Parkinsonism associated deglycase (DJ-1) (PARK7)

Parkinsonism associated deglycase (DJ-1, encoded by the PARK7 gene) is a highly conserved, multifunctional protein of the peptidase C56 family, primarily recognized for its roles in cellular defense against oxidative stress, DNA repair, and maintenance of protein and metabolite integrity[1][2][4]. DJ-1 forms a homodimer and exerts chaperone and redox sensor functions, inhibiting the aggregation of disease-associated proteins (such as α-synuclein) and protecting cells from oxidative and glycation-induced damage[1][4]. Mutation or loss of DJ-1 function is causally linked to autosomal recessive early-onset Parkinson's disease, while altered DJ-1 activity or expression is also implicated in a range of cancers. DJ-1’s diverse biochemical activities, including esterase, protease (under specific conditions), glyoxalase, and putative deglycase activities, underscore its reputation as a cellular "Swiss army knife"[1][4]. DJ-1 is considered an emerging therapeutic target for both neurodegeneration and cancer, though clinical drugs specifically targeting it remain in early phases of research.

Other names

DJ-1DJ1Protein DJ-1Parkinson disease protein 7GATD2Maillard deglycaseOncogene DJ1Protein/nucleic acid deglycase DJ-1HEL-S-67pEpididymis secretory sperm binding protein Li 67pParkinson disease (autosomal recessive, early onset) 7

Antioxidant: protecting cells from oxidative damage; Modulation of protein glycation and glyoxalase activity; Regulation of transcription (as coactivator for androgen receptor and other factors); Repair of glycated DNA/nucleotide adducts.