Cyclo(dehydrohistidyl-L-tryptophyl) inhibits nitric oxide production by preventing the dimerization of inducible nitric oxide synthase

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dc.contributor.authorMi Jin Sohn-
dc.contributor.authorG M Hur-
dc.contributor.authorH S Byun-
dc.contributor.authorWon Gon Kim-
dc.date.accessioned2017-04-19T09:08:58Z-
dc.date.available2017-04-19T09:08:58Z-
dc.date.issued2008-
dc.identifier.issn0006-2952-
dc.identifier.uri10.1016/j.bcp.2007.10.021ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8281-
dc.description.abstractDimerization of inducible NOS has been known to be a potential therapeutic target for iNOS-mediated pathologies. Cyclic dipeptides are among the simplest peptides commonly found as by-products of food processing or metabolites of microorganisms. In this study, we found that cyclo(dehydrohistidyl-l-tryptophyl) (CDHT), a cyclic dipeptide from an unidentified fungal strain Fb956, prevents iNOS dimerization in activated microglial BV-2 cells. CDHT inhibited NO production with an IC50 of 6.5 μM in LPS-treated BV-2 cells. Western blot analysis and iNOS activity measurement of fractions from size-exclusion chromatography of cell lysates indicated that CDHT inhibits dimerization of iNOS, while it has no effect on iNOS expression or enzyme activity. The CDHT inhibition of iNOS dimerization was confirmed by partially denaturing SDS-PAGE analysis. In contrast, CDHT did not affect cGMP production in endothelial HUVEC cells, which indicates no inhibition of endothelial NOS activity. These results reveal that CDHT, one of the simplest and cyclic dipeptides, selectively inhibits NO production by inhibiting iNOS dimerization, and could be a useful therapeutic agent for inflammation-mediated diseases.-
dc.publisherElsevier-
dc.titleCyclo(dehydrohistidyl-L-tryptophyl) inhibits nitric oxide production by preventing the dimerization of inducible nitric oxide synthase-
dc.title.alternativeCyclo(dehydrohistidyl-l-tryptophyl) inhibits nitric oxide production by preventing the dimerization of inducible nitric oxide synthase-
dc.typeArticle-
dc.citation.titleBiochemical Pharmacology-
dc.citation.number4-
dc.citation.endPage930-
dc.citation.startPage923-
dc.citation.volume75-
dc.contributor.affiliatedAuthorMi Jin Sohn-
dc.contributor.affiliatedAuthorWon Gon Kim-
dc.contributor.alternativeName손미진-
dc.contributor.alternativeName허강민-
dc.contributor.alternativeName변희선-
dc.contributor.alternativeName김원곤-
dc.identifier.bibliographicCitationBiochemical Pharmacology, vol. 75, no. 4, pp. 923-930-
dc.identifier.doi10.1016/j.bcp.2007.10.021-
dc.subject.keywordBV-2 microglia-
dc.subject.keywordCyclo(dehydrohistidyl-l-tryptophyl)-
dc.subject.keywordDimerization-
dc.subject.keywordiNOS-
dc.subject.keywordLPS-
dc.subject.keywordNitric oxide-
dc.subject.localBV-2 microglia-
dc.subject.localCyclo(dehydrohistidyl-l-tryptophyl)-
dc.subject.localcyclo(dehydrohistidyl-L-tryptophyl)-
dc.subject.localDimerization-
dc.subject.localInducible nitric oxide synthase (iNOS)-
dc.subject.localInducible nitric oxide synthase-
dc.subject.localinducible nnitric oxide synthase-
dc.subject.localiNOS-
dc.subject.localInducible nitric oxide synthease (iNOS)-
dc.subject.localINOS-
dc.subject.localinducible nitric oxide synthase-
dc.subject.localLPS-
dc.subject.localNO-
dc.subject.localnitric oxide-
dc.subject.localnitric oxide (NO)-
dc.subject.localNitric oxide-
dc.subject.localNO (Nitric oxide)-
dc.subject.localnitric oxide.-
dc.subject.localNitric oxid-
dc.subject.localNitric oxide (NO)-
dc.description.journalClassY-
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Division of Research on National Challenges > Infectious Disease Research Center > 1. Journal Articles
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