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PubMed1991

Secondary deposition of beta amyloid within extracellular neurofibrillary tangles in Alzheimer-type dementia.

The hippocampal areas of 34 autopsy specimen brains from aged demented and nondemented subjects were examined using double staining of Bodian and beta protein. In 18 cases (75.5 +/- 7.4 years old), none of the extracellular neurofibrillary tangles (E-NFTs) were immunoreactive with beta protein. In 16 cases (82.9 +/- 5.4 years old), the minority of E-NFTs were immunoreactive with beta-protein antiserum. These beta-immunoreactive E-NFTs frequently appeared in the areas having senile plaques, while they were not observed in the area lacking beta-immunoreactive senile plaques. The ultrastructure of beta-immunoreactive E-NFTs revealed that they consisted of extracellular amyloid fibrils, extracellularly located bundles of paired helical filaments, astroglial processes and degenerating neurites. These findings suggest that the beta immunoreactivity of E-NFTs comes from secondary deposition of amyloid fibrils.

Aged↗

PubMed1990

Phosphate-dependent monoclonal antibodies to neurofilaments and Alzheimer neurofibrillary tangles recognize a synthetic phosphopeptide.

Five phosphate-dependent monoclonal antibodies to the neurofilament heavy polypeptide bound strongly to a phosphorylated synthetic peptide, which contains a single Lys-Ser-Pro sequence that occurs in human neurofilaments. Three of the antibodies label Alzheimer's disease neurofibrillary tangles and two do not, suggesting that in tangles an epitope similar to the peptide is available to some but not all of the antibodies. In addition, some antibodies were found to be more affected than others by enzymatic dephosphorylation of the antigen, but because all the antibodies bound the same synthetic phosphopeptide they do not bind to mutually exclusive phosphorylation sites. Instead the more phosphate-dependent antibodies might bind the phosphate group more directly, as suggested by their inhibition by inorganic phosphate and free phosphoserine.

Alzheimer Disease↗

PubMed1991

Presenile appearance of abundant Alzheimer's neurofibrillary tangles without senile plaques in the brain in myotonic dystrophy.

In 7 myotonic dystrophy (MyD) cases of 35- to 56-year old and 18 non-neurological age-matched controls paraffin-embedded temporal lobe sections were stained by the modified Bielschowsky method to count neurofibrillary tangles (NFTs) and senile plaques (SPs). In the parahippocampal gyrus, NFTs were observed in all the MyD cases; a few in the youngest, with an increase in number with age to the abundant appearance in the 4 cases in their 50s. The eldest also had many NFTs in the hippocampus. By contrast, the control subjects had, if any, only a few NFTs in the hippocampus and the parahippocampal gyrus. No SPs were observed in any MyD or control case. Thus, it was found that in MyD NFTs appear, unaccompanied by SPs, at an abnormally early age in the parahippocampal gyrus, with a rapid age-related increase in their number. This neuronal change may belong to the progeric features observed in this condition.

Adult↗

PubMed1988

Ganglioglioma containing osseous tissue and neurofibrillary tangles.

A ganglioglioma involving the temporoparietal lobe in a 49-year-old patient displayed several unusual histopathologic features. A large central focus of osseous tissue that was found may have resulted from metaplasia of a mesodermal component of the lesion. In addition, occasional ganglioma cells showed neurofibrillary tangles and granulovacuolar changes. The presence of these cytoplasmic structures, usually seen in Alzheimer's disease and other degenerative conditions, within a ganglioglioma emphasizes the diverse settings in which such neuronal changes may occur and may provide clues to their pathogenesis.

Brain Neoplasms↗

PubMed1985

The dissolution of language in Pick's disease with neurofibrillary tangles: a case study.

This paper is a detailed retrospective history of a patient who began to have difficulty with speaking and comprehension in 1967, and whose neuropathological examination at time of death 12 1/2 years later was consistent with a diagnosis of Pick's disease, complicated by neurofibrillary tangles. It follows the deteriorating course of his language abilities in the context of relatively less-impaired general cognitive abilities, using two sources of information. The first is his own written record of his deteriorating abilities, shown in letters and notes he wrote over this period. The second is through an oral history obtained from the patient's family. The purpose of this report is to illustrate in detail the course of a degenerative condition and to suggest the utility of such descriptional records in increasing understanding of language deterioration in dementia.

Aged↗

PubMed1984

A descriptive study of neuritic plaques and neurofibrillary tangles in an autopsy population.

From July 1, 1980 to December 2, 1982, all individuals at autopsy at the University of Michigan Medical Center greater than or equal to 65 years of age and selected individuals less than 65 years of age were examined for neuritic plaques and neurofibrillary tangles. Sections of the hippocampal, parahippocampal temporal gyrus, and fusiform gyrus were examined. In a total population of 199, each individual was classified as having none, few, or many of each lesion. The frequency of the joint presence of many plaques and tangles increased monotonically after age 71 years. There was no significant difference in the joint distribution of these lesions with sex or race. There was a strong correlation between the presence of one lesion and the other; the correlation for the two lesions was similar for males and females, but for blacks, it was significantly higher than for non-blacks. The distribution of these lesions in autopsy populations may be useful in identifying other related hypothetical risk factors for dementia of Alzheimer's type.

Age Factors↗

PubMed1988

Increased Mr 60,000 protein phosphorylation is correlated with neocortical neurofibrillary tangles in Alzheimer's disease.

Increased Mr 60,000 protein phosphorylation has been found in the cytosol fraction of brain tissue from Alzheimer's disease patients. A correlation between this biochemical change and the morphologic abnormalities found in Alzheimer's disease was sought. Three neuropathologic features were studied: neurofibrillary tangles and neuritic plaques, findings characteristic of Alzheimer's disease, and gliosis, a non-specific change. The number of tangles correlated well with the extent of Mr 60,000 protein phosphorylation (p less than 0.001); but the number of plaques did not. To investigate the possibility that gliosis causes the increased Mr 60,000 protein phosphorylation, cases of Pick's disease and multi-infarct dementia were also studied. The levels of Mr 60,000 protein phosphorylation in these cases were comparable to those seen in normal controls. These findings suggest that the increased Mr 60,000 protein phosphorylation is closely related to diseased, tangle-bearing neurons and is not directly related to neuritic plaque formation or secondary gliosis.

Alzheimer Disease↗

PubMed1990

Distribution of neurofibrillary tangle formation and [3H]-D-aspartate receptor binding in the thalamus in the normal elderly brain, in Alzheimer's disease and in Parkinson's disease.

The overactivity of glutamatergic neurons may underlie some neurodegenerative disorders, including Alzheimer's disease (AD). We explored the relationship between glutamatergic transmission and neurofibrillary tangle formation by measuring [3H]-D-aspartate binding activity and the proportion of neurons containing tangles within individual thalamic nuclei in five AD cases. Five elderly normal and five Parkinson's disease (PD) cases were used as controls. A highly significant correlation between [3H]-D-aspartate binding and tangle counts in Alzheimer's disease suggests that those thalamic nuclei which normally receive a relatively dense glutamatergic afferent input are predisposed to tangle formation. There were no significant differences in individual thalamic nuclear [3H]-D-aspartate binding between controls and the AD and PD groups.

Aged↗

PubMed1979

Neurofibrillary tangles induced by a sclerosing angioma.

A sclerosing angioma in the frontal cortex of a 40 year old woman produced local pressure, with resulting alteration of the blood-brain barrier. In the narrow cortical zone affected by chronic pressure, the level of aluminum was significantly elevated; and all neurons had neurofibrillary tangles of the Alzheimer type.

Adult↗

PubMed1986

Occurrence of neuropil threads in the senile human brain and in Alzheimer's disease: a third location of paired helical filaments outside of neurofibrillary tangles and neuritic plaques.

Paired helical filaments, pathologically changed components of the cytoskeleton of human nerve cells, are demonstrated by a specific silver staining technique, immunostaining and electron microscopy. Accumulations of these filaments are found in the telencephalic cortex of old-aged individuals and patients suffering from Alzheimer's disease. Apart from neurofibrillary tangles and neuritic plaques, paired helical filaments are encountered in neuropil threads. At this third location, pathological filaments occur in small and inconspicuous profiles scattered throughout both allocortical and isocortical areas. The pattern of distribution and packing density of neuropil threads varies between different cortical areas and layers.

Aged↗

PubMed1991

The binding of basic fibroblast growth factor to Alzheimer's neurofibrillary tangles and senile plaques.

Brain sections from Alzheimer's disease (AD) patients and controls were treated with basic fibroblast growth factor (bFGF) and then immunostained with anti-bFGF. Additional sections were treated with biotinylated bFGF without using the anti-bFGF. Labelling was visualized by the ABC method. Both protocols above intensely labelled neurofibrillary tangles, senile plaques and amyloidotic vessels in AD brains. Omission of the bFGF treatment abolished the staining of the AD lesions. The pretreatment of sections with heparitinase also reduced their staining. These results indicate that AD lesions contain bFGF-binding sites and that the chemical substrate for bFGF binding to AD lesions was heparan sulfate.

Alzheimer Disease↗

PubMed1987

Staining with monoclonal antibodies to neurofilaments distinguishes between subpopulations of neurofibrillary tangles, between groups of axons and between groups of dendrites.

A new monoclonal antibody (mab) against neurofilaments is described (mab 1215) and its reactions compared with previously characterized mabs (BF10; RT97). Mab 1215 recognizes an epitope on the heavy neurofilament polypeptide (NF-H). In Alzheimer's disease, mab 1215 recognizes only a subpopulation of neurofibrillary tangles and stains a proportion of tangles in the hippocampus but none of those in the olfactory bulb. However, mabs RT97 and BF10 stain the majority of tangles in both brain areas. Of the three antibodies, only mab BF10 recognizes, specifically, axons of granular cells in the dentate gyrus of the hippocampus. Mab 1215 recognizes more dendrites in the pyramidal layer than either mab BF10 or mab RT97. Our observations indicate that neurofilaments are not identical in all axons and that, contrary to previous reports, NF-H is present in dendrites. The dendritic form of NF-H appears to be different from NF-H in axons and this could be due to differences in the state of phosphorylation of NF-H. We suggest that the finding that distinct subpopulations of tangles exist indicates that tangles are not static lesions. Further investigations into this possibility may illuminate the pathophysiology of Alzheimer's disease.

Aged↗

PubMed1988

Neurofibrillary tangle formation in the nucleus basalis of Meynert ipsilateral to a massive cerebral infarct.

Two cases of massive cerebral infarct in the territory of the middle cerebral artery on one side of the brain are presented, in which many (Patient 1) or several (Patient 2) neurofibrillary tangle-bearing neurons were observed in the nucleus basalis of Meynert (nbM), ipsilateral to the infarcts. Tangles were absent or rare in the opposite nbM or in other areas of the brain. Considering the widespread projection of nbM axons to the ipsilateral cerebral cortex, this suggests that formation of neurofibrillary tangles can occur as a retrograde reaction in nbM neurons secondary to massive, old cerebral infarction.

Aged↗

PubMed1988

Solubility of neurofibrillary tangles and ultrastructure of paired helical filaments in sodium dodecylsulphate.

Temporal cortex from 14 cases of Alzheimer-type dementia and 6 cases of Down's syndrome, all selected for severe Alzheimer pathology, was homogenised in distilled water, NaOH, or sodium dodecylsulphate (SDS) containing 0.1% beta-mercaptoethanol. The homogenates were stained with Congo red, and the neurofibrillary tangles and plaque cores were counted under crossed-polarisation microscopy. The number of tangles and plaque cores in the water-treated extracts was not related to age, sex, post-mortem interval or duration of dementia. The number of tangles after extraction in SDS or NaOH, as a percentage of tangles in water-treated extracts, was 57 +/- 25 (mean +/- SD) for 1% SDS, 43 +/- 17 for 5% SDS and 37 +/- 22 for 0.2 M NaOH. Plaque cores were essentially insoluble in all three agents. The percentage of tangles insoluble in 1% SDS did not correlate with age or post-mortem interval but decreased with increasing duration of dementia. Enhanced tangle solubility with increasing duration of dementia suggests that the nature of tangles changes with time; one possibility is that this reflects transformation of intracellular to extracellular tangles. Paired helical filament (PHF) length and the number of repeats per PHF were measured in electron micrographs of PHF prepared with and without treatment by 1% SDS. There was no significant multimodality of PHF length to suggest that PHF broke at regular intervals. The mean repeat length (PHF length/number of repeats) was greater for PHF isolated in the presence of 1% SDS than in its absence, showing that SDS affects ultrastructure by untwisting PHF.(ABSTRACT TRUNCATED AT 250 WORDS)

Aged↗

PubMed1987

Autoantibodies to neurofibrillary tangles and brain tissue in Alzheimer's disease. Establishment of Epstein-Barr virus-transformed antibody-producing cell lines.

Multiple EBV-transformed B cell lines were established from five patients with a clinical diagnosis of Alzheimer's disease (AD) and six age-matched controls. The supernatants were screened for antibody activity against SDS-treated isolated neurofibrillary tangles (NFT). Reactive supernatants were identified from both the AD and control group. The frequencies of anti-NFT antibody-secreting lines were 6.3 and 1.6% for the AD and the control groups, respectively. A proportion of these supernatants also stained NFT in situ and neurons and/or glia in sections of the frontal and the temporal cortexes of autopsied AD and normal brains, as well as cells from three cell lines (HeLa, fibroblast, and neuroblastoma). Several patterns of staining were revealed by these supernatants, indicating different reactive antigens. One supernatant stained NFT and astrocytes in sections from AD brains. It did not stain sections from two normal brains. This cell line is the result of the immortalization of a circulating B cell making antibody specific for an antigen in AD. The present approach may provide new insights in the pathogenesis of AD.

Alzheimer Disease↗

PubMed1990

Neurofibrillary tangles in some cases of dementia pugilistica share antigens with amyloid beta-protein of Alzheimer's disease.

Formalin-fixed, paraffin-embedded temporal lobe sections from eight former boxers' brains were examined using an immunohistochemical method with antibodies to amyloid beta protein. In accord with recent observations in Alzheimer's disease, significant numbers of beta-protein immunoreactive neurofibrillary tangles (NFT) were observed in three cases. Most of these immunoreactive NFTs appeared to be tombstone tangles, although not all such tangles were stained. This immunoreaction was completely abolished by preincubation of antibodies with synthetic beta-protein peptides, and the identity of the immunostained NFTs was confirmed by polarization microscopy of sections counterstained with Congo red. However, it is not yet clear if the beta-protein antigens are, in fact, an integral part of paired helical filaments. These observations, together with our recent finding of beta-immunoreactive plaque-like lesions in dementia pugilistica, also emphasize the many similarities in pathology between this condition and Alzheimer's disease.

Adult↗

PubMed1987

Isolation of cDNAs coding for epitopes shared by microtubule-associated proteins and neurofibrillary tangle in Alzheimer's disease.

5 cross-hybridizing cDNA clones of sizes 2.2 (3 cDNAs), 1.3 and 0.8 kb corresponding to tau microtubule-associated protein have been isolated from a rat brain lambda gt11 expression library. Antibodies affinity-purified using the fusion protein encoded by the cDNAs were observed to label tau polypeptides on Western blots and Alzheimer's neurofibrillary tangles.

Alzheimer Disease↗

PubMed1988

Lewy bodies contain epitopes both shared and distinct from Alzheimer neurofibrillary tangles.

Most of the identified constituents of the filamentous inclusions characteristic of the neurodegenerative diseases of aging are derived from the cytoskeleton. This study was undertaken to define immunocytochemically the cytoskeletal constituents of the filamentous cytopathologic marker of idiopathic Parkinson disease, the Lewy body (LB). An array of antibodies specific to neurofilaments, tubulin, microtubule associated proteins (tau, MAP1 and MAP2) and Alzheimer neurofibrillary tangles (NFT) were used to immunostain sections containing LB. All the antibodies to tubulin, MAP1 and MAP2 and the majority of the antibodies to neurofilaments and NFT recognized LB. The two monoclonal antibodies to NFT that recognize LB also react with ubiquitin, which has been identified in NFT. The prominent NFT component, tau, is apparently not incorporated into LB. These findings suggest that the presence of tau might not be a prerequisite to the formation of abnormal filaments. Therefore, although LB contain elements of neurofilaments, microtubules and ubiquitin, as do other abnormal neuronal filaments, they are distinct in composition. These distinctive and shared features may provide useful insights regarding the mechanisms underlying the formation of filaments in LB as well as those of other neuronal inclusions.

Alzheimer Disease↗