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Increase in dopamine turnover and tyrosine hydroxylase enzyme in hippocampus of rats fed on low selenium diet
Author(s) -
Castaño A.,
Ayala A.,
RodriguezGomez J. A.,
De La Cruz C. P.,
Revilla E.,
Cano J.,
Machado A.
Publication year - 1995
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490420511
Subject(s) - tyrosine hydroxylase , endocrinology , glutathione reductase , medicine , glutathione peroxidase , dopamine , tyrosine 3 monooxygenase , superoxide dismutase , catalase , chemistry , monoamine oxidase , tyrosine , peroxidase , glutathione , enzyme , biochemistry , biology , oxidative stress
We have studied the turnover of dopamine, noradrenaline, and serotonin and their metabolites in hippocampus of adult female rats that were fed control or selenium‐deficient diets during 15 days. Under these circumstances, there was an increase of dopamine turnover (4‐fold) in rats fed with selenium‐deficient diet with respect to controls and also an increase in the tyrosine hydroxylase activity (75.8%), which was the result of the increase of the amount of the enzyme (2‐fold), without significant change in the phosphorylation of the tyrosine hydroxylase. In addition the glutathione peroxidase, glutathione reductase, catalase, and superoxide dismutase activities have been studied. After selenium‐deficient diet, the enzymatic activities of superoxide dismutase and catalase did not show change with respect to the controls; however glutathione reductase and glutathione peroxidase significantly decreased 15% and 29%, respectively. It is concluded that the increase in dopamine turnover seems to be associated with the induction of tyrosine hydroxylase enzyme. In these conditions the decrease in antioxidant capacity may produce a cascade of events, which accelerates the degenerative process, since the increase in dopamine turnover produces an increase in oxygen radical by monoamine oxidase activity. © 1995 Wiley‐Liss, Inc.