Cayman 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. 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. 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. . PARK7 is also a glyoxalase that converts glyoxal and methylglyoxal to glycolic and lactic acid, respectively, in the absence of glutathione. It acts as a redox-sensitive molecular chaperone and inhibits aggregation of α-synuclein in cell-free assays and in murine neuroblastoma cells. 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. Mutations to PARK7 have been linked to autosomal recessive, early-onset Parkinson’s disease.

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