Figure 1.

Potential origin and regulation of peroxiredoxin 4. Peroxiredoxin 4 (Prx4) is known to switch between dimer and pentadimeric decamer structure [3], with potential decameric structure having been identified in circulation [11]. It has been shown that Prx4 redox-dependently binds to the cell surface of human umbilical vein endothelial cells [9]. Specific and non-specific stimulation of various tissues has influenced Prx4 expression, oxidation or oligomerization and may ultimately result in secretion of Prx4. H2O2: hydrogen peroxide; LPS: lipopolysaccharide; NaDOC: sodium deoxycholate; NF-κB: nuclear factor-kappa B; NO: nitric oxide; Prx4: peroxiredoxin 4; RNS: reactive nitrogen species; TRAIL: tumor necrosis factor-related apoptosis-inducing ligand.

Schulte BMC Medicine 2011 9:137   doi:10.1186/1741-7015-9-137
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