CHANGES OF THIOL-DISULFIDE BALANCE IN PARKINSON’S DISEASE

Abstract

Parkinson’s disease (BP) is one of the most common neurodegenerative pathologies. It is characterized by a selective death of DA neurons in the black substance of the midbrain, resulting from the formation of an excess of free radicals and the development of oxidative stress. Attempts to use antioxidants as a means of pathogenetic therapy of BP have been unsuccessful. Modern concepts of the understanding of the role of oxidative stress in the development of Parkinson’s disease (PD), as well as other neurodegenerative diseases suggest that an important role in the mechanisms of metabolic changes leading to the death of nervous tissue is played not only by the enhancement of formation of free radical products but also by the weakening of antioxidant defense systems in brain tissue. The most important components of the thiol/disulphide buffer systems involved in maintaining the redox balance in the brain are pairs of oxidized and reduced glutathione (GSH/GSSG), as well as thiol/disulfide oxidoreductases. Controlling the intensity of formation of free radical products from cellular antioxidant redox enzymes, primarily glutathione and thioredoxin-dependent enzyme systems, is extremely important not only to prevent brain tissue damage due to oxidative stress, but also to maintain the redox balance. The review presents the data showing pronounced changes in the redox potential of the glutathione system, thiol-disulphide balance, S-glutathionylation of in brain tissue proteins in experimental PD models, and in postmortem brain tissue samples of patients with PD. The elucidation of the mechanisms of maintaining the redox balance in brain tissue under oxidative stress in PD can serve as a justification for a new direction in neuroprotection and a search for new agents for pathogenetic therapy of PD.