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  • 1
    Electronic Resource
    Electronic Resource
    Alzheimer paired helical filaments: Immunochemical identification of polypeptides (1984)
    Springer
    Acta neuropathologica 62 (1984), S. 259-267 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer disease ; Senile dementia ; Neurofibrillary tangles ; Paired helical filaments ; Neurofibrous proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Antisera to isolated Alzheimer neurofibrillary tangles (ANT) of paired helical filaments (PHF) were raised in rabbits. These anti-PHF sera immunolabeled both ANT in sections of Alzheimer hippocampus and ANT which were isolated and extracted with sodium dodecyl sulfate (SDS). The immunostaining of ANT in tissue sections was removed by absorption of the anti-PHF serum with small amounts of PHF and also with 40-fold the amount of a fraction prepared identically from normal brain; neurofilament and brain microtubule preparations used at the same concentration as the normal brain control fraction did not eliminate the tangle staining. Furthermore, the tangle staining was also not removed with glial filaments or actin and myosin filaments. No labeling of the neurofilaments of axons and cerebellar basket fibers by anti-PHF sera was observed in tissue sections from non-neurologic brain. On paper blots of SDS-polyacrylamide gels anti-PHF serum reacted with neither polypeptides of the normal brain control fraction nor major microtubule and neurofilament polypeptides. However, the immunoblots of PHF preparations with the anti-PHF serum revealed staining of several polypeptide bands in the 45,000–70,000 molecular weight (MW) region, material on top of the gel and diffuse staining of the high MW region. The tangles staining in tissue sections by the anti-PHF serum was abolished by its absorption with PHF polypeptides extracted from high and low molecular weight areas of SDS polyacrylamide gels but not with identically prepared neurofilament polypeptides. These results indicate that (1) the antigen(s) recognized by the anti-PHF serum is inherent to the PHF, (2) this PHF polypeptide(s) is at least partly soluble in SDS, and (3) this polypeptide(s) occurs in normal brain but is not associated with microtubules, neurofilaments, actin, or myosin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00687607
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  • 2
    Electronic Resource
    Electronic Resource
    Alzheimer neuropathology in non-Down's syndrome mentally retarded adults (1990)
    Springer
    Acta neuropathologica 80 (1990), S. 362-367 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer disease ; Mental retardation ; Neuritic plaques ; Neurofibrillary tangles ; Paired helical filaments
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We examined the brains of 385 mentally retarded adults aged 23–90 years without Down's syndrome (DS), metabolic disorder, or hydrocephalus to extend our knowledge about the occurrence of Alzheimer-type neuropathology in this population. Relevant measures of neuropathology also were related to selected information available from clinical records. The presence of one or more neurofibrillary tangles (NFT) and/or neuritic plaques (NP) was observed in 63.4% of all cases and varied with age. The prevalence of positive cases was higher when mental retardation was due to head trauma, congenital malformation, or familial factors and when a history of seizures was reported. Comprehensive morphometric analyses of neocortical, hippocampal and parahippocampal areas indicated that recommended agespecific quantitative criteria for the diagnosis of Alzheimer disease [Khachaturian ZS (1985) Arch Neurol 42:1097–1105] were met in 9.5% of cases less than 50 years of age, 54.2% between 50 and 65, 70% between 66 and 75, and 87% of the cases greater than 75 years of age. However, a limited immunohistochemical study revealed that in most cases the NP did not have a neuritic component containing paired helical filaments and in this respect most of the plaques observed in this population may differ from those most strongly associated with Alzheimer disease. In addition, substantial numbers of NFT were seen in frontal cortex, contrasting with results reported in the literature for nonretarded populations. The number of NP per mm2 consistently increased with age for all areas examined, while the relationship between NFT density and age varied across areas, and was clearly not monotonic. Our studies show that the neuropathological lesions currently considered hallmarks of Alzheimer disease are prevalent among non-DS mentally retarded adults, and the regional density of these lesions is high. Thus, while people with DS are affected at an earlier age, clear Alzheimer neuropathology develops in many mentally retarded individuals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00307688
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  • 3
    Electronic Resource
    Electronic Resource
    Alzheimer paired helical filaments: Bulk isolation, solubility, and protein composition (1984)
    Springer
    Acta neuropathologica 62 (1984), S. 167-177 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer disease/senile dementia of the Alzheimer type ; Neurofibrillary tangles ; Paired helical filaments ; Intermediate filaments ; Neurofibrous proteins ; Cytoskeleton
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A method has been developed for the bulk isolation of Alzheimer neurofibrillary tangles (ANT) of paired helical filaments (PHF) from histopathologically confirmed cases of Alzheimer disease/senile dementia of the Alzheimer type (AD/SDAT). The fresh or frozen autopsied cerebral cortex affected with Alzheimer neurofibrillary changes is dissociated by homogenization and sieving through nylon bolting cloth and the ANT are separated by a combination of sucrose discontinuous density gradient centrifugation, glass bead column chromatography, and sodium dodecyl sulfate (SDS) treatment. The isolated ANT produce red-green birefringence when viewed through polarized light after staining with Congo red. Ultrastructurally, the isolated PHF are well preserved and have the dimensions of the PHF seen in situ. Two major Populations of ANT which exist in different proportions in AD/SDAT brains are identified on the basis of their solubility in SDS. The ANT I and the ANT II are soluble and insoluble respectively on treatment with 2% SDS at room temperature for 5 min. Solubilization of the ANT II requires several repeated extractions with a solution containing 10% each of SDS and β-mercaptoethanol (BME) at 100°C for 10 min. Sonication of the ANT II greatly facilitates their solubilization. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of the isolated ANT reveals the presence of two major polypeptides with molecular weights (MW) of 62,000 and 57,000, several minor polypeptides with MW below 57,000, and a significant amount of material not entering the stacking and the resolving gels. Re-electrophoresis of polypeptides extracted from various areas of the resolving gel or of the material which does not enter the gel generates the same polypeptide profile as on the first gel, suggesting that the PHF material which does not enter the gel may result from the reaggregation of the polypeptides that enter the resolving gel. None of the polpeptides observed in the isolated PHF comigrate in the SDS-PAGE with any of the neurofilament polypeptides, tubulin, actin, or myosin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00691849
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  • 4
    Electronic Resource
    Electronic Resource
    Alzheimer paired helical filaments: Identification of polypeptides with monoclonal antibodies (1985)
    Springer
    Acta neuropathologica 68 (1985), S. 279-283 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer disease ; Senile dementia ; Neurofibrillary pathology ; Neurofibrillary tangles ; Paired helical filaments ; Neurofibrous proteins ; Neurofibrils
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Paired helical filaments (PHF) were isolated from autopsied brain of cases of Alzheimer dementia, and their polypeptides were identified with monoclonal antibodies to PHF by Western blots. The PHF polypeptide profile consisted of several bands with a size difference of less than 5 kilodalton (kDa) between adjacent bands; the most prominent bands were in the 45–62 kDa region. These PHF polypeptides were also labeled with tangles reactive antisera to microtubules from normal brain but had electrophoretic patterns different from those of microtubules and neurofilaments. These studies define the molecular weight profile of PHF polypeptides and suggest that they might originate from normal brain proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00690830
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  • 5
    Electronic Resource
    Electronic Resource
    Lectin histochemistry of plaques and tangles in Alzheimer's disease (1987)
    Springer
    Acta neuropathologica 73 (1987), S. 1-11 
    Details
    ISSN: 1432-0533
    Keywords: Alzheimer's disease ; Neuritic plaques ; Amyloid ; Neurofibrillary tangles ; Lectin receptors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Biotinyl derivatives of several lectins and avidin-horseradish peroxidase were used to study the localization of glycoconjugates in amyloid plaques and in neuritic tangles in brains of patients with Alzheimer's disease (AD), Downs syndrome (DS) and Gerstmann-Sträussler syndrome (GSS). The lectins tested recognize the following residues: β-d-galactosyl [Ricinus communis agglutinin 120, (RCA-1) and peanut agglutinin, (PNA)]; α-d-galactosyl [Griffonia simplicifolia agglutinin (GSA)]; α-d-mannosyl〉α-d-glucosyl [concanavalin A (Con A) andLens culinaris agglutinin (LcH)];N-acetyl- andN-glycolylneuraminic acid [Limax flavus agglutinin (LFA) andLimulus polyphemus agglutinin (LPA)];N-acetyl-glucosaminyl and sialyl [wheat germ agglutinin (WGA)];N-acetyl-d-galactosaminyl [Helix pomatia agglutinin (HPA) andDolichos biflorus agglutinin (DBA)] and α-l-fucosyl [Ulex europeus agglutinin (UEA-1)]. The majority of lectins listed above bind preferentially to the peripheral area of AD plaques, whereas in plaques of DS they are mainly bound to central amyloid core. In neurofibrillary tangles of AD brains only residues recognized by WGA and HPA or DBA were found, whereas in DS brains, in addition to above mentioned, β-d-galactose (RCA-1) and sialic acid (LFA) were also present. In brain microblood vessels the strongest reaction in endothelia appeared with UEA-1 and RCA-1, indicating the abundance of α-l-fucosyl and β-d-galactosyl residues. In AD brains deposits of amyloid were noted in the wall of some blood vessels, where monosaccharide residues recognized by RCA-1, GSA, UEA and WGA but not by Con A and LFA were present. However, our studies of some organs (liver, kidney, heart and testes) of patients with generalized amyloidosis revealed a lack of these sugar residues. It indicates, that the composition of amyloid present in brains of AD is different to that in other organs in generalized amyloidosis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00695495
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