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Glutathione‐related enzymes in brain in Parkinson's disease
Author(s) -
Sian J.,
Dexter D. T.,
Lees A. J.,
Daniel S.,
Jenner P.,
Marsden C. D.
Publication year - 1994
Publication title -
annals of neurology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.764
H-Index - 296
eISSN - 1531-8249
pISSN - 0364-5134
DOI - 10.1002/ana.410360306
Subject(s) - glutathione , substantia nigra , glutathione peroxidase , globus pallidus , chemistry , caudate nucleus , putamen , glutathione reductase , gpx3 , medicine , biochemistry , endocrinology , biology , enzyme , basal ganglia , central nervous system , dopamine , dopaminergic
The activities of enzymes related to glutathione synthesis, degradation, and function were analyzed in various brain regions (cerebral cortex, caudate nucleus, putamen, globus pallidus, and substantia nigra) from patients dying with pathologically proven Parkinson's disease (PD) and multiple system atrophy (MSA), and from matched controls with no neurological disorder. The activity of the glutathione degradative enzyme, σ‐Glutamyltranspeptidase, was selectively elevated in substantia nigra (SN) in PD. In contrast, the activity of the synthetic enzyme, σ‐glutamylcysteine synthetase, was unaltered in SN and other brain areas in PD. Similarly, glutathione peroxidase and glutathione transferase activities were unaltered in SN or in other brain regions in PD. σ‐Glutamylcysteine synthetase, σ‐glutamyltranspeptidase, glutathione peroxidase, and glutathione transferase activities were normal in SN and most other brain areas in MSA. However, glutathione peroxidase activity was increased in the lateral globus pallidus and caudate nucleus in MSA. The depletion of reduced glutathione (GSH) in the SN in PD, with no change in oxidized glutathione (GSSG), may be due to efflux of GSH mainly out of glia promoted by σ‐glutamyltranspeptidase, perhaps with additional increased conversion of GSH to GSSG (which itself is transported out of cells by σ‐glutamyltranspeptidase), in response to increased hydrogen peroxide formation.