Hostname: page-component-5db6c4db9b-s6gjx Total loading time: 0 Render date: 2023-03-26T23:21:10.867Z Has data issue: true Feature Flags: { "useRatesEcommerce": false } hasContentIssue true

Two Types of Spheroid Bodies in the Nigral Neurons in Parkinson's Disease

Published online by Cambridge University Press:  18 September 2015

Tatsuo Yamada*
Kinsmen Laboratory of Neurological Research, Department of Psychiatry and The Neurodegenerative Diseases Centre, University of British Columbia, Vancouver
Haruhiko Akiyama
Kinsmen Laboratory of Neurological Research, Department of Psychiatry and The Neurodegenerative Diseases Centre, University of British Columbia, Vancouver
Patrick L. McGeer
Kinsmen Laboratory of Neurological Research, Department of Psychiatry and The Neurodegenerative Diseases Centre, University of British Columbia, Vancouver
2255 Wesbrook Mall, University of B.C., Vancouver, British Columbia, Canada V6T 1W5
Rights & Permissions[Opens in a new window]


HTML view is not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

Dendritic spheroid bodies (SBs) and Lewy bodies (LBs) were identified in comparable numbers in the substantia nigra pars compacta (SBC) of nine parkinsonian cases and one case of striatonigral degeneration but were not found irt cases of Huntington's disease or neurologically normal controls. The immunohistochemical profile of the SBs in dystrophic dendrites of nigrostriatal dopaminergic neurons was remarkably similar to that of the LBs found within dendrites or free of the SNC neuropil. Both types of inclusions stained positively with antibodies to tyrosine hydroxylase, ubiquitin and microtubule-associated protein-2 (MAP2), and negatively for Tau-2, although they had different ultrastructural appearances. A few intracellular LBs were stained by antibodies to neurofilament proteins (NFs) 68, 160, and 200 kD, but dendritic SBs and extracellular LBs were not so stained. These data indicate that dendritic SBs and extracellular LBs may have a common molecular pathogenetic origin in Parkinson's disease. On the other hand, the SBs seen in the pars reticulata (SNR) and in the distal nigrostriatal axons even in control cases were generally stained by antibodies to NFs and ubiquitin but not to MAP2. This latter staining pattern in similar to that shown by SBs in the anterior horn in ALS and in the cerebellum of neurologically normal brains and is believed typical of axonal as opposed to dendritic SBs.

Original Articles
Copyright © Canadian Neurological Sciences Federation 1991



1.Jellinger, K. Neuroaxonal dystrophy: its natural history and related disorders. Prog Neuropathol 1973; 2: 129180.Google Scholar
2.Smith, MC. Argyrophilic bodies in the human spinal cord. J Neurol Neurosurg Psychiatry 1955; 18: 1316.CrossRefGoogle Scholar
3.Clark, AW, Parhad, IM, Griffin, JW, et al. Neurofilamentous axonal swellings as a normal finding in the spinal anterior horn of man and other primates. J Neuropathol Exp Neurol 1984; 43: 253262.CrossRefGoogle ScholarPubMed
4.Carpenter, S. Proximal axonal enlargement in motor neuron disease. Neurology 1968; 18:842851.CrossRefGoogle ScholarPubMed
5.Schmidt, Ml, Carden, MJ, Lee, VM-Y, et al. Phosphate dependent and independent neurofilament epitopes in the axonal swellings of patients with motor neuron disease and controls. Lab Invest 1987; 56: 282294.Google ScholarPubMed
6.Manetto, V, Sternberger, NH, Perry, G, et al. Phosphorylation of neurofilaments is altered in amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 1988; 47: 642653.CrossRefGoogle ScholarPubMed
7.Leigh, PN, Anderton, BH, Dodson, A, et al. Ubiquitin deposits in anterior horn cells in motor neuron disease. Neurosci Lett 1988; 93: 197203.CrossRefGoogle Scholar
8.Kato, T, Katagiri, T, Hirano, A, et al. Lewy body-like hyaline inclusions in sporadic motor neuron disease are ubiquitinated. Acta Neuropathol (Berl) 1989; 77: 391396.CrossRefGoogle ScholarPubMed
9.Lowe, J, Aldridge, F, Lennox, G, et al. Inclusion bodies in motor cortex and brainstem of patients with motor neurone disease are detected by immunocytochemical localization of ubiquitin. Neurosci Lett 1989; 105:713.CrossRefGoogle Scholar
10.Migheli, A, Autilio-Ganbetti, P, Gambetti, C, et al. Ubiquitinated filamentous inclusions in spinal cord of patients with motor neuron disease. Neurosci Lett 1990; 114: 510.CrossRefGoogle ScholarPubMed
11.Hirano, A, Inoue, K. Early pathological changes of amyotrophic lateral sclerosis: electron microscopic study of chromatolysis, spheroids and Bunina bodies. Neurol Med (Tokyo) 1980; 13: 148160.Google Scholar
12.Sasaki, S, Kamei, H, Yamane, K, et al. Swelling of neuronal processes in motor neuron disease. Neurology 1988; 38: 11141118.CrossRefGoogle ScholarPubMed
13.Jellinger, K. Pathology of Parkinson’s syndrome. In: Calne, DB (ed.). Handbook of Experimental Pharmacology, Drugs for the Treatment of Parkinson’s Disease. Springer-Verlag, 1989; 88: 4794.CrossRefGoogle Scholar
14.Leigh, PN, Probst, A, Dale, GE, et al. New aspects of pathology of neurodegenerative disorders as revealed by ubiquitin antibodies. Acta Neuropathol (Berl) 1989; 79: 6172.CrossRefGoogle ScholarPubMed
15.Forno, LS. Pathology of Parkinson’s disease: the importance of the substantia nigra and Lewy bodies. In: Stern, GM (ed.) Parkinson’s Disease. Baltimore: The John Hopkins University Press, 1990: 185238.Google Scholar
16.Hershko, A, Ciechanover, A. The ubiquitin pathway for the degradation of intracellular proteins. In: Cohn, WE, Moldave, K (eds.). Progress in Nucleic Acid Research and Molecular Biology. New York: Academic Press Inc., 1986; 33: 1956.Google Scholar
17.Goldman, JE, Yen, S-H, Chiu, F-C, et al. Lewy bodies of Parkinson’s disease contain neurofilament antigens. Science 1983; 221: 10821084.CrossRefGoogle ScholarPubMed
18.Nakazato, X, Sasaki, A, Hirato, J, et al. Immunohistochemical localization of neurofilament protein in neuronal degenerations. Acta Neuropathol (Bed) 1984; 64: 3036.CrossRefGoogle ScholarPubMed
19.Kahn, J, Anderton, BH, Gibb, WRG, et al. Neuronal filaments in Alzheimer’s, Pick’s and Parkinson’s diseases. N Engl J Med 1985;313:520521.Google ScholarPubMed
20.Forno, LS. The Lewy body in Parkinson’s disease. Adv Neurol 1986;45:3543.Google Scholar
21.Forno, LS, Sternberger, LA, Sternberger, NH, et al. Reaction of Lewy bodies with antibodies to phosphorylated and non-phosphorylated neurofilaments. Neurosci Lett 1986; 64: 253258.CrossRefGoogle ScholarPubMed
22.Papola, MA. Lewy Bodies of Parkinson’s disease. Immune electron microscopic demonstration of neurofilament antigens in constitutent filaments. Arch Pathol Lab Med 1986; 110: 11601163.Google Scholar
23.Galloway, PG, Grundke-Iqbal, I, Iqbal, K, et al. Lewy bodies contain epitopes both shared and distinct from Alzheimer neurofibrillary tangles. J Neuropath Exp Neurol 1988; 47: 654663.CrossRefGoogle ScholarPubMed
24.Bancher, C, Lassmann, H, Budka, H, et al. An antigen profile of Lewy bodies: Immunocytochemical indication for protein phosphorylation and ubiquitination. J Neuropath Exp Neurol 1989; 48: 8193.CrossRefGoogle ScholarPubMed
25.Duffy, PE, Tennyson, VM. Phase and electron microscopic observations of Lewy bodies and melanin granules in the substantia nigra and locus coeruleus in Parkinson#x2019;s disease. J Neuropath Exp Neurol 1965; 24: 398414.CrossRefGoogle Scholar