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  • 1
    Electronic Resource
    Electronic Resource
    A Comparative Study on the Substructures of Neurofilaments and Paired Helical Filaments from Alzheimer Neurofibrillary Tangles (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 455 (1985), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1985.tb50485.x
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  • 2
    Electronic Resource
    Electronic Resource
    Young adult-form of dementia with neurofibrillary changes and lewy bodies (1987)
    Springer
    Acta neuropathologica 74 (1987), S. 97-104 
    Details
    ISSN: 1432-0533
    Keywords: Dementia ; Neurofibrillary changes ; Lewy bodies ; Alzheimer's disease ; Parkinsonism-dementia complex
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Alzheimer's neurofibrillary tangles, Lewy bodies and chromatolytic neurons were found in the brain at autopsy of a 28-year-old male with pyramidal and extrapyramidal signs, and severe dementia of 7-year duration prior to his death. Review of histological material showed generalized changes involving both cortical and subcortical structures. These changes were characterized by the presence of neurofibrillary tangles, Lewy bodies and chromatolytic neurons. Neuritic plaques were not found. There was also loss of neurons and gliosis in the prefrontal cortex, hippocampus, amygdaloid nucleus, basal ganglia, midbrain and pons. There were spongiform changes due to loss of neurons. Myelin stain showed pallor of myelin in long tracts and in subcortical regions. The neurofibrillary tangles were mostly composed of Alzheimer's paired helical filaments (PHF). PHF were immunostained with both polyclonal and monoclonal antibodies to PHF and the microtubule-associated protein tau. Some Lewy bodies were immunolabelled with monoclonal antibodies to PHF. To the best of our knowledge it is the first reported case of a young adult-form of dementia with extensive formation of neurofibrillary changes and Lewy bodies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00688346
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  • 3
    Electronic Resource
    Electronic Resource
    The comparative immunoreactivities of brain amyloids in Alzheimer's disease and scrapie (1987)
    Springer
    Acta neuropathologica 74 (1987), S. 313-323 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer amyloids ; Synthetic peptide ; Antibodies ; Fibril formation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary An antibody was raised to a synthetic peptide corresponding to a published sequence for the first 24 residues of a cerebrovascular amyloid peptide (CVAP). Immunohistochemical staining of tissue sections revealed that the antibody bound extensively to cerebrovascular amyloid in Alzheimer disease (AD/SDAT) and Down's syndrome cases. The antibody bound less extensively to neuritic plaques (primitive and mature) and indetectably to neurofibrillary tangles. The antibody did not label scrapie plaques, scrapie-associated fibrils, or Gerstmann-Sträussler syndrome plaques. Immunoblotting experiments showed that the cerebrovascular amyloid peptide epitopes contaminating the neurofibrillary tangle preparations could be extracted with urea, leaving the neurofibrillary tangles intact. These data confirm that the cerebrovascular amyloid peptide is a component of cerebrovascular amyloid, and suggest that its epitopes are also components of neuritic plaque amyloid. The reduced level of immunostaining on amyloid cores in tissue sections suggests that either the cerebrovascular amyloid peptide epitopes are a minor component of amyloid cores, or that their mode of packing or state of processing in amyloid cores renders them relatively inaccessible to the antibody. We also conclude that the cerebrovascular amyloid peptide is not a component of neurofibrillary tangles. The synthetic cerebrovascular amyloid peptide possesses amyloid-like properties: at neutral pH it forms insoluble aggregates consisting of 5–7-nm fibrils, which form red-green birefringent adducts with Congo red and fluoresce with thioflavine S.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00687207
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  • 4
    Electronic Resource
    Electronic Resource
    Laminar distribution of neuritic plaques in normal aging, Alzheimer's disease and Down's syndrome (1988)
    Springer
    Acta neuropathologica 77 (1988), S. 21-25 
    Details
    ISSN: 1432-0533
    Keywords: Neuritic (senile) plaque ; Alzheimer disease ; Down's syndrome ; Aging brain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Quantitative studies of neuritic (senile) plaques in six cortical layers were carried out in brains from people with confirmed clinical and neuropathological diagnosis of senile dementia of the Alzheimer type (SDAT) and Down's syndrome (DS). The same studies were performed on brains of normal old-aged people. In Alzheimer disease (AD) and DS cases the highest numbers of neuritic plaques (NP) were observed in temporal lobe layers III and II and occipital lobe layers III, IV and II. In normal old-aged people the highest numbers of NP were found in temporal lobe III and V and in occipital lobe IV, III, and V layer. The plaque numbers in both temporal and occipital cortices of AD and DS were significantly higher than that of normal old-aged people but there was no difference between AD and DS.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00688238
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  • 5
    Electronic Resource
    Electronic Resource
    Alzheimer neuropathology in non-Down's syndrome mentally retarded adults (1990)
    Springer
    Acta neuropathologica 80 (1990), S. 362-367 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer disease ; Mental retardation ; Neuritic plaques ; Neurofibrillary tangles ; Paired helical filaments
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We examined the brains of 385 mentally retarded adults aged 23–90 years without Down's syndrome (DS), metabolic disorder, or hydrocephalus to extend our knowledge about the occurrence of Alzheimer-type neuropathology in this population. Relevant measures of neuropathology also were related to selected information available from clinical records. The presence of one or more neurofibrillary tangles (NFT) and/or neuritic plaques (NP) was observed in 63.4% of all cases and varied with age. The prevalence of positive cases was higher when mental retardation was due to head trauma, congenital malformation, or familial factors and when a history of seizures was reported. Comprehensive morphometric analyses of neocortical, hippocampal and parahippocampal areas indicated that recommended agespecific quantitative criteria for the diagnosis of Alzheimer disease [Khachaturian ZS (1985) Arch Neurol 42:1097–1105] were met in 9.5% of cases less than 50 years of age, 54.2% between 50 and 65, 70% between 66 and 75, and 87% of the cases greater than 75 years of age. However, a limited immunohistochemical study revealed that in most cases the NP did not have a neuritic component containing paired helical filaments and in this respect most of the plaques observed in this population may differ from those most strongly associated with Alzheimer disease. In addition, substantial numbers of NFT were seen in frontal cortex, contrasting with results reported in the literature for nonretarded populations. The number of NP per mm2 consistently increased with age for all areas examined, while the relationship between NFT density and age varied across areas, and was clearly not monotonic. Our studies show that the neuropathological lesions currently considered hallmarks of Alzheimer disease are prevalent among non-DS mentally retarded adults, and the regional density of these lesions is high. Thus, while people with DS are affected at an earlier age, clear Alzheimer neuropathology develops in many mentally retarded individuals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307688
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  • 6
    Electronic Resource
    Electronic Resource
    Presence of non-fibrillar amyloid b protein in skin biopsies of Alzheimer's disease (AD), Down's syndrome and non-AD normal persons (1994)
    Springer
    Acta neuropathologica 88 (1994), S. 201-206 
    Details
    ISSN: 1432-0533
    Keywords: Key words Amyloid β protein ; Skin biopsy ; Alzheimer's disease ; Down's syndrome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A total of 66 skin biopsies from persons with Alzheimer's disease (AD) or Down's syndrome (DS) and from persons without AD were used in this study. The age range was from 7 to 89 years. Positive immunoreactivity of skin biopsies to monoclonal antibody 4G8, which is reactive to amino acid residue 17 – 24 of synthetic amyloid β protein (Aβ), and 4G8-Fab (the antigen-binding fragment of 4G8 IgG, reactive only to amyloid plaque) was observed in the epidermis-dermis junction or the basement membrane of the epidermis and in some blood vessels of the biopsy skins of 13/18 (72  %) AD, 9/10 (90  %) DS, and 14/38 (37  %) non-AD control cases. The Fisher exact probability test revealed a significant difference (P=0.0415 one-tailed) in immunoreactivity between AD and age-matched controls. There was also a significant difference (P=0.0152 one-tailed; P=0.0200 two-tailed) between DS and age-matched control in the same test. Immuno-gold electron microscopy examination of these cases with positive immunoreactivity revealed that the gold particles were deposited along the basement membrane of the epidermis. Amyloid fibrils were not observed in the regions with gold particles. Results of this study suggest that Aβ is associated with the basement membrane of skin and is present in amorphous, non-fibrillar form as soluble Aβ.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00293394
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  • 7
    Electronic Resource
    Electronic Resource
    Comparison of four staining methods on the detection of neuritic plaques (1989)
    Springer
    Acta neuropathologica 78 (1989), S. 22-27 
    Details
    ISSN: 1432-0533
    Keywords: Neuritic plaques ; Alzheimer disease ; Down syndrome ; Normal aging ; Immunostaining
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The sensitivities of four staining methods for detecting the presence of neuritic plaques in the normal aging. Alzheimer disease (AD) and Down's syndrome (DS) brains were compared. The Bielschowsky method and immunostaining with monoclonal antibody (4G8, IgG2b) to β-amyloid revealed the highest numbers of plaques. The thioflavin S-staining method showed about 38%–70% of plaques as shown by the Bielschowsky method. The Bodian method is the least sensitive method revealing about 26%–39% of plaques as compared with the Bielschowsky method. In the first part of this study, serial sections (6 μm) of the plaques from AD and DS brains were cut and stained with Bielschowsky, thioflavin S and Bodian methods, respectively. In the second part, Bielschowsky and immunostaining methods were used to stain serial sections (6 μm) of plaques from the same block of brain tissue. A Zeiss Axiophot fluorescence microscope, coupled with the Cambridge Quantiment 970 and Zeiss Videoplan computerized image analyzers, was used to quantify the number of plaques. Both Bielschowsky and immunostaining methods revealed the presence of both the peripheral zone (halo) and the central core of a classical plaque and resulted in the highest plaque counts. The central core of the thioflavin S-stained plaques were still clearly present, but the peripheral zone was barely visible. In Bodian stain, however, both central core and peripheral zone were poorly stained and not detectable by computer. They were quantified by human eye observation. The Bielschowsky method and immunostaining with pretreatment with formic acid are, therefore, the most sensitive methods showing the highest contrast of plaque image and thus facilitate the quantification of plaque by computer. However, Bielschowsky method is not a specific method for plaques. It stains neurofibrillary tangles and blood vessels regardless of whether they have amyloid deposits or not. Immunostaining is a sensitive and specific method for amyloid and exhibits low background staining. It confirmed that all Bielschowsky-stained plaques contained amyloid deposit.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00687398
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  • 8
    Electronic Resource
    Electronic Resource
    Spectrum of morphological appearance of amyloid deposits in Alzheimer's disease (1989)
    Springer
    Acta neuropathologica 78 (1989), S. 337-347 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer's disease ; Amyloidosis ; β-protein ; Immunocytochemistry ; Paired helical filaments
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Immunocytochemical staining with monoclonal antibodies to the β-protein on tissue sections which have been pretreated with formic acid is not only a very specific but also a highly sensitive method for the detection of amyloid deposits in the brains of Alzheimer's disease victims. We report here a spectrum of morphological appearance of the brain amyloid deposits which are one of the main histopathological correlates of this disorder. Deposits of the β-protein are not only found in the well-known lesions [congophilic angiopathy and senile (neuritic) plaques] but are also seen under various morphological forms for which the word “plaques” does not appear an appropriate term: amyloid fibrils are found as large areas of diffuse infiltration of the neuropil, as ribbon-like infiltration in the subpial layer of the cerebral cortex, as granular deposits in the white matter, as diffuse deposits in the molecular layer of the cerebellum and the basal ganglia and as star-shaped deposits in the cerebellar Purkinje cell layer. The morphology of these deposits seems to depend on the cyto-and fibroarchitectonics of the brain region in which they are found, on the amount of amyloid deposited, and also on the type of staining technique used. It is only under specific circumstances that the deposition of amyloid in the neuropil is accompanied by the formation of paired helical filaments in nerve cell processes and their parent perikarya. In conclusion, our studies suggest that the extent of brain amyloidosis in Alzheimer's disease is much wider than so far appreciated.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00688170
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  • 9
    Electronic Resource
    Electronic Resource
    Presence of non-fibrillar amyloid β protein in skin biopsies of Alzheimer's disease (AD), Down's syndrome and non-AD normal persons (1994)
    Springer
    Acta neuropathologica 88 (1994), S. 201-206 
    Details
    ISSN: 1432-0533
    Keywords: Amyloid β protein ; Skin biopsy Alzheimer's disease ; Down's syndrome
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A total of 66 skin biopsies from persons with Alzheimer's disease (AD) or Down's syndrome (DS) and from persons without AD were used in this study. The age range was from 7 to 89 years. Positive immunoreactivity of skin biopsies to monoclonal antibody 4G8, which is reactive to amino acid residue 17–24 of synthetic amyloid β protein (Aβ), and 4G8-Fab (the antigen-binding fragment of 4G8 IgG, reactive only to amyloid plaque) was observed in the epidermis-dermis junction or the basement membrane of the epidermis and in some blood vessels of the biopsy skins of 13/18 (72%) AD, 9/10 (90%) DS, and 14/38 (37%) non-AD control cases. The Fisher exact probability test revealed a significant difference (P=0.0415 one-tailed) in immunoreactivity between AD and age-matched controls. There was also a significant difference (P=0.0152 one-tailed; P=0.0200 two-tailed) between DS and age-matched control in the same test. Immuno-gold electron microscopy examination of these cases with positive immunoreactivity revealed that the gold particles were deposited along the basement membrane of the epidermis. Amyloid fibrils were not observed in the regions with gold particles. Results of this study suggest that Aβ is associated with the basement membrane of skin and is present in amorphous, non-fibrillar form as soluble Aβ.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00293394
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  • 10
    Electronic Resource
    Electronic Resource
    The doublet microtubules of rods of the rabbit retina (1982)
    Springer
    Anatomy and embryology 165 (1982), S. 315-328 
    Details
    ISSN: 1432-0568
    Keywords: Rabbit photoreceptor ; Retina ; Microtubules ; Protofilaments ; Connecting cilium ; Outer doublets ; Microtubule assembly ; Tubulin of oligomers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The connecting cilium of the rabbit photoreceptor rod is composed of nine outer doublets, lacking dynein side arms. The central singlet microtubules are absent. In cross section, there is an inner dense ring situated between the doublets and the center core of the cilium. As the doublet microtubules progress from the connecting region into outer segments, the cylindrical array of the nine pairs of doublets spreads out as a brush-like arrangement into the incisure cavity of the outer segment. The microtubules continue as doublets for much of the length of the outer segment. The B-tubules terminate first; the A-tubules extend as single tubules into the apical region of the photoreceptor. Before the B-tubules end, they open up, forming hook-shaped projections from the A-tubules. The gradual reduction in length of these hook-shaped structures suggests that near their distal ends each B-tubule opens because of the separation of protofilament 1 of the B-tubule from protofilament 1 of the adjacent A-tubule. Subsequently, the B-tubule protofilaments terminate individually.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00305570
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