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  • Biochemistry and Biotechnology  (1)
  • Down’s syndrome  (1)
  • precursor-like protein 1  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Amyloid precursor-like protein 1 accumulates in neuritic plaques in Alzheimer’s disease (1997)
    Springer
    Acta neuropathologica 94 (1997), S. 519-524 
    Details
    ISSN: 1432-0533
    Schlagwort(e): Key words Alzheimer’s disease ; Amyloid ; precursor-like protein 1 ; Amyloid precursor protein ; Plaques
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract The Alzheimer’s disease (AD) β-amyloid precursor protein (APP) and the amyloid precursor-like protein 1 (APLP1) and 2 (APLP2) are members of a superfamily of proteins that appear functionally related. Although APLPs are highly homologous to APP in the N- and C-terminal domains, they lack the βA4/amyloid peptide, i.e., the main constituent of neuritic plaques in AD. To assess a potential role of APLP1 in AD, we have determined its immunohistochemical distribution in human hippocampal formation, a structure which is strongly affected in AD, and compared it with APP immunoreactivity. There was a considerable overlap of APP and APLP1 regional expression patterns. Significant APLP1 immunoreactivity was observed in neuritic plaques. Large pyramidal neurons of the subiculum showed an accumulation of APLP1 protein in their dendritic compartment. Some astrocytes elicited perinuclear APLP1 staining, but this was observed in both AD and control brains. These findings raise the possibility that APLP1 may contribute to the pathogenesis of AD-associated neurodegeneration.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s004010050745
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Reverse relationship between β-amyloid precursor protein and β-amyloid peptide plaques in Down’s syndrome versus sporadic/familial Alzheimer’s disease (1999)
    Springer
    Acta neuropathologica 97 (1999), S. 113-118 
    Details
    ISSN: 1432-0533
    Schlagwort(e): Keywords Alzheimer’s disease ; Down’s syndrome ; β-Amyloid precursor protein ; β-Amyloid peptide
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Strong genetic evidence has been accumulated in favor of a central role of β-amyloid precursor protein (APP) and β-amyloid peptide (βA4) in the pathogenesis of Alzheimer’s disease (AD). We employed four newly developed APP and βA4 antibodies and performed a comparative neuropathological study of patients with Down’s syndrome (DS), early-onset familial AD and sporadic AD to investigate the distribution of APP and βA4 plaque densities in the cerebral cortex of these disorders. Quantitative analysis of APP versus βA4 plaques revealed that brains with early-onset familial AD and sporadic AD showed significantly more βA4 plaques than brains with DS (P 〈 0.05). In contrast, APP plaques were more abundant in DS cerebral cortex (P 〈 0.02). These observations suggest that the development of pathological changes in DS brains does not parallel that observed in AD, which might be attributable to different causes in the pathogenesis of βA4 formation. A comparison of these disorders may be useful to further complement our knowledge of the mechanisms leading to plaque development.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s004010050963
    Standort Signatur Einschränkungen Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    A synthetic substrate assay for the gamma-secretase of the β-A4 amyloid of alzheimer's disease (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 1 (1995), S. 132-139 
    Details
    ISSN: 1075-2617
    Schlagwort(e): βA4 amyloid peptide ; radiometric assay ; transmembrane peptide ; reverse-phase TLC ; Chemistry ; Biochemistry and Biotechnology
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Chemie und Pharmazie
    Notizen: γ-secretase, the endoprotease which releases the C-terminus of βA4 amyloid peptide, cleaves within the hydrophobic transmembrane domain of the amyloid precursor protein. In order to obtain a substrate for γ-secretase, a dodecapeptide which spans the cleavage site was synthesized, labelled with 125-iodine and conjugated to an agarose gel. A radiometric solid-phase assay was developed using this immobilized substrate. Peptide products were separated by reverse-phase HPLC and TLC to allow characterization of the cleavage site(s).
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/psc.310010205
    Standort Signatur Einschränkungen Verfügbarkeit
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