어 -
dc.publisher AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC -
dc.title NF-kappa B modulates aquaporin-2 transcription in renal collecting duct principal cells -
dc.type Article -
dc.description.journalRegisteredClass scopus -
dc.subject.keywordPlus INDUCED NEPHROTIC SYNDROME -
dc.subject.keywordPlus ENHANCER-BINDING PROTEIN -
dc.subject.keywordPlus WATER CHANNEL EXPRESSION -
dc.subject.keywordPlus DOWN-REGULATION -
dc.subject.keywordPlus NULL MICE -
dc.subject.keywordPlus ACTIVATION -
dc.subject.keywordPlus MECHANISM -
dc.subject.keywordPlus GENE -
dc.subject.keywordPlus HYPERTONICITY -
dc.subject.keywordPlus PERMEABILITY -

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