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  • Alzheimer-type dementia  (5)
  • Key words Adrenal chromaffin cell  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Diffuse type of senile plaques in the cerebellum of Alzheimer-type dementia demonstrated byβ protein immunostain (1989)
    Springer
    Acta neuropathologica 77 (1989), S. 314-319 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer-type dementia ; Senile plaques ; β Protein ; Formic acid treatment ; Cerebellum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We studied senile plaques (SP) in the cerebella of six autopsied subjects with Alzheimer-type dementia (ATD) and ten non-ATD autopsied subjects between the ages of 78 and 90. Neither SP nor amyloid angiopathy (AA) was observed in any of the non-ATD subjects. In the four of the six ATD subjects, diffuse plaques in the molecular layer were seen as ill-defined areas of fine fibrillar materials by β protein immunostaining with formic acid pretreatment, the modified Bielschowsky stain, and periodic acid-methenamine silver (PAM) stain. The plaques were not visible with Bodian, Congo red, or periodic acid-Schiff stains. Compact plaques in the Purkinje cell or in the granular cell layers were found in three of the six subjects. Their amyloid core was often surrounded by areolar amyloid deposits. AA was observed in three of the six subjects. The argyrophilia of the diffuse and compact plaques, demonstrated by the modified Bielschowsky and PAM stains, became undetectable when the sections were first treated with formic acid. Such treatment made the plaques immunoreactive with β protein antiserum. The findings suggested that cerebellar diffuse plaques and compact plaques consist mainly of an amyloid component, and are characteristic of ATD.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00687584
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Distinctive, rapid, and easy labeling of diffuse plaques in the Alzheimer brains by a new methenamine silver stain (1990)
    Springer
    Acta neuropathologica 79 (1990), S. 569-572 
    Details
    ISSN: 1432-0533
    Keywords: Senile plaques ; Methenamine silver stain ; Alzheimer-type dementia ; Down's syndrome ; Amyloid β protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have developed a new methenamine silver (MS) stain for detecting diffuse plaques distinctively on paraffin-embedded tissue sections of Alzheimer-type dementia, Down'n syndrome, and mentally normal aged brains. This rapid and easy method selectively labels amyloid-related component of senile plaques, but not of kuru plaques found in Gerstmann-Sträussler syndrome. Our MS stain shows almost the same staining pattern as that of the β protein immunostaining with formic acid pretreatment. Therefore, new MS stain is appropriate to routine or screening studies for senile plaques including diffuse plaques.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00296119
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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
    Calcium channel subtypes in porcine adrenal chromaffin cells (1997)
    Springer
    Pflügers Archiv 434 (1997), S. 179-187 
    Details
    ISSN: 1432-2013
    Keywords: Key words Adrenal chromaffin cell ; Ca2+ current ; Ca2+ channel ; Nifedipine ; ω-Conotoxin GVIA ; ω-Agatoxin IVA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The effects of nifedipine, ω-conotoxin GVIA (ω-CgTx) and ω-agatoxin IVA (ω-AgTx) on Ca2+ currents, a 60-mM-K+-induced increase in intracellular Ca2+ concentration ([Ca2+]i) and catecholamine secretion were examined to clarify the subtypes of Ca2+ channels in cultured adrenal chromaffin cells from the pig. Nifedipine, ω-CgTx, and ω-AgTx inhibited Ca2+ currents in a dose-dependent manner, suggesting the presence of L-, N- and P-type Ca2+ channels. The maximal doses of nifedipine (10 μM), ω-CgTx (1 μM), and ω-AgTx (0.1 μM) inhibited Ca2+ currents to 85%, 22%, and 94% of control currents, respectively. The inhibitory effects of these three blockers were observed in the same cell, indicating that at least three subtypes of Ca2+ channels are present in porcine chromaffin cells. The increase in [Ca2+]i and catecholamine secretion induced by 60 mM K+ were inhibited equally by nifedipine (10 μM) and ω-CgTx (1 μM), but not by ω-AgTx (0.1 μM). These results suggest that L-, N- and P-type Ca2+ channels are present in porcine adrenal chromaffin cells, and that the major pathways of Ca2+ entry evoked by a high concentration of K+ are L- and N-type Ca2+ channels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004240050381
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  • 7
    Electronic Resource
    Electronic Resource
    Calcium channel current facilitation in porcine adrenal chromaffin cells (1998)
    Springer
    Pflügers Archiv 435 (1998), S. 781-788 
    Details
    ISSN: 1432-2013
    Keywords: Key words Adrenal chromaffin cell ; Ca2+ channel ; Facilitation ; Ba2+ current ; G protein ; GTPγS ; GDPβS ; ω-Conotoxin GVIA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  The mechanisms of depolarizing-prepulse-induced facilitation of Ca2+ channel current were investigated in a study of porcine chromaffin cells. The Ba2+ current evoked by a pulse to 0 mV was increased by a strong depolarizing prepulse (conditioning pulse), termed ”facilitation”. This facilitation increased with an increase in either the duration or the voltage of the conditioning pulse, and decreased with an increase in the interpulse interval. For example, the Ba2+ current was increased to 1.14 times the control (facilitation ratio) by a 150-ms conditioning pulse to +100 mV followed by a 10-ms interpulse interval. Forskolin, 8-bromo-adenosine 3′,5′-cyclic monophosphate (8-bromo-cAMP) and Rp-adenosine 3′,5′-cyclic monophosphothioate (Rp-cAMPS) did not affect the facilitation of the Ba2+ current, suggesting that a cAMP-dependent mechanism is not involved. Intracellular guanosine 5′-O-(3-thiotriphosphate) (GTPγS) decreased the Ba2+ current to 0.59 times the control and GDPβS increased it to 1.19. However, neither GTPγS nor guanosine 5′-O-(2-thiodiphosphate) (GDPβS) changed the amplitude of the Ba2+ current that was facilitated by the conditioning pulse. Thus, GTPγS increased the facilitation ratio to 2.05 and GDPβS decreased it to 1.05. Furthermore, the facilitation of the Ba2+ current was abolished by ω-conotoxin GVIA but not by either ω-agatoxin IVA or nifedipine. These results suggest that, in porcine chromaffin cells, there is a ω-conotoxin GVIA-sensitive N-type Ca2+ channel that is under the inhibitory control of a G protein, which can be relieved by a conditioning pulse.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004240050584
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