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  • 1
    Electronic Resource
    Electronic Resource
    A neuropathological subset of Alzheimer's disease with concomitant Lewy body disease and spongiform change (1989)
    Springer
    Acta neuropathologica 78 (1989), S. 194-201 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer disease ; Diffuse Lewy body disease ; Spongiform change ; Creutzfeldt-Jakob disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The neuropathological heterogeneity of Alzheimer's disease (AD) is increasingly recognized. Diffuse Lewy body disease, for example, most frequently occurs in cases fulfilling histopathological criteria for AD, and these patients usually present with dementia rather than parkinsonism. We report five cases of concomitant AD and diffuse Lewy body disease with still another coexistent neuropathological feature: localized and stereotyped spongiform change in the neuropil. This spongiform change was most striking in the superior and inferior temporal, entorhinal, and insular cortex and the amygdala and was virtually indistinguishable from that seen in Creutzfeldt-Jakob disease. Electron microscopic study on one case revealed membrane-containing vacuoles in close association with neuritic plaques and plaired helical filament-filled processes. Immunocytochemistry using antibodies to prion proteins (PrPsc or PrP27–30) failed to label plaque or vascular amyloid in the five cases. Four primates inoculated with brain tissue from one case have not evidenced neurological disease in the 3 years since the transmission experiment. We conclude that these cases represent a neuropathological subset of AD with relatively widespread Lewy bodies and a localized spongiform change, predominantly involving the medial temporal region. Despite the light and electron microscopic commonality with Creutzfeldt-Jakob disease, there is no clear evidence that these cases represent a form of transmissible spongiform encephalopathy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00688209
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  • 2
    Electronic Resource
    Electronic Resource
    Immunoelectron microscopic study of synaptic pathology in Alzheimer's disease (1991)
    Springer
    Acta neuropathologica 81 (1991), S. 428-433 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer's disease ; Biopsy ; Synapses ; Synaptophysin ; Immunoelectron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Alzheimer's disease (AD) is characterized by an extensive loss of neurons and synapses in the neocortex which correlates strongly with psychometric tests of dementia. To characterize the ultrastructural changes in presynaptic terminals in AD, we studied biopsy material from the frontal cortex. We also examined, at the ultrastructural level, abnormal neurites scattered in the AD neuropil and in the plaque region using sections from autopsy material immunolabeled with anti-synaptophysin. We found that, regardless of amyloid deposits, some presynaptic terminals were distended and contained swollen vesicles and dense bodies. These altered synaptic organelles were similar to those found in dystrophic neurites. The latter structures displayed synaptophysin immunoreactivity, mostly localized to outer membranes of synaptic vesicles and dense bodies. The present study supports the hypothesis of progressive synaptic pathology in AD neocortex and favors the notion that the dystrophic process originates from presynaptic terminals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00293464
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  • 3
    Electronic Resource
    Electronic Resource
    Membranous Cytoplasmic Granules in Infantile Amaurotic Idiocy (1960)
    [s.l.] : Nature Publishing Group
    Nature 188 (1960), S. 1000-1002 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] INFANTILE amaurotic idiocy is characterized chemically by an accumulation of gangliosides in the nervous system. It has been suggested that the gangliosides occur naturally in polymeric form and in association with polypeptides or proteins1. The appearance of the involved neurons and results of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/1881000a0
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  • 4
    Electronic Resource
    Electronic Resource
    Dementia of the Alzheimer Type (1980)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Neuroscience 3 (1980), S. 77-95 
    Details
    ISSN: 0147-006X
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ne.03.030180.000453
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  • 5
    Electronic Resource
    Electronic Resource
    THE PREPARATION AND SOME PROPERTIES OF PURIFIED MYELIN FROM THE CENTRAL NERVOUS SYSTEM (1964)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 11 (1964), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1964.tb06719.x
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  • 6
    Electronic Resource
    Electronic Resource
    ON NEUROFILAMENT and NEUROTUBULE PROTEINS FROM HUMAN AUTOPSY TISSUE (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 29 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Neurofilaments and neurotubules are the principal fibers of the mature normal neuron. In this study the protein subunits of these neurofibrils were isolated from human autopsy tissue, and compared by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and by two dimensional peptide maps of the tryptic digest of these proteins labelled with 125I. The α and the β monomers of neurotubule are related but distinct in their peptide maps, while the major neurofilament protein subunit (molecular weight, 50,000) is remarkably similar to β tubulin. The neurofilament fraction binds colchicine, but the specificity is not yet determined. Neurotubule and neurofilament are also similar in having minor proteins which coelectrophorese on the gels. These results suggest that neurofilament and neurotubule may share one or more protein subunits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb10689.x
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