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Hallervorden‐Spatz disease: Cysteine accumulation and cysteine dioxygenase deficiency in the globus pallidus
Author(s) -
Perry Thomas L,
Norman Margaret G.,
Yong Voon Wee,
Whiting Sharon,
Crichton John U.,
Hansen Shirley,
Kish Stephen J.
Publication year - 1985
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.410180411
Subject(s) - globus pallidus , cysteine , medicine , chemistry , biochemistry , basal ganglia , enzyme , central nervous system
We describe neurochemical abnormalities found in the brains of 2 patients with autopsy‐confirmed Hallervorden‐Spatz (HS) disease. In 1 patient, contents of cystine and of glutathione‐cysteine mixed disulfide in the globus pallidus were markedly elevated above values for appropriate control subjects. Activity of cysteine dioxygenase, which converts cysteine to cysteine sulfinic acid, was reduced in the globus pallidus, but normal in the frontal cortex and putamen of both patients. γ‐Aminobutyric acid content was markedly decreased in the globus pallidus and substantia nigra of both patients. These results suggest that cysteine accumulates locally in the globus pallidus in Hallervorden‐Spatz disease as a result of an enzymatic block in the metabolic pathway from cysteine to taurine. Accumulated cysteine may chelate iron, accounting for the local increase in iron content in Hallervorden‐Spatz disease. The combined excess of cysteine and ferrous iron may generate free radicals that damage neuronal membranes to cause the typical morphological changes observed in this disorder.