Protein deglycase DJ-1 (DJ-1)

Protein deglycase DJ-1 is a highly conserved, multifunctional enzyme belonging to the Class I glutamine amidotransferase-like superfamily, and is found in many mammalian tissues including the brain. DJ-1 acts as a redox-sensitive chaperone and deglycase, repairing protein and nucleic acids damaged by metabolic byproducts like methylglyoxal and glyoxal, particularly under oxidative stress. It inhibits α-synuclein aggregation, plays important roles in protection against neurodegeneration and in cellular redox signaling, and regulates androgen receptor-dependent transcription. Mutations in the PARK7 gene encoding DJ-1 cause autosomal recessive, early-onset Parkinson's disease, making DJ-1 a key disease-associated protein and a focus of drug discovery for neuroprotective therapies. DJ-1 additionally serves as a biomarker for Parkinson's disease and potentially certain cancers, but its broad cellular functions and tight regulation necessitate careful consideration when developing therapeutic interventions.

Other names

DJ-1PARK7PARK7_HUMANParkinson disease (autosomal recessive, early onset) 7parkinson protein 7DJ1

Drugs targeting DJ-1 may act by enhancing its antioxidative activity, stabilizing its structure, augmenting deglycase function, or reducing its pathological oxidation