Decreased Ferritin Levels in Brain in Parkinson's Disease

Abstract: Ferritin levels were measured in postmortem brain tissue from patients dying with Parkinson's disease [treated with L‐3,4‐dihydroxyphenylalanine (L‐DOPA)] and from control patients. Ferritin levels were decreased in the substantia nigra, caudate‐putamen, globus pallidus, cerebral cortex, and cerebellum when compared with age‐matched control tissues. However, in CSF from L‐DOPA‐treated patients and in serum from L‐DOPA‐treated and untreated parkinsonian patients, ferritin levels were normal. Previous studies have suggested an increased total iron content in substantia nigra of parkinsonian brain. The failure of substantia nigra ferritin formation to be stimulated by increased iron levels suggests some defect in iron handling in this critical brain region in Parkinson's disease. The reason for decreased ferritin levels throughout the parkinsonian brain is not clear but does not seem to reflect a general system deficit in ferritin.

[1]  K. Earle Studies on Parkinson's disease including x-ray fluorescent spectroscopy of formalin fixed brain tissue. , 1968, Journal of neuropathology and experimental neurology.

[2]  R D Klausner,et al.  Iron-responsive elements: regulatory RNA sequences that control mRNA levels and translation. , 1988, Science.

[3]  K. Jellinger,et al.  Pathology of Parkinson's disease. Changes other than the nigrostriatal pathway. , 1991, Molecular and chemical neuropathology.

[4]  Y. Agid,et al.  Does levodopa aggravate Parkinson's disease? , 1988, Neurology.

[5]  Peter Riederer,et al.  Transition Metals, Ferritin, Glutathione, and Ascorbic Acid in Parkinsonian Brains , 1989, Journal of neurochemistry.

[6]  C. Marsden,et al.  Increased Nigral Iron Content and Alterations in Other Metal Ions Occurring in Brain in Parkinson's Disease , 1989, Journal of neurochemistry.

[7]  H. Munro,et al.  Induction of ferritin subunit synthesis by iron is regulated at both the transcriptional and translational levels. , 1988, The Journal of biological chemistry.

[8]  Elizabeth C. Theil Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms. , 1987, Annual review of biochemistry.

[9]  C. Marsden,et al.  LIPID PEROXIDATION AS CAUSE OF NIGRAL CELL DEATH IN PARKINSON'S DISEASE , 1986, The Lancet.

[10]  R. L. Wixom,et al.  Hemosiderin: nature, formation, and significance. , 1980, International review of experimental pathology.

[11]  R D Klausner,et al.  Identification of the iron-responsive element for the translational regulation of human ferritin mRNA. , 1987, Science.

[12]  C. Marsden,et al.  in vitro characterisation of dopamine receptors in the superior colliculus of the rat , 1987, Neuropharmacology.

[13]  R. Crichton,et al.  Iron uptake and utilization by mammalian cells. I: Cellular uptake of transferrin and iron , 1983 .

[14]  B. Hallgren,et al.  THE EFFECT OF AGE ON THE NON‐HAEMIN IRON IN THE HUMAN BRAIN , 1958, Journal of neurochemistry.

[15]  P. Harrison,et al.  Effect of ferritin-containing fractions with different iron loading on lipid peroxidation. , 1983, The Biochemical journal.

[16]  C. Marsden,et al.  Basal Lipid Peroxidation in Substantia Nigra Is Increased in Parkinson's Disease , 1989, Journal of neurochemistry.

[17]  H. Munro,et al.  SMALL-SCALE ISOLATION OF FERRITIN FOR THE ASSAY OF THE INCORPORATION OF 14C-LABELLED AMINO ACIDS. , 1965, The Biochemical journal.

[18]  B. Halliwell,et al.  Iron and free radical reactions: two aspects of antioxidant protection , 1986 .

[19]  C. Marsden,et al.  INCREASED NIGRAL IRON CONTENT IN POSTMORTEM PARKINSONIAN BRAIN , 1987, The Lancet.