PARK7 Human

PARK7 was initially identified as an oncogene product and later found to be associated with Parkinson’s disease (PD) and several types of cancer . The protein is approximately 20 kDa in size and is highly conserved across different species . Its primary function is to protect cells from stress conditions, particularly oxidative stress, through both enzymatic and non-enzymatic mechanisms .

The key element for PARK7’s function is the highly conserved cysteine residue at position 106 (Cys106) . This residue is crucial for the protein’s enzymatic glyoxalase activity and its non-enzymatic functions, including antioxidant, chaperone, co-transcription factor, and anti-apoptotic/ferroptotic activities . Oxidation of Cys106 is essential for PARK7 to perform these functions, but excessive oxidation can lead to the loss of its neuroprotective activity and contribute to the development of neurodegenerative diseases .

In the context of Parkinson’s disease, PARK7 is involved in protecting dopaminergic neurons from oxidative stress and other cellular stressors . The loss of function or mutations in the PARK7 gene can lead to the degeneration of these neurons, which is a hallmark of Parkinson’s disease . This makes PARK7 a critical target for therapeutic interventions aimed at slowing or preventing the progression of Parkinson’s disease .

Recombinant human PARK7 is produced using genetic engineering techniques to study its structure, function, and role in various diseases . This recombinant protein is used in research to develop potential therapeutic agents that can modulate its activity and provide neuroprotection .

Recent studies have focused on developing inhibitors, probes, and proteolysis-targeting chimeras (PROTACs) to study PARK7 in living cells . These tools help researchers understand the biological functions of PARK7 and its involvement in disease processes, opening new opportunities for therapeutic interventions .