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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 67 (1985), S. 272-278 
    ISSN: 1432-0533
    Keywords: Amyloidosis ; Amyloid fibril protein ; Creutzfeldt-Jakob disease ; Senile dementia of Alzheimer type ; Autoclaving
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The permanganate method, the immunoperoxidase method, and a newly developed autoclave method were used to distinguish different types of amyloid fibril proteins in formalin-fixed, paraffinembedded tissue sections. All tissues from permanganate-sensitive cases (AA type) lost the affinity of Congo red and green birefringence under polarized light after incubation with special autoclave treatment. AL type systemic amyloidosis and amyloid plaques of CJD and GSS were permanganate-resistant, but decreased markedly the affinity of Congo red after prolonged autoclaving. On the other hand, prealbumin type systemic amyloidosis and senile plaques of SDAT were resistant to both permanganate oxidation and prolonged autochlaving. Thus, amyloid plaques of CJD and GSS are identical to AL type in systemic amyloidosis, and senile plaques are similar to the prealbumin type. However, anti-prealbumin antiserum did not stain senile plaque amyloid. The anti-human P component stained positively systemic amuyloids and cerebral amyloid plaques of SSE, but failed to stain senile plaques of SDAT. Therefore, the amyloid fibril protein of senile plaues is apparently different from other types of amyloid depositions. Amyloid plaques of SSE are different from senile plaques not only with regard to fibril proteins, but also to globular protein in the amyloid.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 79 (1989), S. 129-136 
    ISSN: 1432-0533
    Keywords: Ferritin ; Microglia ; Immunohistochemistry ; Scrapie-associated fibrils
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary An immunohistochemical analysis of formalin-fixed, paraffin-embedded brain sections was performed with antisera against holoferritin and the light(L)-subunit of ferritin. Sections immunostained using anti-glial fibrillary acidic protein (GFAP), Ricinus communis agglutinin-1 (RCA-1) stain for microglia and iron stain (Berlin blue stain) were compared. The L-subunit of ferritin was purified from normal human spleen according to the modified scrapie-associated fibrils purification, and the antiserum was raised in a rabbit. Both ferritin antisera positively stained resting and, more markedly, reactive microglia, both of which were also stained with RCA-1 but not with GFAP. Ferritin-positive resting microglia were seen more abundantly in cerebral and cerebellar cortices than in white matter. The advantages of ferritin antisera over RCA-1 are as follows. (1) RCA-1 heavily stains blood vessels, while anti-ferritin does not, hence the microglial cells are more readily visualized with ferritin immunohistochemistry. (2) Reactive microglia and macrophages are more strongly stained with anti-ferritin. (3) The staining intensity of ferritin is independent of the length of tissue fixation in formalin. However, anti-ferritin is inferior to RCA-1 in staining resting microglia with a scanty cytoplasm, especially in the white matter, probably because the former recognizes cytoplasmic components, while the latter recognizes cell membrane. Iron stain only gave a reaction to microglial cells in brains with neurosyphilis and to hemosiderin-laden macrophages. Thus, in addition to RCA-1, ferritin antisera are useful as a microglia marker in formalin-fixed, paraffin-embedded sections.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 82 (1991), S. 260-265 
    ISSN: 1432-0533
    Keywords: Immunohistochemistry ; Gerstmann-Sträussler syndrome ; Alzheimer's disease ; Kuru plaque ; Senile plaque
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We investigated paraffin-embedded brain sections from three patients with Gerstmann-Sträussler syndrome and three patients with Alzheimer's disease or senile dementia of Alzheimer type using anti-human prion protein antisera and anti-β/A4 protein antisera after protein denaturation treatments. After incubation with guanidine-thiocyanate, trichloroacetate, and phenol, the immunoreactivity of kuru plaques and senile plaques was enhanced to the same level as the formic acid treatment. These treatments revealed small compact amyloid deposits, amyloid deposits surrounding the plaque cores, and diffuse plaques. Most of these chemicals changed the congophilia of both amyloids. It is possible that these treatments denature amyloid fibril proteins and break down the structure of amyloid fibrils, thus revealing buried epitopes.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-0533
    Keywords: Modified tau ; Subcortical nuclei ; Alzheimer's disease ; Progressive supranuclear palsy ; Normal brain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Tau-positive neurons relating to neurofibrillary tangles and diffuse cytoplasmic stainings were quantitatively examined in the brains of 61 nondemented persons including 24 age-matched controls, 10 patients with Alzheimer's disease (AD) and 5 with progressive supranuclear palsy (PSP). In nondemented persons, the locus ceruleus (LC) was found to contain tau-positive neurons initially in persons in their 30s, whereas the hippocampus contained such neurons initially in persons in their 40s. The LC had a higher incidence and density than the hippocampus in almost all age classes. As neuronal tau accumulation is considered a histological change occurring with normal aging, the LC might be involved in the earliest aging in the normal brain. In AD there was conspicuous tau accumulation in the same sites which were vulnerable to tau accumulation in the age-matched controls. In PSP tau accumulated heavily in a set of sites different from the age-matched controls and AD. Thus, subcortical tau accumulation in AD is increased far more than that under normal aging process, while that in PSP is not simply in an increased state of the normal aging process.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-0533
    Keywords: Creutzfeldt-Jakob disease ; Prion protein ; Intracellular accumulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Amyloid plaques in Creutzfeldt-Jakob discase, kuru, and Gerstmann-Sträussler-Scheinker syndrome are known to contain an abnormal isoform of a cellular protein, the prion protein (PrP). The prion protein in its normal cellular isoform is a membranebound glycoprotein of unknown function. The mechanisms causing a modification of PrP and accumulation in amyloid plaques are unknown. Here we present a case of Creutzfeldt-Jakob disease with widespread deposition of immunohistochemically labeled PrP in the internal granular layer of the cerebellum. Immunohistochemically labeled PrP was deposited in delicate granules, which often were associated with cellular processes or the cytoplams of undefined cells, or diffusely deposited in the neuropil.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-0533
    Keywords: Prion protein ; β protein ; Amyloid ; Immunohistochemistry ; Immuno-electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We examined paraffin-embedded brain sections from three patients with Creutzfeldt-Jakob disease (CJD) and four patients with Gerstmann-Sträussler syndrome (GSS) who also had β protein deposits in the brains. Immunostaining using anti-prion protein (PrP) and anti-β protein coupled with formic acid pretreatment, revealed PrP deposits and β protein deposits, respectively. In all four GSS patients examined, sequential double immunostaining and single immunostaining in serial sections or simultaneous double immunofluorescence revealed the colocalization of PrP and β protein in the same amyloid plaques. The plaques labeled with both antibodies were designated as β-PrP plaques. Small kuru plaques of less than 15 μm in diameter were rarely found to coexist with β deposits. The percentages of β-PrP plaques in larger kuru plaques were not constant among the four GSS patients. The colocalization patterns of both deposits were observed as being roughly of two types as follows: (1) diffuse β protein deposits located around the PrP core; and (2) a β protein core and PrP core simultaneously existing in one amyloid plaque. Under an electron microscope, we were able to confirm the presence of both β protein and PrP in a single plaque in four GSS patients older than 60 years old. In contrast, no colocalization of either deposits was seen in the amyloid plaque core fractions of a young GSS patient who had no β protein deposits, even at the electron microscopic level. Therefore, the colocalization of both proteins in a single plaque is believed to be age-related and incidental in GSS patients but suggests a similar morphogenesis of both amyloid deposits.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0533
    Keywords: Prion protein ; Amyloid ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We examined 7 patients with Creutzfeldt-Jakob disease (CJD) with a methionine-to-valine change at prion protein (PrP) codon 129 (CJD129 patients). These CJD129 patients did not have either a condon 117 or 198 point mutation. For comparison, we also examined 7 patients with Gerstmann-Sträussler syndrome (GSS) with a proline-to-leucine change at PrP codon 102 (GSS102 patients) and 13 patients without any known mutations at codons 102, 117, 129, 178, or 200 (CJDwild patients). CJD129 patients had a long clinical duration and ataxia at onset, but rarely had any periodic synchronous discharge in their electroencephalogram. Unlike CJDwild patients, all CJD129 patients have typical congophilic PrP plaques in their brain. These clinicopathological findings were similar to those of GSS102. However, the distribution and morphology of PrP deposits revealed by immunohistochemistry were different between CJD129 and GSS102. In GSS102 more numerous and various types of PrP plaques are seen throughout the brain, while in CJD129 patients a unicentric core was the major feature of PrP plaques. The change in codon 129 influences the clinical course and pathological findings in CJD.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 76 (1988), S. 212-215 
    ISSN: 1432-0533
    Keywords: Amyloidosis ; Cerebral amyloid ; Cerebral amyloidoma
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The brain of a 60-year-old patient with bronchial carcinoma presented a focal amyloid deposit in the white matter associated with myelin and axonal destruction. An additional lesion was found in the basal ganglia. This silent focal intracerebral accumulation of amyloid substance may be a prestadium of a “cerebral amyloidoma”. The histochemical chemical and immunohistochemical analysis of the accumulated amyloid indicated that it may belong to a novel type of amyloid.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-0533
    Keywords: Creutzfeldt-Jakob disease ; Amyloid angiopathy ; Prion protein ; Immunohistochemistry ; Experimental transmission
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary It was difficult to make a definite pathological diagnosis in a 73-year-old man with Creutzfeldt-Jakob disease (CJD) due to extensive amyloid angiopathy which lacked any severe spongiform changes. Immunostaining using anti-prion protein (PrP) antibody revealed fine granular deposits in the gray matter, after hydrolytic autoclaving pretreatment on tissue sections. Western blotting also revealed an abnormal isoform of PrP, but PrP gene analysis did not show any abnormalities. The primary transmission experiments were repeated three times and induced spongiform encephalopathy in a few mice after a long incubation period.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-0533
    Keywords: Alzheimer's disease ; Creutzfeldt-Jakob disease ; Prion protein ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We report here a 75-year-old-male with a slowly progressive dementia of 5-year duration along with a rapid exacerbation of symptoms in the terminal 3 months. Neuropathological examinations revealed findings consistent with conspicuous Alzheimer's disease and mild Creutzfeldt-Jakob disease (CJD). The plaque amyloid was exclusively composed of β-protein. The immunohistochemistry of prion protein using hydrolytic autoclaving pretreatment showed diffuse gray matter stainings in the sections of both the cerebral and cerebellar cortices. This method was thus considered useful in confirming the diagnosis of CJD for this case.
    Type of Medium: Electronic Resource
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