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  • 1
    Digitale Medien
    Digitale Medien
    Distribution of cortical neurofibrillary tangles in progressive supranuclear palsy: A quantitative analysis of six cases (1992)
    Springer
    Acta neuropathologica 84 (1992), S. 45-51 
    Details
    ISSN: 1432-0533
    Schlagwort(e): Alzheimer's disease ; Cerebral cortex ; Neurofibrillary tangles ; Progressive supranuclear palsy ; Tau protein
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary Progressive supranuclear palsy is characterized neuropathologically by the presence of high densities of neurofibrillary tangles in several subcortical structures. In some cases, neurofibrillary tangles have also been described in the cerebral cortex. We performed a quantitative regional and laminar analysis of the distribution of these lesions in six cases of progressive supranuclear palsy. We observed that the neurofibrillary tangle distribution in the cerebral cortex was largely confined to the hippocampal formation. In particular, in all the cases neurofibrillary tangles were observed in the granule cell layer of the dentate gyrus. In the prefrontal and inferior temporal cortex, neurofibrillary tangles were predominantly distributed in layers II and III. In addition, there were moderate-to-high neurofibrillary tangle densities in the primary motor cortex. This localization pattern contrasts with the neurofibrillary tangle distribution observed in the cerebral cortex of Alzheimer's disease cases, where tangles are denser in layer V than in layer III, and where the primary motor cortex and the dentate gyrus are usually not involved. These results suggest that specific elements of the cortical circuitry might be differentially vulnerable in progressive supranuclear palsy as compared to Alzheimer's disease.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00427214
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  • 2
    Digitale Medien
    Digitale Medien
    Hyperphosphorylated tau proteins differentiate corticobasal degeneration and Pick’s disease (1996)
    Springer
    Acta neuropathologica 91 (1996), S. 351-359 
    Details
    ISSN: 1432-0533
    Schlagwort(e): Key words Cytoskeleton ; Microtubule-associated ; proteins ; Neurodegenerative disorders ; Protein ; phosphorylation ; Western blotting
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract In neurodegenerative disorders, hyperphosphorylated tau proteins aggregate into abnormal filaments. In the present study, tau protein alterations were studied in one corticobasal degeneration and seven Pick’s disease cases using specific immunological probes. The typical lesions of corticobasal degeneration and Pick’s disease were revealed by immunohistochemistry, including the presence of Pick bodies and achromatic swollen neurons, neuritic alterations, and neurofibrillary tangles. Tau-immunoreactive glial tangles were also observed. By immunoblotting, the case of corticobasal degeneration was characterized by the tau profile previously reported to occur in progressive supranuclear palsy with an intense labeling of the two tau 64 and 69 bands, while tau 55 was not visualized. In Pick’s disease cases with Pick bodies and neurofibrillary tangles, a tau triplet similar to that encountered in Alzheimer’s disease (tau 55, 64 and 69) was detected. Furthermore, a particular tau profile was found in four Pick’s disease cases showing only Pick bodies and no neurofibrillary tangles. In these cases, tau 55 and 64 were strongly immunoreactive, whereas tau 69 was almost unlabeled. These differences are likely to be related to particular pools of tau isoforms present within the degenerating neurons. Since there is a great diversity of neurodegenerative disorders with substantial clinical and neuropathological overlap, the electrophoretic profile of tau proteins could represent a useful marker for the type of neurodegeneration.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s004010050436
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  • 3
    Digitale Medien
    Digitale Medien
    Cellular distribution of the iron-binding protein lactotransferrin in the mesencephalon of Parkinson’s disease cases (1996)
    Springer
    Acta neuropathologica 91 (1996), S. 566-572 
    Details
    ISSN: 1432-0533
    Schlagwort(e): Key words Ferritin ; Free radicals ; Oxidative stress ; Neurodegenerative disorders ; Transferrins
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Changes in the distribution of the iron-binding protein lactotransferrin have recently been described in the central nervous system during a variety of neurodegenerative disorders. To investigate whether lactotransferrin is associated with the neuropathological changes that characterize Parkinson’s disease, we analyzed the distribution of this protein in the mesencephalon of neurologically normal individuals and patients affected with Parkinson’s disease using quantitative immunohistochemical methods. High levels of lactotransferrin were observed in a large population of neurons in the substantia nigra of control cases. Lactotransferrin-positive neurons were severely affected by the neurodegenerative process that occurs in Parkinson’s disease as indicated by a severe decrease in the number of immunolabeled neurons in all of these cases. Quantitative analysis also demonstrated higher immunolabeling levels of lactotransferrin in the surviving neurons in the substantia nigra and ventral tegmental area of Parkinson’s disease cases compared to control cases. These results suggest that lactotransferrin may participate actively in the mechanism of neuronal degeneration in Parkinson’s disease.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s004010050468
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  • 4
    Digitale Medien
    Digitale Medien
    Phosphorylated serine422 on tau proteins is a pathological epitope found in several diseases with neurofibrillary degeneration (1999)
    Springer
    Acta neuropathologica 97 (1999), S. 221-230 
    Details
    ISSN: 1432-0533
    Schlagwort(e): Key words Neurodegenerative disorders ; Neurofibrillary tangles ; Phosphorylation ; Serine422 ; Tau protein
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract Neuronal inclusions with bundles of abnormal filaments made of tau polymers are found in numerous diseases with neurofibrillary degeneration. Tau proteins are the basic components of paired helical filaments (PHF) in Alzheimer’s disease (AD), and are abnormally phosphorylated. A disease-specific phosphorylation site at serine422 was demonstrated on PHF, but not on tau proteins from biopsy-derived brain samples. In the present study, we report the characterization of a polyclonal antibody (988) against the serine422 phosphorylation site. By using biochemical and immunohistochemical methods, we confirmed that it is not found on tau proteins from biopsy- or autopsy-derived control samples, and we investigated the presence of this epitope on tau proteins in several neurodegenerative disorders, including AD, Down syndrome (DS), Guamanian amyotrophic lateral sclerosis/Parkinsonism-dementia complex (ALS/PDC), corticobasal degeneration (CBD), progressive supranuclear palsy (PSP), postencephalitic parkinsonism (PEP) and Pick’s disease (PiD). By Western blotting, antibody 988 labeled the characteristic tau triplet (tau 55, 64, 69) in AD, DS, Guamanian ALS/PDC and PEP. PSP and CBD exhibited their typical tau doublet (tau 64, 69), whereas the doublet tau 55 and 64 was detected in PiD. In all of these neurodegenerative disorders, antibody 988 clearly labeled NFT and dystrophic neurites, as well as Pick bodies in PiD cases, whereas no staining was observed in control cases. These data indicate that phosphorylation of serine422 on tau proteins is a common feature among neurodegenerative disorders and is therefore not specific of AD. Moreover, phosphorylation of this epitope permits the distinction between normal tau proteins and pathological tau proteins.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/s004010050978
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