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  • Dementia  (3)
  • Polymer and Materials Science  (3)
  • Amyloid β/A4 protein  (2)
  • Neuropil threads  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Presence of apolipoprotein E on extracellular neurofibrillary tangles and on meningeal blood vessels precedes the Alzheimer b-amyloid deposition (1994)
    Springer
    Acta neuropathologica 88 (1994), S. 413-419 
    Details
    ISSN: 1432-0533
    Keywords: Key words Amyloid β protein ; Alzheimer's disease ; Dementia ; Apolipoprotein E
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The localization of apolipoprotein E (ApoE) has been examined immunohistochemically in the autopsied brains of middle-aged and old-aged control subjects, with and without amyloid β protein (Aβ) deposits, and of Alzheimer's disease patients. Senile plaques were consistently labeled with ApoE antiserum even in the very early stage of senile plaque formation seen in the fifth decade. In the cerebellar molecular layer, small dots of ApoE immunoreactivity, which were prominent in the Alzheimer's disease subjects, were observed in addition to immunoreactivity in diffuse plaques. ApoE antisera labeled all of the extracellular neurofibrillary tangles (NFT), whereas only a small minority of extracellular NFT were positive for Aβ. A punctate pattern of ApoE immunoreactivity was seen at the media of the meningeal vessels lacking amyloid, when senile plaques were present in the nearby cortex. In the early stage of amyloid angiopathy, the distribution of ApoE immunoreactivity was much more extensive than that of Aβ positivity. These findings suggest that ApoE accumulates in the early stage of senile plaque formation and, furthermore, that ApoE accumulation precedes Aβ deposition in extracellular NFT and amyloid angiopathy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00389492
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  • 2
    Electronic Resource
    Electronic Resource
    Diffuse plaques associated with astroglial amyloid β protein, possibly showing a disappearing stage of senile plaques (1998)
    Springer
    Acta neuropathologica 95 (1998), S. 217-222 
    Details
    ISSN: 1432-0533
    Keywords: Key words Amyloid β protein ; Alzheimer’s disease ; Dementia ; Astrocytes ; Senile plaques
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract To clarify whether senile plaques disappear, we examined amyloid β protein (Aβ) deposits in non-demented subjects, and found novel diffuse plaques associated with astroglial Aβ. Formalin-fixed paraffin-embedded sections from cortical areas were immunolabeled with a panel of Aβ antibodies, and astroglial and microglial markers. Cerebral Aβ deposition was primarily found as diffuse plaques (DP) in these subjects. A subset of DP was associated with clusters of intensely Aβ-positive small granules. The clusters, which were located just adjacent to astroglial nucleus, had the characteristics of lipofuscin granules and, therefore, were quite different from “small stellate deposits”. Substantial amounts of Aβ-positive granules were found inside astrocytes by dual labeling of Aβ and glial fibrillary acid protein, and the majority of astroglial Aβ immunoreactivity was located on lipofuscin granules. Aβ-positive granules lacked immunoreactivity with antisera for the N-terminal region of Aβ. These peculiar DP showed a much weaker staining than ordinary DP. The DP associated with astroglial Aβ were found in about one third of the subjects, although the density varied widely among individuals. From these findings, we propose that DP, which are associated with the N-terminal truncated Aβ in astrocytes, represent the disappearing stage of senile plaques.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004010050790
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  • 3
    Electronic Resource
    Electronic Resource
    Ultrastructure of diffuse plaques in senile dementia of the Alzheimer type: comparison with primitive plaques (1991)
    Springer
    Acta neuropathologica 82 (1991), S. 13-20 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer-type dementia ; Senile plaques ; Amyloid β/A4 protein ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We compared the ultrastructure between diffuse and primitive plaques in the brains of senile dementia, using pairs of routine electron microscopic ultrathin sections and adjacent semithin sections, which were immunolabeled for β protein. In the frontal cortex, amyloid fibrils were rarely seen in a minority of diffuse plaques, suggesting an initial stage of the diffuse plaques. A majority of the diffuse plaques had electrondense material and/or amyloid fibrils between cell processes in part of but not the entire β/A4-immunoreactive areas. Small degenerating neurites were often seen with apparent amyloid fibrils in the diffuse plaques, and these were considered to be in an advanced stage. The size and number of degenerating neurites were proportional to the amount of amyloid. Bundles of amyloid fibrils were occasionally surrounded by astroglial processes forming gap junctions. Neurons were found within some diffuse plaques, but capillaries were rarely seen. In contrast, in the temporal cortex, the diffuse plaques were smaller, and even these small ones had apparent amyloid fibrils. The amount of amyloid correlated significantly with plaque size in the temporal cortices, but not in the frontal cortices. Most of the diffuse plaques of the frontal lobe remained as advanced diffuse plaques (apparent amyloid with occasional astroglia and some degenerating neurites) for a long time, and did not transformed into primitive plaques, whereas the temporal diffuse plaques tended to transform into primitive plaques.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310918
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  • 4
    Electronic Resource
    Electronic Resource
    Ultrastructure of the neuropil threads in the Alzheimer brain: their dendritic origin and accumulation in the senile plaques (1990)
    Springer
    Acta neuropathologica 80 (1990), S. 368-374 
    Details
    ISSN: 1432-0533
    Keywords: Neuropil threads ; Alzheimer-type dementia ; tau protein ; Palred helical filaments ; Senile plaques
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Thread-like structures immunoreactive with paired helical filaments and tau antisera were demonstrated as mesh-works in the neocortices of five brains with Alzheimer-type dementia, but not in those of five normal aged control brains. The ultrastructure of the threads was examined using paired routine electron microscopic ultrathin sections and adjacent 0.4-μm-thick semithin sections, immunostained for β protein. Outside the β protein-positive senile plaques, neuropil threads appeared sporadically as small slender neurites, containing either regularly constricted or straight filaments. These neurites often showed dendritic profiles. Similar threads were also seen within the senile plaques. The threads were accumulated in amyloid fibril-rich primitive plaques, but not in amyloid fibril-poor diffuse plaques. The presence of these threads was closely associated with neurofibrillary tangle formation. Our findings suggest that wide-spread change of the neuropil neurites, neuropil threads or curly fibers, both outside and inside of the senile plaques are dendritic in origin and play an important role in the clinical manifestation of dementia.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307689
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  • 5
    Electronic Resource
    Electronic Resource
    Extracellular neurofibrillary tangles associated with degenerating neurites and neuropil threads in Alzheimer-type dementia (1991)
    Springer
    Acta neuropathologica 81 (1991), S. 603-609 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer-type dementia ; Neurofibrillary tangles ; Neuropil threads ; Amyloid β/A4 protein ; Astroglia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We examined the cellular components of extracellular neurofibrillary tangles (E-NFT) in the hippocampal areas in cases with Alzheimer-type dementia. Immunohistochemically, the E-NFT were labeled for the C terminus of tau and glial fibrillary acidic protein. Moreover, the majority of the E-NFT was associated with intensely argyrophilic rods and with tau-and ubiquitin-immunoreactive dots. Ultrastructurally, the E-NFT consisted mainly of extracellular paired helical filaments (PHF) and astroglial processes. The extracellular PHF tended to be straighter and thinner. One third of the E-NFT was associated with small degenerating neurites containing many dense bodies and with neuropil threads containing PHF. These findings suggested that extracellular PHF promote both intense astroglial reaction and neuritic alteration, and that the E-NFT are continuously changing their morphology.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00296369
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  • 6
    Electronic Resource
    Electronic Resource
    A variety of cerebral amyloid deposits in the brains of the Alzheimer-type dementia demonstrated byβ protein immunostaining (1988)
    Springer
    Acta neuropathologica 76 (1988), S. 541-549 
    Details
    ISSN: 1432-0533
    Keywords: β Protein ; Senile plaques ; Amyloid ; Alzheimer ; Dementia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We studied cerebral amyloid deposits in the hippocampal area immunohistochemically, using antiserum to syntheticβ peptide (1–28) in 66 patients with or without dementia and aged 17 to 91 years old. Senile plaques (SP) and amyloid angiopathy (AA) were detected in 36 (55%) and 19 (29%) patients, respectively. Also, cerebral amyloid deposits from the brains of seven patients with dementia and five patients without were studied in serial sections stained with Bodian, modified Bielschowsky, Congo red, andβ protein immunostain. In the patients with Alzheimer-type dementia (ATD) diffuse plaques, typical of this group, were stained withβ protein antiserum but not with Bodian stain, because the plaques were devoid of abnormally swollen neuritic processes. The diffuse plaques often contained one or more neuronal cell bodies. As well as primitive and classic plaques and AA, theβ protein immunostain demonstrated small deposits among the SP, small stellate deposits of layer 1, subpial fibrillar deposits, and focal cribriform deposits of parasubiculum, which may be new types of amyloid deposits. Amyloid plaques within the subcortical white matter were only found in ATD brains. In the non-demented patients various kinds of SP, including diffuse and compact ones, were immunostained. They tended to be small and few.β protein immunostain with formic acid pretreatment is a useful method for the identification of a variety of senile cerebral amyloid deposits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00689591
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  • 7
    Electronic Resource
    Electronic Resource
    Synthese und eigenschaften einiger höhergliedriger cyclischer ätheracetale (1977)
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 178 (1977), S. 3191-3195 
    Details
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Optimized syntheses of 1,3,6,9-tetraoxacycloundecane (2), 1,3,6,9,12-pentaoxacylotetradecane (3), and 1,3,6,9,12,14,17,20-octaoxacyclodocosane (4) as well as some physical and chemical properties and the proof of structure are reported.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/macp.1977.021781202
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  • 8
    Electronic Resource
    Electronic Resource
    Preparation and characterization of macroporous polystyrene resins containing ethynyl groups and transition metal acetylide complexes (1987)
    Bognor Regis [u.a.] : Wiley-Blackwell
    Journal of Polymer Science Part A: Polymer Chemistry 25 (1987), S. 2281-2288 
    Details
    ISSN: 0887-624X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Ethynylated polystyrene resins were prepared as functionalized polymer supports by the iodination reaction of macroporous polystyrene resins and reacted with transition metal diethynyl complex (Mt = Ni) and metal halides (Mt = Rh, Pd, and Pt) in a basic solvent using cuprous iodide as a catalyst to obtain macroporous polystyrene resins containing organotransition metals. The distribution of the metal acetylide complexes in the modified macroporous resins was determined by an electron probe microanalyzer. A gradient in the transition metal distribution was observed in any case of the modified resins. The stability of the organotransition metal complexes in the polymer matrix could be compared with a low molecular weight analogous complex quantitatively.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/pola.1987.080250824
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  • 9
    Electronic Resource
    Electronic Resource
    Adsorption mechanism of heavy-metal ion by microspherical tannin resin (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 45 (1992), S. 1463-1472 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: The spherical tannin resin (STR) resulting from the reaction between Mimosa (Acacia Mollissima) tannin (condensed-type tannin) and formaldehyde was very porous. The specific surface area of the STR made from 37.5% of tannin was 139.2 m2/g (1 g of the resin in this is wet resin corresponding to 1 g of dried resin). Properties such as specific surface area and average pore radius could be controlled by adjusting the tannin concentration. The apparent activation energy of Cu2+ ion adsorption by STR was 3 kcal/mol, and that of Cr6+ ion was 2 kcal/mol. Since the energy was small, we concluded that the adsorption of metal ions was not influenced significantly by the adsorption temperature. The heat of adsorption for Cu2+ ions was only 1.6 kcal/mol, which suggests that the adsorption was a physical phenomenon. It was thought that the diffusion of heavy-metal ions into the porous resin was the rate-determining step of the adsorption since the elution profile of the column method was analogous to the profile of active carbon, which adsorbs physically, the heavy metal ions gradually leaking through the column. The surface and cross section of the STR were observed before and after Cu2+ ion adsorption with the scanning electron microscope. The pores of the spherical resin were clogged with adsorbed copper, suggesting that the Cu2+ ions were adsorbed during the formation of a multimolecular layer. The adsorption may therefore have been due to physical attractive forces. The rate of adsorption and adsorption isotherms of Cu2+ ions from copper salts having various anions was found to vary depending on the type of anion. These phenomena were not thought to be due to the properties of the spherical resin but to differences in the hydration state of copper ions.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1992.070450815
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