Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    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
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Substructures of paired helical filaments from alzheimer's disease neurofibrillary tangles (1985)
    Springer
    Acta neuropathologica 66 (1985), S. 173-176 
    Details
    ISSN: 1432-0533
    Keywords: Paired helical filaments ; Neurofilaments ; Substructures ; Alzheimer's disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Presented studies reveal that each of the approximately 10 nm filaments forming the paired helical filaments (PHF) is made up of four protofilaments. Each of the protofilaments is a beaded structure, consisting of globules connected by longitudinal bars. A cross-view of PHF shows eight globules linked by transverse bars. The transverse bars are shorter than the longitudinal bars. Comparison between PHF and neurofilament protofilaments indicates structural differences between these profiles, i.e., the globules making the PHF protofilaments are larger and the longitudinal bars are longer than those in the normal neurofilaments. A three-dimensional diagram of PHF structure is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00688696
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    High resolution analysis of paired helical filaments in Alzheimer's disease (1987)
    New York, NY : Wiley-Blackwell
    Journal of Electron Microscopy Technique 5 (1987), S. 347-355 
    Details
    ISSN: 0741-0581
    Keywords: Paired helical filaments ; Alzheimer's disease ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Results of this comparative study indicated that electron microscopy of supra-ultrathin sections provided the best resolution, revealing the subunit structures, globules (32 Å ± 4), and longitudinal bars (47 Å ± 6) of paired helical filaments (PHF). A three-dimensional model of PHF substructure is therefore presented. The image of brightfield electron micrographs of isolated PHF positively stained with 2% phosphotungstic acid (PTA) also provided high resolution and revealed the presence of the beaded structures of these heavily stained filaments in the crossing-over region of PHF. Noisy background of the negatively stained preparation of isolated PHF substantially reduced the resolution. Severe flattened morphology of this preparation further complicated the interpretation of image analysis. Darkfield electron micrographs offered high-image contrast with low noise in the background clearly demonstrating the ropelike twisting configuration of PHF, but did not reveal the substructures of PHF. The tilting (±45°) analysis of these PHF prepared by uranyl acetate staining and rotary-shadowing and unidirectional shadowing methods with platinum showed that these heavy metals were deposited on the top filaments (away from the carbon film on the grid) in the crossing-over region of PHF.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1060050405
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...