A new compound from Micromonospora sp. SA246, 9-hydroxycrisamicin-A, activates hepatitis B virus replication

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dc.contributor.authorSeok Won Yoon-
dc.contributor.authorIn Young Park-
dc.contributor.authorBo Hwa Sohn-
dc.contributor.authorJae Hyouk Lee-
dc.contributor.authorW H Yeo-
dc.contributor.authorYoung Ik Lee-
dc.date.accessioned2017-04-19T09:01:10Z-
dc.date.available2017-04-19T09:01:10Z-
dc.date.issued2004-
dc.identifier.issn0006-291X-
dc.identifier.uri10.1016/j.bbrc.2004.05.061ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/6522-
dc.description.abstractA new compound from Micromonospora sp. SA246, 9-hydroxycrisamicin-A (9-HCA-A), showed potential for activating hepatitis B virus (HBV) replication. To define the mechanism of 9-HCA-A, we used HepG2 2.2.15 cells which support HBV replication. 9-HCA-A activated HBV replication, increased episomal and integrated HBV DNA content, and increased secretions of HBV antigens (HBsAg and HBeAg) into culture medium. 9-HCA-A also activated HBV transcription in Hep2 2.2.15 cell line. To examine transcriptional control mechanisms, we analyzed the effect of 9-HCA-A on four different HBV promoters (Core, PreS1, PreS2, and X) in hepatoma cell line. 9-HCA-A responsive element was located at HBx promoter. By EMSA, we showed that 9-HCA-A activated the HBx promoter by detaching the 9-HCA-A responsive element binding protein (9H-REBP). Protein phosphatase (PP2A1) treatment detaches the 9H-REBP from the HBx promoter, similar to 9-HCA-A, while protein kinase A treatment does not detach the 9H-REBP from the HBx promoter. Our results showed that 9H- REBP functions as a repressor of HBV replication while 9-HCA-A activated protein phosphatase released the BP on the HBx promoter, thus activating HBV replication.-
dc.publisherElsevier-
dc.titleA new compound from Micromonospora sp. SA246, 9-hydroxycrisamicin-A, activates hepatitis B virus replication-
dc.title.alternativeA new compound from Micromonospora sp. SA246, 9-hydroxycrisamicin-A, activates hepatitis B virus replication-
dc.typeArticle-
dc.citation.titleBiochemical and Biophysical Research Communications-
dc.citation.number3-
dc.citation.endPage865-
dc.citation.startPage859-
dc.citation.volume319-
dc.contributor.affiliatedAuthorSeok Won Yoon-
dc.contributor.affiliatedAuthorIn Young Park-
dc.contributor.affiliatedAuthorBo Hwa Sohn-
dc.contributor.affiliatedAuthorJae Hyouk Lee-
dc.contributor.affiliatedAuthorYoung Ik Lee-
dc.contributor.alternativeName윤석원-
dc.contributor.alternativeName박인영-
dc.contributor.alternativeName손보화-
dc.contributor.alternativeName이재혁-
dc.contributor.alternativeName여운형-
dc.contributor.alternativeName이영익-
dc.identifier.bibliographicCitationBiochemical and Biophysical Research Communications, vol. 319, no. 3, pp. 859-865-
dc.identifier.doi10.1016/j.bbrc.2004.05.061-
dc.subject.keyword9-Hydroxycrisamicin-
dc.subject.keywordHBV-X-
dc.subject.keywordMicromonospora sp. SA246-
dc.subject.keywordPhosphorylation-
dc.subject.keywordProtein phosphatase-
dc.subject.keywordXPBP-
dc.subject.local9-Hydroxycrisamicin-
dc.subject.localHBV-X-
dc.subject.localMicromonospora sp. SA246-
dc.subject.localPhosphorylation-
dc.subject.localphosphorylation-
dc.subject.localProtein phosphatase-
dc.subject.localXPBP-
dc.description.journalClassY-
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