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Reverse relationship between β-amyloid precursor protein and β-amyloid peptide plaques in Down’s syndrome versus sporadic/familial Alzheimer’s disease (1999)

Egensperger, Rupert ; Weggen, Sascha ; Ida, Nobua ; [et al.]

Springer

Acta neuropathologica 97 (1999), S. 113-118

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ISSN: 1432-0533

Keywords: Keywords Alzheimer’s disease ; Down’s syndrome ; β-Amyloid precursor protein ; β-Amyloid peptide

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/s004010050963

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A synthetic substrate assay for the gamma-secretase of the β-A4 amyloid of alzheimer's disease (1995)

Evin, Geneviève ; Beyreuther, Konrad ; Masters, Colin L.

New York, NY [u.a.] : Wiley-Blackwell

Journal of Peptide Science 1 (1995), S. 132-139

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ISSN: 1075-2617

Keywords: βA4 amyloid peptide ; radiometric assay ; transmembrane peptide ; reverse-phase TLC ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: 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).

Additional Material: 4 Ill.