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  • 1
    Electronic Resource
    Electronic Resource
    Matrix Metalloproteinases in the Neocortex and Spinal Cord of Amyotrophic Lateral Sclerosis Patients (1996)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 67 (1996), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Matrix metalloproteinases (MMPs) were analyzed by immunohistochemistry and zymography in amyotrophic lateral sclerosis (ALS) and control brain and spinal cord specimens. Three major bands of enzyme activity (70, 100, and 130 kDa) were consistently observed and were subsequently identified as MMP-2 (70 kDa; also known as EC 3.4.24.24 or gelatinase A) and MMP-9 (100 and 130 kDa; also known as EC 3.4.24.35 or gelatinase B). Immunohistochemical studies established the presence of MMP-2 in astrocytes and MMP-9 in pyramidal neurons in the motor cortex and motor neurons in the spinal cord of ALS patients. Although a significant decrease in MMP-2 activity was noticed in the ALS motor cortex, statistically significant increases in MMP-9 (100-kDa) activity were observed in ALS frontal and occipital cortices (BA10 and 17) and all three spinal cord regions when compared with control specimens. The highest MMP-9 (100-kDa) activities in ALS were found in the motor cortex and thoracic and lumbar cord specimens. The abnormally high amount of MMP-9 and its possible release at the synapse may destroy the structural integrity of the surrounding matrix, thereby contributing to the pathogenesis of ALS.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1996.67010251.x
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  • 2
    Electronic Resource
    Electronic Resource
    Somataglycan-S: A Neuronal Surface Proteoglycan Defines the Spinocerebellar System (1994)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 62 (1994), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The formation and maintenance of functionally specific neuronal networks may depend on specific proteoglycans localized to the surface membranes of a subset of neurons. Monoclonal antibody (MAb) 6A2 labeled a distinct subset of CNS neurons: the somas and proximal dendrites of cells making up the spinocerebellar and reticular systems. These pathways contribute to proprioceptive and exteroceptive functions. Ultrastructurally, MAb 6A2 immunoreactivity was distributed focally along the cell surface membranes and the adjacent extracellular space. On western blots of immunoaffinity-purified preparations from cerebellar homogenates, a major, broad band of ∼400 kDa is labeled by MAb 6A2. Increased electrophoretic mobility of the purified antigen after digestion with chondroitinase ABC and keratanase suggests that the antigen is a proteoglycan bearing chondroitin sulfate and keratan sulfate glycosaminoglycans. Unsulfated N-acetyl- galactosamine residues linked to unsaturated uronic acid constituted the initial disaccharide in the chondroitin sulfate glycosaminoglycan chains. N- and O-linked oligosac- charides on the core protein were detected by the biotinylated lectins wheat germ agglutinin and Jacalin, respectively, and by MAb anti-HNK-1. Lyase and glycosidase digests result in a 280-kDa band. This proteoglycan, somataglycan-S, may provide a key to the role of glycoconjugates in determining neuronal diversity and system specificity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1994.62041615.x
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of Neutral Proteinases from Alzheimer-Affected and Control Brain Specimens: Identification of Calcium-Dependent Metalloproteinases from the Hippocampus (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 58 (1992), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Three neutral proteinases from human hippocam-pal tissue have been identified and partially characterized using substrate gel electrophoresis. The proteinases showed activity when gelatin was used as the substrate, but had no detectable activity against casein. Based on the results of inhibition studies and the calcium requirements, it was concluded that the activities were due to calcium-dependent me-talloproteinases. The apparent molecular weights were 130,000 (MP-130), 100,000 (MP-100), and 70,000 (MP-70). Half-maximal activities were observed with 20 μM Ca2+ for MP-130,40 μM Ca2+ for MP-100, and 800 μM Cn2+ for MP-70. In the presence of Ca2+, Zn2+ reestablished the activities of the three metalloproteinases at a lower concentration than did either Co2+ or Mn2+. One millimolar Al3+ inhibited 67% of the MP-70 activity, but did not affect the MP-100 and MP-130 activities. An analysis of Alzheimer-affected hip-pocampal and control samples showed that the specific activity (in units per milligram of sodium dodecyl sulfate-soluble protein) of MP-70 varied less than the activities of MP-100 and MP-130 between the two groups. Although p-amino-phenylmercuric acetate (p-APMA) increased the activities of MP-70 by 70% in both groups of specimens, the resulting activities from Alzheimer samples were greater than those from control samples (p 〈 0.01). A wide range of MP-100 specific activity was observed in both groups, and its mean activity was higher in Alzheimer-affected samples (p 〈 0.05). Treatment with p-APMA increased the activity of MP-100 only 25% in both groups of tissue samples. MP-130 activity was detected predominantly in Alzheimer-affected hippo-campal specimens, and treatment with p-APMA failed to increase its activity in both the control and the Alzheimer-affected specimens. The results demonstrate an elevated level of metalloproteinase activities, capable of degrading tissue matrix components, in the hippocampus from postmortem Alzheimer patients.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1992.tb09352.x
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  • 4
    Electronic Resource
    Electronic Resource
    Carbonyl-Related Posttranslational Modification of Neurofilament Protein in the Neurofibrillary Pathology of Alzheimer's Disease (1995)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 64 (1995), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: We present the first evidence for carbonyl-related posttranslational modifications of neurofilaments in the neurofibrillary pathology of Alzheimer's disease (AD). Two distinct monoclonal antibodies that consistently labeled neurofibrillary tangles (NFTs), neuropil threads, and granulovacuolar degeneration in sections of AD tissue also labeled the neurofilaments within axons of the white matter following modification by reducing sugars, glutaraldehyde, formaldehyde, or malondialdehyde. The epitope recognized by these two antibodies shows a strict dependency for carbonyl modification of the neurofilament heavy subunit. The in vivo occurrence of this neurofilament modification in the neurofibrillary pathology of AD suggests that carbonyl modification is associated with a generalized cytoskeletal abnormality that may be critical in the pathogenesis of neurofibrillary pathology. Furthermore, the data presented here support the idea that extensive posttranslational modifications, including oxidative stress-type mechanisms, through the formation of cross-links, might account for the biochemical properties of NFTs and their resistance to degradation in vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.1995.64062660.x
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  • 5
    Electronic Resource
    Electronic Resource
    Detecting bioactive amyloid β peptide species in Alzheimer's disease (2004)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 91 (2004), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Amyloid β peptide (Aβ) is believed to play a central role in the pathogenesis of Alzheimer's disease (AD). However, the form of Aβ that induces neurodegeneration in AD, defined here as bioactive Aβ, is not clear. Preventing the formation of bioactive Aβ or inactivating previously formed bioactive Aβ should be a promising approach to treat AD. We have previously developed a cell-based assay for the detection of bioactive Aβ species. The assay is based upon the correlation between the ability of an Aβ sample to induce a unique form of cellular MTT [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] formazan exocytosis, and its ability to activate glia and induce neurotoxicity. Here, we show that this cell-based assay is not only useful for a cellular model of Aβ amyloidogenesis but is also able to detect bioactive Aβ species in a transgenic mouse model of AD, as well as in post-mortem cortex samples from AD patients. There is a good correlation between the extent of glia activation and the level of bioactive Aβ species in the mouse brain. A promising deuteroporphyrin that can inactivate bioactive Aβ species was also identified using this assay. These novel insights and findings should have important implications for the treatment of AD.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.2004.02751.x
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  • 6
    Electronic Resource
    Electronic Resource
    EFFECTS OF ALUMINUM SALTS ON CULTURED NEUROBLASTOMA CELLS (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 22 (1974), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Experimental induction of neurofibrillary tangles was demonstrated several years ago in the central nervous system of rabbits injected with aluminum salts. In the current studies, neuroblastoma cells, capable of morphologic and biochemical differentiation in monolayer culture, have been exposed to medium containing aluminum phosphate; such treatment resulted in an abundant accumulation of 100 Å neurofilaments after 6 days of continous exposure to the aluminum salt. While growth rates and incorporation of radioactive thymidine in treated cells remained similar to controls, total cellular protein, and incorporation of radioactive leucine were significantly increased. Paradoxically, when the protein content of aluminum-treated cultures was maximal, these cultures contained about 20 per cent less ribosomal RNA per cell than in control cultures. In addition, activity of an important neuronal protein, i.e. acetylcholinesterase, was depressed in treated cultures to a level below control values. Both temporal and morphologic similarities between treated neuroblastoma cultures and animals injected with aluminum salts suggest that the observed changes in macromolecular synthesis in cell culture are relevant to in vivo studies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1974.tb04290.x
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  • 7
    Electronic Resource
    Electronic Resource
    Demyelination with hemophagocytic lymphohistiocytosis of the CNS (1981)
    Springer
    Acta neuropathologica 54 (1981), S. 153-155 
    Details
    ISSN: 1432-0533
    Keywords: CNS demyelination ; Histiocytosis ; Immunodepletion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A case of hemophagocytic lymphohistiocytosis with central nervous system involvement in an infant is presented. Marked demyelination of cerebral and cerebellar white matter is associated with an intense histiocytic infiltration and astrogliosis. Histiocytes phagocytic of erythrocytes and lymphocytes are noted in a meningeal, subependymal, and perivascular distribution. Severe depletion of lymphoid tissue, associated with histiocytic infiltration, is also seen in multiple organs. While the etiology of this disease is unknown, alterations in the immune response and possible viral relationships are explored.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00689409
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  • 8
    Electronic Resource
    Electronic Resource
    Secretory ependymoma of the filum terminale (1970)
    Springer
    Acta neuropathologica 15 (1970), S. 240-250 
    Details
    ISSN: 1432-0533
    Keywords: Ependymoma ; Electron Microscopy ; Secretory Granules ; Histochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Ein unikales Ependymom des Filum terminale mit intracytoplas-matischen Sekretgranula wurde licht- und elektronenmikroskopisch nachgewiesen. Auffallende strukturelle und histochemische Änlichkeiten bestehen zwischen den Sekretionsprodukten des Tumors und denen im sekretorischen System des Endabschnittes des Rückenmarks bei Fischen. Die Funktion und der Wirkungsort des Sekretionsproduktes sind unbekannt.
    Notes: Summary An unique ependymoma of the filum terminale with intracytoplasmic secretory granules has been identified by light and electron microscopy. A striking structural and histochemical similarity exists between the tumor secretory product and that found in the secretory system present in the terminal portion of the spinal cord of the fish. The function and site of action of the secretory product is unknown.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00686770
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  • 9
    Electronic Resource
    Electronic Resource
    Axonal transport of neuronal antigens characteristic of subpopulations of central nervous system (CNS) neurons (1989)
    Springer
    Metabolic brain disease 4 (1989), S. 157-167 
    Details
    ISSN: 1573-7365
    Keywords: axonal transport ; guinea pig ; monoclonal antibodies ; retinal ganglion cell
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Monoclonal antibodies (MAbs) are useful for the identification of nervous system antigens localized to neuronal subpopulations. We have examined the transport of the corresponding antigens of four such MAbs in guinea pig retinal ganglion-cell axons. Determination of the axonal transport rate of radiolabeled antigens allowed their assignment to one of the three major anterograde axonal transport rate components, each of which is through to convey a subcellular structural system in the axon. Antigens identified by three of the MAbs were found to be transported in slow component b of axonal transport, the component thought to convey the cytoplasmic matrix, and an antigen identified by the fourth MAb was found in slow component a, similarly thought to contain the linear cytoskeletal elements. Assignment of these antigens to the different rate components suggests that they may be associated with a particular structural system in neurons. Additionally, in cases where more than one nervous system cell type may express a particular antigen, the identity of the neuronal form of the antigen has been confirmed by its axonal transport. The roles that these antigens may play in the nervous system during normal axonal function and during neuropathogenesis can now be further examined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01000292
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  • 10
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    Nanoaggregates of Diverse Asphaltenes by Mass Spectrometry and Molecular Dynamics (2017)
    American Chemical Society (ACS)
    Details
    Publication Date: 2017-09-07
    Description: Energy & Fuels DOI: 10.1021/acs.energyfuels.7b01420
    Print ISSN: 0887-0624
    Electronic ISSN: 1520-5029
    Topics: Chemistry and Pharmacology , Energy, Environment Protection, Nuclear Power Engineering , Process Engineering, Biotechnology, Nutrition Technology
    Published by American Chemical Society (ACS)
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