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  • 1
    Electronic Resource
    Electronic Resource
    GANGLIOSIDES IN NERVOUS TISSUE CULTURES AND BINDING OF 125I-LABELLED TETANUS TOXIN, A NEURONAL MARKER (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 29 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— —Continuous cell lines, primary cell cultures derived from embryonic CNS, and homogenates made from adult and embryonic CNS were compared with respect to their lipid pattern and their ability to bind 125I-labelled tetanus toxin. In parallel experiments de novo synthesis of gangliosides in the cell lines was studied, using [14C]glucosamine as precursor. Of the total lipid only gangliosides were specifically labelled by [14C]glucosamine. The patterns of the de novo synthesized gangliosides corresponded to those present in the respective cells.Pronounced binding of 125I-labelled toxin was only detectable in tissues containing long-chain gangliosides (ganglioside C which represents GDIb and GTI).Accordingly, hybrid (neuroblastoma x glioma) cells, due to their lack of long-chain gangliosides, bound just-discernible amounts of labelled toxin. When previously exposed to gangliosides, their binding of tetanus toxin tremendously increased.It was concluded that only the long-chain gangliosides in the neuronal cells are functionally involved in the binding of the tetanus toxin and that these acceptors of tetanus toxin can be transplanted.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb09626.x
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  • 2
    Electronic Resource
    Electronic Resource
    BINDING CHARACTERISTICS OF 125I-LABELLED TETANUS TOXIN TO PRIMARY TISSUE CULTURES FROM MOUSE EMBRYONIC CNS (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 29 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— The interaction of 125I-labelled tetanus toxin with cells in tissue cultures derived from embryonic CNS has been studied.The optimum toxin binding occurs about 2–3 weeks after transfer of the cells to culture conditions. The amount of label bound per culture was doubled at this time in comparison to the fourth day nfter inoculation.The amount of toxin bound depends on the concentration applied. It reaches its maximum 8 h after application then decreases slowly. Low amounts of radioactivity were still detectable 97 h after washing off the unbound toxin. Up to 80% of the label can be replaced by simultaneous application of‘cold’toxin. Fixation of the toxin is higher at 4°C than at 37°C.Preincubation of the cultures with neuraminidase prevents about 75% of the binding. The presence of cytochalasin B leads to a small but reproducible decrease of binding, whereas colchicine had no measurable effect.The radioactive (1251) material was identified by a double-isotope technique in disc gel electrophoresis before and after reductive cleavage of its disulphide bonds. In every test is was indistinguishable from 131I-labelled toxin added as standard.Our results largely parallel those obtained with synaptosomes and other systems. They suggest that gangliosides might be the acceptor molecules, and that the culture system will be suitable for studying the actions of this toxin in vitro.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb06516.x
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  • 3
    Electronic Resource
    Electronic Resource
    Inhibition by tetanus and botulinum A toxin of the release of [3H]noradrenaline and [3H]GABA from rat brain homogenate (1988)
    Springer
    Cellular and molecular life sciences 44 (1988), S. 224-226 
    Details
    ISSN: 1420-9071
    Keywords: Tetanus toxin ; botulinum toxin ; noradrenaline ; GABA ; brain
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Rat brain homogenate was preloaded with [3H]noradrenaline or [3H]GABA and stimulated with high K+. Tetanus toxin and botulinum A neurotoxin partially prevent the evoked [3H]noradrenaline release in the same range of toxin concentrations starting below 10−10M. In contrast, release of γ-amino butyric acid (GABA) is much more sensitive to tetanus than to botulinum A toxin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01941714
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  • 4
    Electronic Resource
    Electronic Resource
    Depolarization increases inositolphosphate production in a particulate preparation from rat brain (1986)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 334 (1986), S. 1-9 
    Details
    ISSN: 1432-1912
    Keywords: Depolarization ; Ion channels ; Phosphatidylinositol ; Inositol phosphates ; Voltage-dependence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary We have studied the accumulation of inositol phosphates (InsP) due to depolarization. A particulate preparation of rat brain was introduced to rule out transmitter activated mechanisms and to allow free access for drugs of high molecular weights. Potassium depolarization doubled InsP within a few minutes. InsP accumulation depended on time and K+ concentration, and was affected neither by tetrodotoxin nor by atropine. Radioactive metabolites co-eluted with inositol mono-phosphate and inositol bis-phosphate, whereas only minor amounts appeared with inositol tris-phosphate. The content in phosphatidylinositols was decreased. No evidence was found for the involvement of a neurotransmitter. Sea anemone toxin II (around 1 μmol/l), which keeps the Na+-channels open, promoted the InsP accumulation in an atropine-resistant manner. Tetrodotoxin prevented it when given before, and inhibited it when given after initiation by sea anemone toxin II. Moreover the K+ channel blockers 4-aminopyridine, dendrotoxin and tetraethylammonium all caused InsP accumulation. Palytoxin was by far the most potent promoter of InsP accumulation with a detection limit below 10 pmol/l, and displayed a unique bell-shaped concentration-effect correlation. Ouabain (3 μmol/l) and above) also elicited the InsP accumulation. The response to carbachol was not only inhibited completely by atropine, but also partially (more than 50%) by tetrodotoxin, which indicates the involvement of voltage-dependent sodium channels in the receptor-triggered InsP accumulation. Thus independent of the causative agent, depolarization promotes an InsP accumulation. We conclude that degradation of phosphatidylinositols is mediated not only by receptor occupation but also by a positive shift in membrane voltage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00498733
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  • 5
    Electronic Resource
    Electronic Resource
    Oxoferin® und Natriumchlorit — Ein Vergleich (1989)
    Springer
    Journal of molecular medicine 67 (1989), S. 20-25 
    Details
    ISSN: 1432-1440
    Keywords: Oxoferin® ; Sodium chlorite ; Methaemoglobin ; Fibroblast ; Oxidant
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Oxoferin®, a preparation approved for wound treatment, has been subjected to an in vitro analysis. 1. Oxoferin® produces methaemoglobin even if diluted 500fold, and leads to additional alterations if added in high concentrations to red cells. Sodium chlorite (NaClO2, 15 mM) is equivalent to undiluted Oxoferin®. 2. Oxoferin® in fiftyfold dilution damages fibroblasts in cell culture slowly and persistently. This dilution is equieffective with a 200 µM solution of sodium chlorite. Oxoferin® and sodium chlorite also damage vascular endothelial cells. 3. The oxidation equivalent of Oxyoferin® is 12.3 mM sodium chlorite. Our data indicate that Oxoferin® may be equated essentially with aqueous sodium chlorite.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01736530
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  • 6
    Electronic Resource
    Electronic Resource
    Erwiderung (1989)
    Springer
    Journal of molecular medicine 67 (1989), S. 742-742 
    Details
    ISSN: 1432-1440
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01721297
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  • 7
    Electronic Resource
    Electronic Resource
    Botulinum C2 toxin ADP-ribosylates actin (1986)
    [s.l.] : Nature Publishing Group
    Nature 322 (1986), S. 390-392 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Botulinum C2 toxin is a binary toxin and consists of two components, C2-I and C2-II, with relative molecular masses (Mrs) of 50K and 100K, respectively4. Both components are actually completely separate proteins which interact to cause the toxic effects. The 50K component, which is non-toxic in ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/322390a0
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  • 8
    Electronic Resource
    Electronic Resource
    Direct evidence for the specific fixation of Cl. Botulinum A neurotoxin to brain matter (1975)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 287 (1975), S. 97-106 
    Details
    ISSN: 1432-1912
    Keywords: Tetanus Toxin ; Botulinum A Toxin ; Synaptosomes ; Neuraminic Acid ; Fixation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. Rat brain homogenate and synaptosomes from rat brain bind botulinum toxin. The binding is accompanied by partial inactivation. The binding decreases with increasing ionic strength. A considerable fixation of tetanus toxin can still be demonstrated under conditions which prevent the fixation of botulinum toxin. 2. Only the grey substance, not the white substance from bovine brain is able to bind the toxin. 3. Upon pretreatment with neuraminidase, synaptosomes lose nearly all of their binding capacity. However, neither gangliosides nor ganglioside-cerebroside mixtures nor brain extracts could replace the synaptosomes. Thus botulinum A toxin closely resembles tetanus toxin in its ability to react with (a) neuraminidase-sensitive site(s) of the grey matter of the CNS. It differs from tetanus toxin by its stronger sensitivity against ionic forces and by its failure to react with certain gangliosides.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00632641
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  • 9
    Electronic Resource
    Electronic Resource
    Transmembranal and intracellular transport of pharmacologically active proteins and polypeptides (1977)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 297 (1977), S. S11 
    Details
    ISSN: 1432-1912
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00587763
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  • 10
    Electronic Resource
    Electronic Resource
    Neurotoicity of apamin and MCD peptide upon central application (1977)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 300 (1977), S. 189-191 
    Details
    ISSN: 1432-1912
    Keywords: Neurotoxins ; Spinal cord ; Bee venom ; Apamin ; MCD peptide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Besides apamin, the structurally related MCD peptide (mast cell degranulating peptide; peptide 401) is another centrally acting peptide from bee venom. In contrast to apamin, it is hardly neurotoxic upon intravenous injection in mice. Following intraventricular injection, as little as 0.3 μg/animal produce convulsions and respiratory arrest in mice. The clinical picture differs from that elicited by apamin, and apamin is about 10 times more potent than MCD peptide when given intraventricularly. Apamin and MCD peptide, injected into the spinal cord of rats in nanogram amounts, produce circumscript hyperexcitation lasting more than one day, however with complete recovery following sublethal doses. Local apamin poisoning differs from local tetanus (elicited by the same way) by its faster time course.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00505050
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