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  • 1
    Digitale Medien
    Digitale Medien
    Differential Alteration of Various Cholinergic Markers in Cortical and Subcortical Regions of Human Brain in Alzheimer's Disease (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 50 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: The main objective of the present study was to determine whether cholinergic markers (choline acetyl-transferase activity and nicotinic and muscarinic receptors) are altered in Alzheimer's disease. Choline acetyltransferase activity in Alzheimer's brains was markedly reduced in various cortical areas, in the hippocampus, and in the nucleus basalis of Meynert. The maximal density of nicotinic sites, measured using the novel nicotinic radioligand N-[3H]methylcarbamylcholine, was decreased in cortical areas and hippocampus but not in subcortical regions. M1 muscarinic cholinergic receptor sites were assessed using [3H]pirenzepine as a selective ligand; [3H]pirenzepine binding parameters were not altered in most cortical and subcortical structures, although the density of sites was modestly increased in the hippocampus and striatum. Finally, M2-like muscarinic sites were studied using [3H]-acetylcholine, under muscarinic conditions. In contrast to M1 muscarinic sites, the maximal density of M2-like muscarinic sites was markedly reduced in all cortical areas and hippocampus but was not altered in subcortical structures. These findings reveal an apparently selective alteration in the densities of putative nicotinic and muscarinic M2, but not M1, receptor sites in cortical areas and in the hippocampus in Alzheimer's disease.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb02497.x
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  • 2
    Digitale Medien
    Digitale Medien
    Comparative Alterations of Nicotinic and Muscarinic Binding Sites in Alzheimer's and Parkinson's Diseases (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 58 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Medizin
    Notizen: Abstract: We have recently reported on the differential alterations of various cholinergic markers in cortical and subcortical regions in Alzheimer's disease (AD). The main purpose of the present study was to determine if cholinergic deficits observed in patients with AD are unique to this disorder or can be generalized to others such as idiopathic Parkinson's disease (PD) and PD with Alzheimer-type dementia (PD/AD). Muscarinic M1, M2, and nicotinic receptor binding parameters (Kd and Bmax) were determined in various cortical and subcortical areas using selective radioligands ([3H]-pirenzepine, [3H]AF-DX 116, and N[3H]methylcarbamylcholine). Choline acetyltransferase activity was also determined as a marker of the integrity of cholinergic innervation. Alterations of cholinergic markers are comparable in cortical areas in AD, PD, and PD/AD brains. In frontal and temporal cortices, as well as in the hippocampus, choline acetyltransferase activity and binding capacities of M2 and nicotinic binding sites are similarly decreased in these three disorders compared with age-matched control values. M1 receptor binding parameters are not significantly modified in cortical areas in patients with these disorders. In contrast, important differences between AD and PD brain tissues are found in subcortical areas such as the striatum and the thalamus. The density of M1 sites is significantly increased in striatal areas only in patients with AD, whereas densities of nicotinic sites are decreased in thalamus and striatum in PD and PD/AD, but not AD, brain tissues. The binding capacity of M2 sites is apparently unchanged in subcortical areas in all three disorders, although tendencies toward reductions are observed in the striatum of PD and PD/AD patients. Thus, although comparable alterations of various cholinergic markers are observed in cortical areas in the three neurological disorders investigated in the present study, important differences are seen in subcortical areas. This may be relevant to the respective etiological and clinical profiles of AD and PD.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb09752.x
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  • 3
    Digitale Medien
    Digitale Medien
    Selective delayed alternation deficits in dominantly inherited olivopontocerebellar atrophy
    Amsterdam : Elsevier
    Brain and Cognition 16 (1991), S. 121-129 
    Details
    ISSN: 0278-2626
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Medizin , Psychologie
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1016/0278-2626(91)90001-O
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  • 4
    Digitale Medien
    Digitale Medien
    NGF Level Is Not Decreased in the Serum, Brain-Spinal Fluid, Hippocampus, or Parietal Cortex of Individuals with Alzheimer's Disease
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 193 (1993), S. 198-203 
    Details
    ISSN: 0006-291X
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Biologie , Chemie und Pharmazie , Physik
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1006/bbrc.1993.1609
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  • 5
    Digitale Medien
    Digitale Medien
    Evidence for increased amyloid enhancing factor activity in Alzheimer brain extract (1988)
    Springer
    Acta neuropathologica 77 (1988), S. 82-90 
    Details
    ISSN: 1432-0533
    Schlagwort(e): Alzheimer's disease ; Amyloid enhancing factor ; Gel filtration ; Phenylmethylsulfonyl flouride ; Mouse bioassay
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Summary Soluble brain extracts containing 0.1 to 16 mg of protein from 3 normal human brain and 11 patients with Alzheimer's disease, Down's syndrome and other neurological disorders were assayed for amyloid enhancing factor (AEF) activity in the mouse bioassay. At the 0.1 mg dosage, five of seven brain extracts from amyloid-positive samples and only one of four amyloid-negative samples demonstrated AEF activity. Marginal AEF activity was detected in the normal brain extracts at 8 or 16 mg protein dosage. Alzheimer-AEF was aggregated by exhaustive dialysis against 0.01 M phosphate buffer, pH 6 or distilled water and the solubilized aggregate was fractionated on a BioGel P-60 column. Of the two protein peaks, AEF activity was present only in the low mol · wt second fraction, which on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and silver staining showed two discrete and three minor peptide bands between 60 and 66 kDa and one of these was periodic acid-Schiff positive, and three fuzzy bands near 14 kDa. Pretreatment of the crude and second fraction with 10 mM phenylmethylsulfonyl fluoride (PMSF) nearly completely abolished the in vivo AEF bioactivity. It is suggested that (a) a higher AEF concentration is present in amyloid-positive brain samples than those negative for amyloid or normal brain tissues, (b) AEF-positive fraction contains at least five dominant peptides ranging between 14 to 66 kDa, and (c) abolition of PMSF-treated Alzheimer-AEF activity, similar to that of murine AEF, might be due to its serine/thiol proteinase nature. To our knowledge, this is the first time that AEF activity has been demonstrated in Alzheimer brain samples.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00688246
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  • 6
    Digitale Medien
    Digitale Medien
    Biochemical mapping of neurofibrillary degeneration in a case of progressive supranuclear palsy: evidence for general cortical involvement (1994)
    Springer
    Acta neuropathologica 87 (1994), S. 572-577 
    Details
    ISSN: 1432-0533
    Schlagwort(e): KeyWords     Progressive supranuclear palsy Tau proteins ; Neurodegeneration Neurofibrillary tangles ; Mapping
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract A biochemical study was performed to quantify and map the neurodegenerating process in cortical and subcortical brain areas from a case of progressive supranuclear palsy (PSP). Our approach was based on a Western blot analysis of pathological Tau proteins, which are the basic components of neurofibrillary lesions. We found that: (i) the abnormal Tau proteins can be detected in all cortical areas, sometimes in larger amounts than in some subcortical areas; (ii) these abnormal Tau proteins consist of a doublet called Tau 64 and 69, except for in the entorhinal cortex where we detected, as for Alzheimer brains, the triplet of Tau proteins called Tau 55, 64 and 69; (iii) the amounts of abnormal Tau proteins were higher in some neocortical regions, especially in the frontal lobe, than in the hippocampal formation. Our results show that the neocortical pathology in PSP, as revealed by the presence of pathological proteins, is more extended than thought so far. Our biochemical approach appears to be more sensitive than the immunohistochemical one and can clearly differentiates between two types of neurofibrillary pathology, the Alzheimer type with a triplet of abnormal Tau proteins (Tau 55, 64 and 69) and the PSP type with a characteristic doublet (Tau 64 and 69).
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00293317
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  • 7
    Digitale Medien
    Digitale Medien
    Biochemical mapping of neurofibrillary degeneration in a case of progressive supranuclear palsy: evidence for general cortical involvement (1994)
    Springer
    Acta neuropathologica 87 (1994), S. 572-577 
    Details
    ISSN: 1432-0533
    Schlagwort(e): Progressive supranuclear palsy ; Tau proteins ; Neurodegeneration ; Neurofibrillary tangles ; Mapping
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract A biochemical study was performed to quantify and map the neurodegenerating process in cortical and subcortical brain areas from a case of progressive supranuclear palsy (PSP). Our approach was based on a Western blot analysis of pathological Tau proteins, which are the basic components of neurofibrillary lesions. We found that: (i) the abnormal Tau proteins can be detected in all cortical areas, sometimes in larger amounts than in some subcortical areas; (ii) these abnormal Tau proteins consist of a doublet called Tau 64 and 69, except for in the entorhinal cortex where we detected, as for Alzheimer brains, the triplet of Tau proteins called Tau 55, 64 and 69; (iii) the amounts of abnormal Tau proteins were higher in some neocortical regions, especially in the frontal lobe, than in the hippocampal formation. Our results show that the neocortical pathology in PSP, as revealed by the presence of pathological proteins, is more extended than thought so far. Our biochemical approach appears to be more sensitive than the immunohistochemical one and can clearly differentiates between two types of neurofibrillary pathology, the Alzheimer type with a triplet of abnormal Tau proteins (Tau 55, 64 and 69) and the PSP type with a characteristic doublet (Tau 64 and 69).
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00293317
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  • 8
    Digitale Medien
    Digitale Medien
    Neuronal transformations in Alzheimer's disease (1988)
    Springer
    Cell & tissue research 252 (1988), S. 239-248 
    Details
    ISSN: 1432-0878
    Schlagwort(e): Alzheimer's disease ; Neurofibrillary tangles ; Human neurofilaments ; Paired helical filaments ; Virus-like particles ; Human
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Summary Brains of nine early and four advanced Alzheimer patients have been investigated, utilizing three approaches to specify the threshold state of Alzheimer's disease (AD). Extensive thin sectioning electron microscopy (EM) of frontal lobe biopsies, correlated with stringent clinical assessment, has demonstrated that the neuronal cytoskeleton undergoes specific transformations into paired helical filament-like (PHF-like) strands, which lead to the formation of the insoluble paracrystalline paired helical filaments (PHFs). The neurofilamentous network (NFN) transformation plays an important role in this process, whereby segregation, posttranslational modifications and reassembly of the modified components through autocrosslinking, and phase transition occur. According to our data, the threshold state can be defined as the state of irreversible segregation and posttranslational modification of the NFN and the microtubule-associated proteins. At this state, therapeutic intervention to reverse the disease process may be possible. The results indicate similarities between the formation of the paracrystals of the PHFs and the formation of the tropomyosin-like crystals of the Hirano bodies. Close relationships among PHFs and smooth endoplasmic reticulum and plasma membrane do exist. Enveloped virus-like particles have been observed in neurons containing PHFs. A possible role of these virus-like particles as an etiological agent for AD is discussed.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00214366
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