Cysteine Oxidation Targets Peroxiredoxins 1 and 2 for Exosomal Release through a Novel Mechanism of Redox-Dependent Secretion

Close teamwork between Nrf2 and peroxiredoxins 1 and 6 for the regulation of prostaglandin D2 and E2 production in macrophages in acute inflammation

“…Their findings suggest the existence of a protein export system that specifically recognizes glutathionylated proteins including Prx2. The authors recently characterized the role of exosomes for the release of Prx1 and Prx2 [28]. Treatment of HEK cells and monocytic cells with either LPS or TNF-α enhanced secretion of disulphide-linked homodimers of Prx1 and Prx2 [28] (Figs.…”

“…The mechanisms and roles of Prx1 and Prx2 secretion from cells through exosomes should be underscored [28]. Exosomes are small vesicle generated in the endosomal structure and released from various cells.…”

“…The glutathionylation at Cys83 stabilizes the dimer structure [42]. Prx1 and also Prx2 can be secreted from cells associated with exosomes [28,45]. (B) Interaction of Prx1 with TLR4 requires serum components.…”

“…PPAR-γ directly interacts with NF-κB and inhibits its DNA binding [9][10][11][12][13]. their S-glutathionylated dimer forms associated with exosomes [28,45]. [99,100].…”

“…Prx1 is also detected in mouse body fluids, and the secretion of Prx1 from cultured cells was enhanced following the treatment with cytokines such as TGF-β, oncostatin M and IL1-β (reviewed in [27]). A recent study show Prx1 and Prx2 can be secreted from cells as disulphide homodimers in association with exosomes following stimulation by LPS or TNF-α [28]. A previous study demonstrated importance of Prx1 in the initiation of pulmonary inflammation following exposure to non-lethal levels of ozone [29].…”