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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 396 (1982), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 396 (1982), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Anatomy and embryology 165 (1982), S. 315-328 
    ISSN: 1432-0568
    Keywords: Rabbit photoreceptor ; Retina ; Microtubules ; Protofilaments ; Connecting cilium ; Outer doublets ; Microtubule assembly ; Tubulin of oligomers
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The connecting cilium of the rabbit photoreceptor rod is composed of nine outer doublets, lacking dynein side arms. The central singlet microtubules are absent. In cross section, there is an inner dense ring situated between the doublets and the center core of the cilium. As the doublet microtubules progress from the connecting region into outer segments, the cylindrical array of the nine pairs of doublets spreads out as a brush-like arrangement into the incisure cavity of the outer segment. The microtubules continue as doublets for much of the length of the outer segment. The B-tubules terminate first; the A-tubules extend as single tubules into the apical region of the photoreceptor. Before the B-tubules end, they open up, forming hook-shaped projections from the A-tubules. The gradual reduction in length of these hook-shaped structures suggests that near their distal ends each B-tubule opens because of the separation of protofilament 1 of the B-tubule from protofilament 1 of the adjacent A-tubule. Subsequently, the B-tubule protofilaments terminate individually.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 60 (1983), S. 107-112 
    ISSN: 1432-0533
    Keywords: Lymphoid cell adhesiveness ; Endothelium ; Antibody-antigen interaction ; Pathogenic mechanism ; Viral encephalitis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary One of the enigmas in the pathogenesis of inflammation is why the white cells adhere to the endothelium. In trying to define the pathogenic mechanism, we carried out experiments on ferrets infected with an SSPE strain of measles virus. Using immunoperoxidase labeling techniques, viral antigens were demonstrated on the luminal surface and in the cytoplasm of endothelial cells, irrespective of the presence or absence of inflammatory changes. The degree of inflammation corresponded well with antibody titer. These data suggest that the viral antigen in the endothelial cells is the site of interaction between these cells and sensitized lymphoid cells.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 63 (1984), S. 190-197 
    ISSN: 1432-0533
    Keywords: Aluminum ; Neurofibrillary changes ; Axons ; Rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We examined the chronic effect of aluminum on the rabbit central nervous system (CNS) and documented the occurrence of axonal swellings (spheroids) and dendritic thickening in spinal cord neurons in addition to the accumulation of neurofibrillary material in the perikaryon. The axonal swellings always occurred at the first heminode, and the neurofilaments appeared disorganized, whereas in dendrites the neurofilaments generally retained their longitudinal arrangements. Although neurofibrillary tangles were present in cortical neurons, no axonal swellings were observed. Thickening of segments of apical dendrites proximal to the cell body affected by neurofibrillary changes was present. The axonal swellings resembled those observed in IDPN intoxication, and in amyotrophic lateral sclerosis, and may be useful as a model for studying these diseases.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-0533
    Keywords: Ultrastructural cytochemistry ; Concanavalin A receptors ; 5′-Nucleotidase ; Blood-brain barrier ; Vesiculo-canalicular transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Plant lectin concanavalin A conjugated with ferritin (Con A-F) injected i.v. was used for the detection of the specific monosaccharide residues (α-d-mannosyl and α-d-glucosyl) on the luminal surface of endothelial cells (ECs) in brain micro-blood vessels (MBVs). Both normal mice and animals with mechanically damaged blood-brain barrier (BBB) were used in this study. In addition, the activity of 5′-nucleotidase (5′N), the putative receptor for Con A, was studied cytochemically. Various methodologic experiments indicated that the reaction product formed on the luminal plasmalemma of ECs after incubation of samples in the cytochemical medium for the detection of 5′N activity results from the action of unspecific phosphatase hydrolyzing both specific and nonspecific substrates. The abluminal side of the wall of MBVs seems to be a major location of 5′N activity. Thus, no correlation between cytochemically demonstrable 5′N activity and Con A receptor sites on the luminal surface of ECs was noted. After damage of the BBB, extensive internalization of the luminal plasmalemma forming the limiting membranes of pinocytotic vesicles, vacuoles, and endothelial channel-like structures was observed. This process was represented by a relatively rapid translocation of Con A receptors from luminal surface into the interior of the ECs and to the abluminal side of the vessel wall.
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 1432-0533
    Keywords: Blood-brain barrier ; Endothelial cells ; Horseradish peroxidase ; Native ferritin ; Alkaline phosphatase ; Pinocytic transport system ; Canalicular transport system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary An ultracytochemical investigation was performed to study the origin of pinocytic vesicles and canalicular structures within endothelial cells (EC) of the injured mammalian blood-brain barrier (BBB). To accomplish this goal, two electron-dense tracers, native ferritin (NF) and horseradish peroxidase (HRP), were used in conjunction with the detection of alkaline phosphatase (AP) activity, a known marker of EC plasmalemma of brain micro-blood vessels. Brain ECs from (1) mice subjected to crude leptomeningeal damage for 1, 2, or 3 days and (2) cats subjected to cold lesion injury for 1, 4, or 24h were evaluated for tracer transport and AP activity. Fine structural analysis of leaking segments of micro-blood vessels from damaged cerebral cortex or basal ganglia demonstrated pinocytic vesicles, deep invaginations of the luminal plasmalemma and elongated, tubular profiles, all containing tracer. Because we observed in ECs from both experimental models of brain injury a positive reaction for AP activity in the luminal plasmalemma, in its deep invaginations, in deliminating membranes of pinocytic vesicles, and in tubulo-canalicular structures, we conclude that all types of transport structures derive from the same 100Å thick exoplasmic plasmalemmal membranes. Further, besides the pinocytic vesicular transport system (PTS), the canalicular transport system (CTS) appears to serve as an additional important mechanism for macromolecular transport across the damaged mammalian BBB.
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 1432-0533
    Keywords: Non-congophilic granules ; Neuritic plaques ; Corpora amylacea ; Polyglucosan deposits
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Brightly birefringent granular profiles were revealed by examination of samples of fractionated human cerebral cortex in the polarizing microscope. These profiles resemble a plant starch granule in the light microscope and appear to be pure polysaccharide by chemical and histochemical analysis. Localization of this profile in routine 5 μm tissue sections was difficult because the hardness of the granule allows it to be easily displaced by the microtome knife. This fact might easily lead an investigator to believe these granules are artifactual, thus probably accounting for the lack of information about this interesting profile.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 53 (1981), S. 107-112 
    ISSN: 1432-0533
    Keywords: Dendrites ; Purkinje cells ; Golgi stain ; Experimental phenylketonuria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A comparison was made of cerebellar dendritic development in the normal rat and in a new model of phenylketonuria, the phenylacetate-treated suckling rat. Golgi stain analysis of the Purkinje cells shows striking regional variations in the dendritic growth. These variations were observed in both the control and phenylacetate-treated animals and were especially striking before 15 days of life. Quantitative analysis of the dendritic tree revealed, in the phenylacetate-treated rat, a significant reduction in the total number of dendritic branches. However, the individual terminal dendritic length was largely unaltered. These effects of phenylacetate differ from those of deafferentation and starvation. Results of this investigation clearly define the harmful effects of phenylacetate on developing neurons and are compatible with the clinical observation that brain damage in phenylketonuria occurs mainly during the first few years of life, the critical period of neuronal development.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 62 (1984), S. 259-267 
    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
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