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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1. Richarme, G., Mihoub, M., Dairou, J., et al. Parkinsonism-associated protein DJ-1/Park7 is a major protein deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine, and lysine residues. The Journal of Biological Chemisty 290(3), 1885-1897 (2015).

2. Richarme, G., Liu, C., Mihoub, M., et al. Guanine glycation repair by DJ-1/Park7 and its bacterial homologs. Science 357(6347), 208-211 (2017).

3. Clements, C.M., McNally, R.S., Conti, B.J., et al. DJ-1, a cancer- and Parkinson’s disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc. Natl. Acad. Sci. USA 103(41), 15091-15096 (2006).

4. Lee, J.Y., Song, J., Kwon, K., et al. Human DJ-1 and its homologs are novel glyoxalases. Hum. Mol. Genet. 21(14), 3215-3225 (2012).

5. Shendelman, S., Jonason, A., Martinat, C., et al. DJ-1 is a redox-dependent molecular chaperone that inhibits α-synuclein aggregate formation. PLoS Biol. 2(11), e362 (2004).

6. Xiong, H., Wang, D., Chen, L., et al. Parkin, PINK1, and DJ-1 form a ubiquitin E₃ ligase complex promoting unfolded protein degradation. J. Clin. Invest. 119(3), 650-660 (2009).

7. Bonifati, V., Rizzu, P., van Baren, M.J., et al. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299(5604), 256-259 (2003).