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  • 1
    ISSN: 1432-0533
    Keywords: Key words Amyloid ; Apolipoprotein E ; Prion ; Squirrel monkey
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The interaction of various amyloid precursors and apolipoprotein E (apoE) is important for Congophilic amyloid formation. As for cerebral amyloidoses, although the correlation between amyloid β protein (Aβ) and apoE in Alzheimer’s disease (AD) has been clarified, the interaction of prion protein isoform (PrPsc) and apoE in several types of prion diseases (PDs) has not been examined in detail. ApoE colocalization has been confirmed in Congophilic PrPsc plaques, but to clarify the participation of apoE in the early stage of PDs, apoE deposition in immature lesions without Congophilic amyloid in PDs needs to be examined. In the present study two squirrel monkeys were inoculated with mouse PrPsc derived from sheep scrapie, and showed signs of severe spongiform degeneration. These lesions were immunohistochemically characterized as patchy perivacuolar and diffuse synaptic lesions without Congophilic amyloid. The central portion of the assemblies involving a few patchy perivacuolar lesions was detected by methenamine silver staining and appeared as a plaque-like lesion. ApoE was colocalized in all the plaque-like lesions and in half of the patchy perivacuolar lesions, but not in any diffuse synaptic lesions. These immunohistochemical characteristics indicated that apoE colocalization occurred in moderate mature lesions in PDs, and apoE might play an important role in the aggregation of PrPsc after a conformational change from cellular PrP isoform to PrPsc.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Colloid & polymer science 106 (1997), S. 204-208 
    ISSN: 1435-1536
    Keywords: Coil-globule transition ; collapsed transition ; self-organized nano-structure ; single chain dynamics ; hierarchical system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Folding transition from elongated coil into compacted globule in a single polymer chain is discussed based on the results of our recent theoretical and experimental studies. As the theoretical approach to this problem, Monte Carlo simulation on the coil-globule transition for a neutral stiff polymer chain has been performed. It has become clear that toroid and rod are the two representative structures as the product of folding transition: toroid is the most stable and rod is a kinetically forzen metastable structure. As for the experimental methodology, single molecular observation with fluorescence microscopy was applied for the coil-globule transition of a single duplex DNA. With this experimental tool, it became evident that individual DNA chains undergo first-order phase transition. In contrast to this, the ensemble of DNA has the characteristics of diffuse or continuous transition. In other words, the coil-globule transition in the ensemble of the chains appears a kind of cooperative transition without any discrete character in spite of the large discrete change in the effective volume of the individual DNA chains. In order to gain further insight on the manner of folding in single chains, we have also performed electron microscopic observation on the morphology of the collapsed DNA chains.
    Type of Medium: Electronic Resource
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