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  • 11
    Electronic Resource
    Electronic Resource
    Amyloid precursor protein of Alzheimer’s disease: evidence for a stable, full-length, trans-membrane pool in primary neuronal cultures (1999)
    Oxford, UK : Blackwell Science Ltd
    European journal of neuroscience 11 (1999), S. 0 
    Details
    ISSN: 1460-9568
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: We and colleagues have shown that the amyloid protein precursor of Alzheimer’s disease (APP) is distributed along the surface of neurites of fixed but nonpermeabilized neurons in primary culture in a segmental pattern, which shows colocalization with some markers of adhesion patches. This is in contrast to the diffuse pattern of immunoreactivity seen after permeabilization. We have also recently demonstrated that the APP in these surface patches is likely to be integral to the membrane rather than secreted and re-adsorbed, based on alkali stripping experiments and on soluble APP adsorption experiments. Total cellular APP has previously been shown to have a short half-life of ≈ 30–60 min. We confirm this in neurons in primary culture in pulse-chase experiments using short labelling times. Additionally, we provide evidence that a separate, stable pool of neuronal APP can be demonstrated in pulse-chase experiments using long labelling times. Experiments involving inhibition of protein synthesis suggest that this corresponds with the surface, segmental pool. Metabolic labelling followed by surface biotinylation and two-stage precipitation demonstrates that the surface APP is trans-membrane and full-length (not carboxyl-terminal truncated), and confirms that the surface APP belongs to the stable pool. This two-stage procedure is necessary as the surface APP appears to be present in low copy number, and is difficult to detect by direct labelling. This information is consistent with a role for APP in stable cell-matrix or cell–cell interactions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1460-9568.1999.00599.x
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  • 12
    Electronic Resource
    Electronic Resource
    Alzheimer's disease The ins and outs of amyloid- β (1997)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 389 (1997), S. 677-678 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The devastating consequences of Alzheimer's disease — marked by extracellular senile plaques with fibrils of amyloid-β peptide (Aβ) and intraneuronal tangles of polymerized tau protein — are experienced by more and more elderly people in the Western world. The latest step ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/39479
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  • 13
    Electronic Resource
    Electronic Resource
    Spongiform encephalopathies Tracking turncoat prion proteins (1997)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 388 (1997), S. 228-229 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The persistent fear that bovine spongiform encephalopathy (BSE, or ‘mad cow’ disease) has crossed species barriers into humans and other animals has increased the pressure on scientists to come up with a molecular explanation for infectivity. Two in vitro experiments, one assaying the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/388228a0
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  • 14
    Electronic Resource
    Electronic Resource
    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
    Keywords: Key words Alzheimer’s disease ; Amyloid ; precursor-like protein 1 ; Amyloid precursor protein ; Plaques
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004010050745
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  • 15
    Electronic Resource
    Electronic Resource
    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
    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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  • 16
    Electronic Resource
    Electronic Resource
    A structural somatic variant of the Kk antigen is generated by point mutation (1985)
    Springer
    Immunogenetics 22 (1985), S. 35-48 
    Details
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We have previously selected structural variants of the Kk antigen from a (C3 × D2)F1 T-cell lymphoma. Those mutants were identified by the loss of certain epitopes defined by monoclonal antibodies. The variant Kk molecule from HK13.S3 cells is no longer recognized by 40% of the trinitrophenyl-specific, Kk-restricted cytotoxic T lymphocytes. Here we report on the primary structure of the altered Kk molecules from the cell line HK13.S3. Comparison with the parental Kk reveals a single base pair exchange, GCG to GTG, that results in an alanine to valine exchange in position 40 of the protein. This observation emphasizes that minor structural alterations in class I molecules may have a strong effect on the H-2-restricted T-cell response.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00430592
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  • 17
    Electronic Resource
    Electronic Resource
    Specific binding of the alzheimer βA4 amyloid precursor to collagen, laminin, and heparin (1992)
    Springer
    The protein journal 11 (1992), S. 398-399 
    Details
    ISSN: 1573-4943
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01673756
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  • 18
    Electronic Resource
    Electronic Resource
    N-terminal sequence of phage lambda repressor (1976)
    Springer
    Molecular genetics and genomics 147 (1976), S. 115-117 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Lambda repressor was purified from an E. coli strain which produces 150 times more lambda repressor than a single lysogen. The sequence of the fifty N-terminal residues was determined by automated Edman degradation. It contains 43% of all arginine and lysine residues of the chain and constitutes according to the genetic data of Oppenheim et al. (1975) a substantial part of the operator-DNA-binding site of the repressor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00337945
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  • 19
    Electronic Resource
    Electronic Resource
    Recognition of two initiation codons for the synthesis of phage fd gene 2 protein (1980)
    Springer
    Molecular genetics and genomics 180 (1980), S. 489-494 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Bacteriophage fd gene 2 protein was specifically labeled with radioactive amino acids and was isolated from membranous cell structures as an apparently homogenous protein. Amino acid sequence analysis revealed that the protein was initiated at two distinct AUG codons close to the ribosome binding site. The two resulting translation products were found to begin with a deformylated methionine residue. Initiation at the first signal was used for 90% of the chains and at the second signal for 10% of the sequenced molecules. The use of one or the other chain start may influence functions of gene 2 protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268051
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