Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P10636 (tau protein)
 5,110 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A recent report has described the appearance of silver positive, tau-immunoreactive astrocytes in the brains of patients with progressive supranuclear palsy (PSP) (Neurosci. Lett., 135 (1992) 99-102). In this study we confirmed this finding in two cases of PSP by using Bodian silver staining and immunohistochemistry with antibody to human tau protein. By electron microscopy we demonstrated that fibrillary masses present in these unique astrocytes were made up of straight tubules that were indistinguishable from those of neurofibrillary tangles of PSP. The term 'glial fibrillary tangle' was proposed for these structures.
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PMID:Glial fibrillary tangles with straight tubules in the brains of patients with progressive supranuclear palsy. 143 79

Immunohistochemical, ultrastructural and immunoelectron microscopic studies of spinal cord neurofibrillary tangles (NFTs) in progressive supranuclear palsy (PSP) were performed. The spinal cord NFTs reacted with antibodies to tau protein (tau-2), ubiquitin and Alzheimer neurofibrillary tangles (ANTs, Ab 39). Ultrastructurally, the NFTs consisted of bundles of straight fibrils. In longitudinal sections, the individual NFT fibrils appeared as straight fibrils with a diameter of approximately 15 nm. In cross sections, circular structures approximately 15 nm in diameter were seen, and some had a central density. Electron microscopic examination of specimens stained with the antibodies and by the modified Bielschowsky method revealed the products of the tau, ubiquitin and ANTs immunoreactions and silver deposits on the NFT fibrils. This is the first demonstration of the ultrastructure of spinal cord NFTs in PSP.
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PMID:Immunohistochemical, ultrastructural and immunoelectron microscopic studies of spinal cord neurofibrillary tangles in progressive supranuclear palsy. 148 85

A man, aged 58 years, suffered from progressive dementia, parkinsonism, and gaze paralysis for 30 months. Autopsy revealed severe degeneration of the substantia nigra, numerous swollen chromatolytic neurons within the cerebral cortex, scattered basal neurofibrillary tangles, and gliosis of the cerebral white matter and basal ganglia. Unusual globular inclusions positive for tau protein were detected within neurons of the upper cortical layers. Although the pathological findings were comparable with corticonigral degeneration with neuronal achromasia, several clinical and pathological features characteristic for progressive supranuclear palsy, progressive subcortical gliosis, and Pick's disease in this and the nine previously reported cases hampered the unequivocal nosological placement.
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PMID:Corticonigral degeneration with neuronal achromasia and basal neurofibrillary tangles. 208 97

Light microscopic immunohistochemical investigations were performed on neurofibrillary tangles (NFT) in four histologically confirmed cases of Alzheimer's disease (AD) and in five patients with a progressive supranuclear palsy (PSP). The antibody panel included antisera to the neuronal microtubule-associated protein, tau, and to isolated paired helical filaments (PHF), as well as mouse monoclonal antibodies (MAbs) to phosphorylated epitopes on high and medium molecular weight neurofilament subunits (RT97 and BF10, respectively). Paraffin sections were also impregnated with the Gallyas silver method, which specifically stains tangles and cortical neuropil threads in AD, but does not stain normal neurofilaments. All tangles in PSP and AD showed consistent immunostaining with antibodies to tau protein and isolated PHF, regardless of their localization. MAbs RT97 and BF10, however, did not stain or only weakly stained, subcortical tangles in PSP and AD, whereas most cortical NFT in AD were intensely immunostained. All tangles in PSP were as heavily impregnated with Gallyas as they were in AD. Furthermore there were extensive networks of Gallyas-positive, tau- and PHF-immunoreactive neurites in subcortical gray areas containing NFT, and bundles of positive axons in white matter tracts interconnecting subcortical nuclei of PSP. Our studies indicate a much more extensive disruption of fibrillar proteins in PSP subcortical neurons than previously reported. They furthermore indicate a very similar antigenic profile of NFT in PSP and AD, as far as subcortical neurons are concerned.
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PMID:Progressive supranuclear palsy: extensive neuropil threads in addition to neurofibrillary tangles. Very similar antigenicity of subcortical neuronal pathology in progressive supranuclear palsy and Alzheimer's disease. 314 22

Corticobasal degeneration (CBD) is a rare, progressive neurological disorder characterized by widespread neuronal and glial accumulation of abnormal tau protein. Using immunohistochemistry we analyzed tau epitope expression and phosphorylation state in CBD and compared them to cytoskeletal changes in Alzheimer's disease (AD) and progressive supranuclear palsy (PSP). Epitopes spanning the entire length of the tau protein were present in CBD inclusions. An antibody against the alternatively spliced exon 3 did not recognize cytoskeletal lesions in CBD, but did in AD and PSP. Tau epitopes from each region of the molecule were present in cytoskeletal inclusions in CBD, including gray matter astrocytic plaques, gray and white matter threads, and oligodendroglial inclusions. As in AD, tau from CBD was highly phosphorylated. Antibodies that recognized phosphorylated tau epitopes reacted with material from CBD in a highly phosphatase-dependent manner. Again, all types of inclusions contained phosphorylated epitopes. We conclude that abnormal tau protein in CBD comprises the entire tau molecule and is highly phosphorylated, but is distinguished from AD and PSP by the paucity of epitopes contained in the alternatively spliced exon 3.
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PMID:Epitope expression and hyperphosphorylation of tau protein in corticobasal degeneration: differentiation from progressive supranuclear palsy. 757 77

Cell cycle-associated nuclear proteins may have more specialized functions in the adult nervous system in addition to those directly associated with cell proliferation, as suggested by a recent study showing that neurofibrillary tangles (NFT) and dystrophic neurites in Alzheimer's disease (AD) are immunoreactive for the proliferation-associated antigen p105. To further investigate this hypothesis, we studied the expression of another proliferation-associated antigen, Ki-67, in the brains of patients with AD and other neurodegenerative disorders. Formalin-fixed, paraffin-embedded sections from autopsy cases of AD, Down's syndrome with dementia and AD pathology (DS/AD), Pick's disease (PiD), progressive supranuclear palsy (PSP), Lewy body disease (LBD), Parkinson's disease (PD), corticobasal degeneration (CBD), and young and aged normal brains, and from two surgically resected gangliogliomas were immunostained using antibodies to Ki-67 (MIB-1 clone equivalent) and tau (tau). Ki-67 staining was performed following antigen retrieval by microwave heating. Ki-67 labeled NFT that were observed in the AD, DS/AD, PiD, PSP, LBD, and PD cases, one aged normal brain, and one ganglioglioma. Ki-67 generally labeled fewer NFT compared to tau. Pick bodies, ballooned neurons (Pick cells) in CBD and PiD, and nigral corticobasal inclusions in CBD were immunoreactive for tau but not Ki-67. Neither antibody labeled cortical or subcortical Lewy bodies. Our findings suggest that Ki-67 may be involved in the pathogenesis of neurofibrillary degeneration in AD, other neurodegenerative disorders, normal aging, and neoplasms such as ganglioglioma. We postulate a possible role for Ki-67 in the production of the abnormally phosphorylated tau protein that leads to the formation of paired helical filaments within susceptible neurons.
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PMID:Ki-67 immunoreactivity in Alzheimer's disease and other neurodegenerative disorders. 774 28

The neostriatum, nucleus accumbens and basal nucleus of Meynert (bnM) in the parkinsonism-dementia complex of Guam (Guam PDC) were examined immunohistologically, ultrastructurally, quantitatively and topographically, and the results were compared with those in Alzheimer's disease (AD) and progressive supranuclear palsy (PSP). Compared to neurologically normal controls, the number of large neurons in Guam PDC was reduced by approximately 70% in the caudate nucleus and putamen and by more than 90% in the nucleus accumbens. The decreased number of large neurons in the neostriatum was significantly correlated to that in the bnM. The remaining large neurons and many of the medium-sized neurons in the neostriatum and nucleus accumbens were immunopositive for tau protein and contained varying amounts of 21- to 25-nm-wide paired helical filaments (PHFs) admixed with straight tubules. Curly fibers and circularly arranged reactive astrocytes were seen in the nucleus accumbens of many PDC patients. Collectively, these findings, which are similar in part to those of AD and differ from those of PSP, suggest that the large neurons in the neostriatum and nucleus accumbens in Guam PDC degenerate through PHF formation, and that extremely severe loss of large neurons in the nucleus accumbens may be linked to marked degeneration of the limbic and ventral tegmental areas and nucleus dorsal raphe.
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PMID:The neostriatum and nucleus accumbens in parkinsonism-dementia complex of Guam: a pathological comparison with Alzheimer's disease and progressive supranuclear palsy. 798 92

Tau accumulating as paired helical filaments (PHF) in Alzheimer's disease brain is considered to be abnormally phosphorylated on distinct sites. To compare the phosphorylation state of tau-positive neuronal inclusions among diverse neurologic diseases, we have probed these lesions with three well-defined PHF/tau monoclonals, C5, M4 and tau 1, that most likely recognize three proline-directed phosphorylation sites in PHF-tau. In Alzheimer's disease brain all three monoclonals intensely immunostained intracellular neurofibrillary tangles, neuropil threads, senile plaque neurites, and "pretangle neurons" in a phosphorylation-dependent manner. They also stained, in the same manner, Pick bodies in Pick's disease, and neurofibrillary tangles and neuropil threads in various tangle-forming neurologic diseases. In most of these diseases (including Pick's disease, progressive supranuclear palsy, subacute sclerosing panencephalitis, and Alzheimer's disease) astrocytes and oligodendrocytes were found to contain tau-positive inclusions which showed the same immunocytochemical characteristics. Thus, the widely occurring tau-positive inclusions share common phosphorylation characteristics irrespective of underlying diseases or cell types.
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PMID:Neuronal and glial tau-positive inclusions in diverse neurologic diseases share common phosphorylation characteristics. 798 93

We report an autopsy case of progressive supranuclear palsy (PSP) with a five-year clinical course. A 67-year-old man was suffering from a gait disturbance and mental deterioration. Neurological examination at the age of 71 revealed pseudobulbar palsy, horizontal ophthalmoplegia, and truncal dystonia, and a diagnosis of PSP was made. Mental deterioration including forgetfulness and character change was also noted, and the patient sometimes exhibited intermittent stuporous states. Cranial computed tomography and magnetic resonance images revealed moderate brain atrophy, predominantly in the frontal lobes. The patient died of bronchopneumonia at the age of 71. Neuropathological examination confirmed typical pathological changes of PSP, such as neuronal loss, neurofibrillary tangles, and fibrillary gliosis in the subcortical nuclei. Gallyas-Braak silver impregnation revealed neurofibrillary tangles, silver-positive glia and thread-like structures in degenerating subcortical nuclei. In addition to these classical lesions, the argentophilic structures were detected in the cerebral cortex, cortical white matter and cerebellar white matter. In the cerebral cortex, they were abundant mostly in the precentral gyrus and subcortical white matter. Immunohistochemical studies revealed that most silver-positive structures were also tau 2 antibody-positive. Thus, these argentophilic structures seemed to be closely related to abnormal tau protein. Their distribution in this case implies that lesions related to abnormal tau protein may occur more extensively in the brains of PSP than expected.
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PMID:[Widespread argentophilic structures in progressive supranuclear palsy--an autopsy case report]. 806 Jun 88

The gradual intraneuronal accumulation of an insoluble fibrous material which partly consists of abnormally phosphorylated tau protein (neurofibrillary change) represents an important neuropathological hallmark of Alzheimer's disease. Neurofibrillary tangles and neuropil threads formed from this material develop in only a few types of cortical pyramidal cells. The first changes are seen in the entorhinal cortex. The destructive process then spreads into the hippocampal formation and eventually encroaches upon the isocortex. This sequence of events permits the distinction of six stages with a progressive increase in the severity of cortical destruction. The entorhinal region serves as an important interface between the isocortex and hippocampus. This interface function is markedly impaired due to the early deterioration of the entorhinal cortex. Severe entorhinal involvement is considered to represent the morphological counterpart of clinically incipient Alzheimer's disease. Similar changes are found in mentally impaired individuals suffering from Parkinson's disease or progressive supranuclear palsy.
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PMID:Staging of Alzheimer-related cortical destruction. 830 60


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