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  • Articles: DFG German National Licenses  (2)
  • 1990-1994  (2)
  • Amyloid precursor protein  (1)
  • Amyloid β protein  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Topographic heterogeneity of amyloid B-protein epitopes in brains with various forms of neuronal ceroid lipofuscinoses suggesting defective processing of amyloid precursor protein (1990)
    Springer
    Acta neuropathologica 80 (1990), S. 26-34 
    Details
    ISSN: 1432-0533
    Keywords: Neuronal ceroid lipofuscinosis ; Batten disease ; Lipopigment ; Storage disease ; Amyloid precursor protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To verify our hypothesis of defective protease inhibitor domains that are encoded by abnormal processing of amyloid precursor protein (APP) in brains of patients with neuronal ceroid lipofuscinoses (NCL), immunohistochemical and cytochemical studies were performed with monoclonal antibodies (mAbs) directed against various domains of APP. For the studies, 22 autopsy brains were used: 12 with different forms of NCL, and 10 control brains. The staining procedure for the avidin-biotin complex (ABC) technique and the postembedding gold-labelled procedure for electron microscopy (EM) were employed. Of all mAbs used for the study, only mAbs generated against amyloid B-protein bound to neural tissue were affected with NCL. The strongest immunostaining of neurons and of some reactive glial cells was found in brains with the juvenile form of NCL. Only in the infantile form of the disease were some neurons overloaded with storage material weakly immunoreactive. In brains of patients with the adult form of NCL, immunoreactivity was found in affected neurons and in extracellularly deposited material of senile plaques. The results of EM study showed that the immunoreactivity was restricted to lysosomal cytosomes in neural tissue with any form of NCL selectively localized on the curvilinear and fingerprint proteinaceous component of ceroid lipofuscin. Studies performed on control aging brains and Alzheimer's disease (AD) brains confirmed previous observations of immunoreactivity being found diffusely in the protein component of some neurons containing lipopigment. The defective processing of APP in brains with NCL and AD and in ageing brains is discussed. Our present results support the notion of heterogeneity of ceroid lipofuscin storage material in various forms of NCL and underline the hypothesis that abnormalities found in the protease inhibitors or APP in the proteinaceous composition of storage lipopigment could be a key to the unknown etiology of NCL.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00294218
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    Paper (German National Licenses)
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  • 2
    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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    Paper (German National Licenses)
    Fulltext
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