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  • 1
    ISSN: 0942-0940
    Keywords: Acoustic neuroma ; hearing preservation ; hormonal dependence ; histology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Pre-operative and postoperative auditory function was reviewed retrospectively in 98 patients with vestibular schwannomas. According to their hormonal status, women were categorized as “premenopausal” and “postmenopausal”. Before surgery, 48% of the women (65% premenopausal) and 16% of the men presented with sudden hearing loss. The degree of autitory function before operation was similar for women and men. Preservation of preoperative hearing was possible for 41% of the women (21% premenopausal) and 59% of the men. Further details of the surgery and the results of histopathological examination were also compared for women and men. Our results support substantial evidence that hearing preservation after surgery of vestibular schwannoma is easier to accomplish for men than for women. The finding of significantly more sudden hearing loss in premenopausal women may suggest a hormonal influence on tumour growth, which may also be partially responsible for the difference in hearing prognosis between women and men.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0533
    Keywords: Key words Pick’s disease ; Tau protein ; Axons
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Pick bodies and ballooned cells of Pick’s disease and the neurofibrillary lesions of Alzheimer’s disease are characterized by the presence of hyperphosphorylated microtubule-associated protein tau. Little is known about the mechanisms underlying tau hyperphosphorylation in Pick’s disease and the distribution of abnormal tau in affected neurons. We have used a panel of phosphorylation-dependent (AT270, AT8, AT180, 12E8, PHF-1, AT10 and Tau-1) and phosphorylation-independent anti-tau antibodies (N-tau 5 and 134) to stain brain tissue sections from subjects with Pick’s disease and Alzheimer’s disease. These antibodies labeled Pick bodies and neurofibrillary lesions in a similar way, with the exception of antibody 12E8, which stained a subset of neurofibrillary tangles, but no Pick bodies. Moreover, abundant AT8- and PHF-1-positive neuritic profiles were observed in cortical areas rich in Pick bodies, even in the complete absence of neurofibrillary lesions. Unlike the Gallyas-positive neuropil threads of Alzheimer’s disease, which were of variable diameter and covered by spiny appendages, neuritic profiles of Pick’s disease showed a regular diameter, appeared smooth and were Gallyas-negative. In contrast to Alzheimer’s disease, dendritic branches of neurons containing Pick bodies were not labeled by anti-tau antibodies. In the hippocampus, numerous tau-positive axon terminals were found along dendrites of the polymorphic layer of the dentate gyrus. Our results indicate that tau proteins in Pick’s disease and Alzheimer’s disease share similar phosphorylated residues, with the exception of serine 262, which is phosphorylated in Alzheimer tangles but not in Pick bodies or neuritic profiles. Furthermore, we show that hyperphosphorylated tau segregates to different neuronal compartments in the two diseases, with a somatoaxonal distribution in Pick’s disease and a somatodendritic distribution in Alzheimer’s disease.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0533
    Keywords: Key words Argyrophilic grain disease ; Tau protein ; phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Argyrophilic grains (ArG) and coiled bodies of argyrophilic grain disease (AgD) and the neurofibrillary lesions of Alzheimer’s disease (AD) share similar antigenic determinants, among them hyperphosphorylated microtubule-associated protein tau. Nothing is known about the mechanisms underlying tau hyperphosphorylation in AgD, the hyperphosphorylated sites or the intracellular distribution of abnormally phosphorylated tau. We have analysed brain tissue sections from 41 subjects with AgD with a panel of phosphorylation-dependent (AT270, AT8, Tau-1, AT180, 12E8, PHF-1 and AT100) and phosphorylation-independent anti-tau antibodies (N-tau 5, 304, 189 and 134). All antibodies labelled ArG, coiled bodies and neurofibrillary lesions, with the exception of antibody 12E8, which stained a subset of neurofibrillary tangles, but no ArG or coiled bodies. Most pyramidal neurons in areas rich in ArG showed diffuse granular tau labelling in cell bodies and dendrites. Only very few tau-positive cells also contained neurofibrillary tangles. Phosphorylation-dependent anti-tau antibodies also stained a felt-like network of Gallyas-negative filiform neurites in layer CA1 of the hippocampus and in layer pre-Β of the transentorhinal cortex. These results demonstrate a widespread hyperphosphorylation of tau protein in the somatodendritic domain of neurons in AgD, in addition to silver grains in the neuropil. Unlike in AD, tau hyperphosphorylation in the somatodendritic domain in AgD does not appear to be followed by neurofibrillary tangle formation, even in the presence of widespread ArG in the neuropil. Furthermore, our data suggest that no strict correlation exists between the presence or density of ArG in the limbic area and the occurrence of dementia.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-1920
    Keywords: Key words Cavernous haemangioma ; Foramen of Monro ; MRI ; Intraventricular mass
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Cavernous haemangiomas are most commonly found in the subcortical white matter, the pons and the external capsule. We present a case of a cavernous haemangioma that appeared as an intraventricular mass at the foramen of Monro. Despite the unusual location the diagnosis was established by MRI because of the typical appearance. The differential diagnosis included primary and secondary neoplasms at the foramen of Monro.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Der Pathologe 20 (1999), S. 159-168 
    ISSN: 1432-1963
    Keywords: Schlüsselwörter Silberkornkrankheit ; Alzheimer-Erkrankung ; Tau Protein ; Senile Plaques ; Hippocampus ; Key words Argyrophilic grain disease ; Alzheimer’s disease ; Tau protein ; Senile plaque ; Hippocampus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Summary Argyrophilic grain disease (AgD) constitutes one cause of late onset dementia and is histologically characterized by the presence of abundant argyrophilic grains and coiled bodies. Both abnormalities are found mainly in limbic structures, among them the sector CA1 of the hippocampus, the entorhinal cortex, and the amygdala. Using appropriate silver staining techniques, they are easily detectable and can easily be distinguished from neurofibrillary lesions of Alzheimer’s disease (i.e., tangles and threads). Although the histopathology of AgD is well characterized, the nosological status is still unclear because most cases of AgD are associated with Alzheimer-type changes. For some authors, therefore, AgD is considered a variant of Alzheimer’s disease rather than a distinct disease entity. The present review is aimed at presenting argyrophilic grain disease to a larger readership than just neuropathologists who are interested in neurodegenerative disorders. In this review we summarize morphological, immunohistochemical, clinico-pathological and genetic data obtained in more than 90 subjects with AgD. The main conclusions of this review are that AgD represents one of the most frequent, dementing disorders of old age and that it has to be clearly distinguished from Alzheimer’s disease.
    Notes: Zusammenfassung Die Silberkornkrankheit ist eine Demenzform des hohen Alters, die feingeweblich durch das Vorhandensein zahlreicher Silberkörner und sogenannter „coiled bodies” charakterisiert ist. Beide Veränderungen sind im limbischen System (vor allem CA1-Abschnitt des Hippocampus, entorhinale Rinde, Mandelkern) und im Hypothalamus lokalisiert. Die Silberkörner lassen sich mit Hilfe geeigneter Versilberungsmethoden einfach darstellen und sind gut von neurofibrillären Läsionen der Alzheimer-Erkrankung (Tangles und Threads) abgrenzbar. Obwohl die Silberkornkrankheit morphologisch ein gut definiertes Krankheitsbild darstellt, ist deren nosologische Zuordnung noch weitgehend unklar. Dies ist vor allem auf den Umstand zurückzuführen, daß sich in Gehirnen von Silberkornfällen neben den für diese Erkrankung typischen Veränderungen praktisch immer Läsionen vom Alzheimer-Typ finden. Einzelne Autoren meinen deshalb, die Silberkornkrankheit sei lediglich eine Variante der Alzheimer-Erkrankung. Ziel des vorliegenden Übersichtsartikels ist es, die Silberkornkrankheit einer breiten Leserschaft näherzubringen. Zu diesem Zweck berichten wir über die von uns an insgesamt 90 Fällen erhobenen morphologischen, immunhistochemischen, klinisch-pathologischen und genetischen Befunde. Unsere Resultate, zusammen mit aus dem Schrifttum gewonnenen Daten, lassen darauf schließen, daß die Silberkornkrankheit häufiger ist als bisher angenommen und in der Tat eine eigenständige neurodegenerative Erkrankung darstellt, die es von der Alzheimer-Erkrankung abzugrenzen gilt.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-0533
    Keywords: Key words Argyrophilic grain disease ; Dementia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In a previous study we reported on a late onset dementia which occurred in only half of the patients with argyrophilic grain disease (AgD) investigated. To find a correlation between the distribution of argyrophilic grains (ArG) and the occurrence of a late onset dementia, we examined the limbic area in 35 subjects who had ArG as the main neuropathological finding. A retrospective clinical analysis was performed by collecting information from hospital charts supplemented by standardized interviews based on DSM IV criteria for dementia. Sections from the rostral and caudal hippocampal regions, including the entorhinal/transentorhinal and parahippocampal cortex on both sides, were strained by the Gallays method. Nineteen subjects were diagnosed as demented according to these criteria; 16 were considered to have been cognitively normal. High numbers of ArG were observed in the anterior part of the CA1 subfield in all cases. However, the posterior half of CA1 was involved significantly more often and more severely in demented than in non-demented individuals (P 〈 0.01). Moreover, the distribution of ArG in the entorhinal/transentorhinal and parahippocampal cortex was more widespread in the group of demented patients (P 〈 0.05). These results show that the intellectual status of patients with AgD was related to the extension of ArG in the limbic area. We suggest that AgD is a progressive neurodegenerative disorder with early subclincial lesions in the anterior part of the hippocampal formation. To provide a more accurate clinicopathological correlation, the rostrocaudal extension of ArG in the limbic area should be evaluated in AgD cases.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0533
    Keywords: Key words Amyotrophy ; Axonopathy ; Neurofilaments ; Tau protein ; Transgenic mice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Coding region and intronic mutations in the tau gene cause frontotemporal dementia and parkinsonism linked to chromosome 17. Some of these mutations lead to an overproduction of tau isoforms with four microtubule-binding repeats. Here we have expressed the longest four-repeat human brain tau isoform in transgenic mice under the control of the murine Thy1 promoter. Transgenic mice aged 3 weeks to 25 months overexpressed human tau protein in nerve cells of brain and spinal cord. Numerous abnormal, tau-immunoreactive nerve cell bodies and dendrites were seen. In addition, large numbers of pathologically enlarged axons containing neurofilament- and tau-immunoreactive spheroids were present, especially in spinal cord. Signs of Wallerian degeneration and neurogenic muscle atrophy were observed. When motor function was tested, transgenic mice showed signs of muscle weakness. Taken together, these findings demonstrate that overexpression of human four-repeat tau leads to a central and peripheral axonopathy that results in nerve cell dysfunction and amyotrophy.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-0533
    Keywords: Key words Neurofibrillary tangles ; Microtubule-associated protein tau ; Heparan sulphate ; α-Synuclein ; Neurodegenerative diseases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Microtubule-associated protein tau forms neurofibrillary lesions in Alzheimer’s disease and several other neurodegenerative disorders, such as Niemann-Pick disease type C, subacute sclerosing panencephalitis, argyrophilic grain disease, myotonic dystrophy and motor neuron disease with neurofibrillary tangles. In this study we have compared the characteristics of tau pathology in these diseases using immunohistochemistry and phosphorylation-dependent and phosphorylation-independent anti-tau antibodies. The pattern of staining for heparan sulphate and α-synuclein was also investigated. We show that in all of these diseases tau deposits were stained by all anti-tau antibodies used, with the exception of argyrophilic grains which do not stain with antibody 12E8, confirming our previous findings. Heparan sulphate staining was present to a variable extent in all of these diseases, with the exception of subacute sclerosing panencephalitis, in which no staining was observed. Heparan sulphate staining coexisted with tau staining. In some cases it was more extensive than the tau staining. α-Synuclein staining was present in presynaptic terminals with the exception of one case of Alzheimer’s disease, in which α-synuclein-positive Lewy bodies were observed in the hippocampal formation. These findings indicate that tau deposits are antigenically similar in several neurodegenerative diseases and that tau staining is often associated with heparan sulphate staining, supporting the concept that heparan sulphate may be involved in the assembly of tau protein into filaments.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-0533
    Keywords: Key words Argyrophilic grain disease ; Hyperphosphorylated tau protein ; Glial fibrillary ; tangles ; Astrocytes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Argyrophilic grain disease (AgD), a frequent type of late onset dementia, is characterized by the occurrence of Gallyas-stained neuropil grains in the hippocampus, entorhinal cortex, amygdala and hypothalamus. High numbers of neurons containing hyperphosphorylated tau protein, but devoid of tangles, are encountered in areas rich in argyrophilic grains (ArGs). A third type of change consists of slender argyrophilic and tau-immunoreactive cytoplasmic inclusions in white matter oligodendrocytes, the coiled bodies. We now extend earlier studies on glial pathology in AgD (20 cases) and compare the results with glial changes in old age (10 cases) and Alzheimer’s disease (AD; 7 cases). Numerous non-argyrophilic, non-neuronal tau-positive stellate cells in the amygdala and anterior entorhinal cortex were consistently found in all of the 20 AgD cases but not in AD cases. Double-labelling experiments performed on paraffin sections with phosphorylation-dependent anti-tau antibody AT8, anti-glial fibrillary acidic protein and anti-CD44, revealed coexpression of these markers in stellate cells. The high expression of CD44 indicate that they probably correspond to reactive astrocytes. Unlike astrocytic plaques in corticobasal degeneration (CBD), where AT8 reactivity is accumulating in distal astrocytic processes, tau reactivity in AgD was found in all astrocytic cell compartments. The absence of glial fibrillary tangles further distinguished tau-labelled astrocytes in AgD from astrocytic plaques in CBD and tufted astrocytes in progressive supranuclear palsy (PSP). In contrast to AD and aged non-demented control cases tau-positive non-argyrophilic astrocytes represent a consistent finding in anterior limbic structures in AgD. Our findings point to a more widespread pathology of the glial cell population in AgD than previously supposed, and will be of further help in differentiating AgD from other neurodegenerative disorders, including AD, PSP, CBD and Pick’s disease.
    Type of Medium: Electronic Resource
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