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나노의학 연구단
나노의학 연구단
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Peroxiredoxin-mediated disulfide bond formation is required for nucleocytoplasmic translocation and secretion of HMGB1 in response to inflammatory stimuli

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Title
Peroxiredoxin-mediated disulfide bond formation is required for nucleocytoplasmic translocation and secretion of HMGB1 in response to inflammatory stimuli
Author(s)
Man Sup Kwak; Hee Sue Kim; Khulan Lkhamsuren; Young Hun Kim; Myeong Gil Han; Jae Min Shin; In Ho Park; Woo Joong Rhee; Se Kyoung Lee; Sue Goo Rhee; Jeon-Soo Shin
Publication Date
2019-06
Journal
REDOX BIOLOGY, v.24, no., pp.UNSP101203 -
Publisher
ELSEVIER SCIENCE BV
Abstract
© 2019 The Authors The nuclear protein HMGB1 (high mobility group box 1) is secreted by monocytes-macrophages in response to inflammatory stimuli and serves as a danger-associated molecular pattern. Acetylation and phosphorylation of HMGB1 are implicated in the regulation of its nucleocytoplasmic translocation for secretion, although inflammatory stimuli are known to induce H 2 O 2 production. Here we show that H 2 O 2 -induced oxidation of HMGB1, which results in the formation of an intramolecular disulfide bond between Cys 23 and Cys 45 , is necessary and sufficient for its nucleocytoplasmic translocation and secretion. The oxidation is catalyzed by peroxiredoxin I (PrxI) and PrxII, which are first oxidized by H 2 O 2 and then transfer their disulfide oxidation state to HMGB1. The disulfide form of HMGB1 showed higher affinity for nuclear exportin CRM1 compared with the reduced form. Lipopolysaccharide (LPS)–induced HMGB1 secretion was greatly attenuated in macrophages derived from PrxI or PrxII knockout mice, as was the LPS-induced increase in serum HMGB1 levels
URI
https://pr.ibs.re.kr/handle/8788114/6228
ISSN
2213-2317
Appears in Collections:
Center for Nanomedicine (나노의학 연구단) > Journal Papers
Files in This Item:
201906_Peroxiredoxin-mediated disulfide bond formation is required for nucleocytoplasmic translocation_Jeon-Soo Shin.pdfDownload

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