DJ-1/PARK7 (human, recombinant)

DJ-1/Parkinson disease protein 7 (PARK7) is a dimeric protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues in oxidatively damaged proteins.¹ It acts on early glycation intermediates (hemithioacetals and aminocarbinols) to prevent the formation of irreversibly damaged advanced glycation end products (AGEs). PARK7 also repairs methylglyoxal- and glyoxal-glycated dGTP, GTP, GDP, GMP, RNA, and DNA.² Knockdown of PARK7 in vitro increases glycated DNA, DNA strand breaks, and phosphorylated p53 levels but decreases mRNA expression of the antioxidant-related enzyme NAD(P)H:quinone acceptor oxidoreductase 1 (NQO1) and destabilizes the nuclear factor erythroid 2-related factor (Nrf2), a master regulator of antioxidant transcriptional responses.³ . PARK7 is also a glyoxalase that converts glyoxal and methylglyoxal to glycolic and lactic acid, respectively, in the absence of glutathione.⁴ It acts as a redox-sensitive molecular chaperone and inhibits aggregation of α-synuclein in cell-free assays and in murine neuroblastoma cells.⁵ PARK7 forms a complex with the E3 ubiquitin ligase Parkin and PTEN-induced putative kinase 1 (PINK1) that promotes ubiquitination and degradation of Parkin substrates, including Parkin itself and Synphilin-1 in neuroblastoma SH-SY5Y cells and human brain lysates.⁶ Mutations to PARK7 have been linked to autosomal recessive, early-onset Parkinson’s disease.⁷

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