Abstract：
: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 H2O2 production. Here we show that H2O2-induced oxidation of HMGB1, which results in the formation of an intramolecular disulfide bond between Cys23 and Cys45, 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 H2O2 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.
journal_name
Redox Bioljournal_title
Redox biologyauthors
Kwak MS,Kim HS,Lkhamsuren K,Kim YH,Han MG,Shin JM,Park IH,Rhee WJ,Lee SK,Rhee SG,Shin JSdoi
10.1016/j.redox.2019.101203subject
Has Abstractpub_date
2019-06-01 00:00:00pages
101203issn
2213-2317pii
S2213-2317(19)30257-5journal_volume
24pub_type
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