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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 61 (1993), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: The microtubule-associated protein τ is found primarily in neuronal tissues and is highly enriched in the axon. It promotes microtubule assembly in vitro and stabilizes microtubules in cells. To study how τ protein might be involved in the unique features of axonal microtubules, we have analyzed the effect of E. coli-synthesized τ protein using an in vitro centrosome-mediated microtubule regrowth assay over a wide range of τ/tubulin ratios. We report that microtubule assembly promoted by τ protein exhibits characteristic changes dependent on the τ/tubulin ratio. Above a threshold level, nucleation of new microtubules is favored over growth of existing ones, τ isoform variation does not change this phase transition in microtubule assembly. We discuss how τ might participate in the elaboration of axonal morphology based on our results and present evidence that the phase transition from microtubule growth to nucleation is critical for axonal development.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford UK : Blackwell Science Ltd
    Journal of neurochemistry 73 (1999), S. 0 
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: To determine the effect of neurotrophins on the survival and morphological differentiation of CNS neurons, we examined NT2-N cells, which provide a unique culture model for terminally differentiated and polar human neurons. Here we report the development of conditions for the long-term culture of NT2-N cells in low density and in chemically defined medium. We show that NT2-N cells express mRNAs for TrkA, TrkB, and TrkC tyrosine kinase receptors and the low-affinity nerve growth factor receptor (p75NTR). All members of the nerve growth factor-related family of neurotrophic factors promote neuronal survival in long-term cultures with ∼1 ng/ml for half-maximal survival. At high concentrations (〉20 ng/ml), the neurotrophins reversed the survival-promoting effect as judged by MTT [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] conversion. In contrast to the uniform effect of all neurotrophins on neuronal survival, brain-derived neurotrophic factor selectively induced an increased dendritic complexity. These results demonstrate that NT2-N cells provide a useful model to analyze the effect of neurotrophins on the survival and morphological differentiation of CNS neurons in vitro. In addition, the data indicate that neuronal survival and the development of morphological complexity are differentially regulated in a multireceptor context.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of cardiovascular electrophysiology 6 (1995), S. 0 
    ISSN: 1540-8167
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Bradycardia-Induced Polymorphic VT. In a patient with severe left ventricular dysfunction resulting from chronic nonparoxysmal sinus tachycardia, rate control and improvement in left ventricular function were achieved with atrioventricular junction ablation and ventricular pacemaker implantation. Within 12 hours after the ablation procedure, several episodes of polymorphic ventricular tachycardia that may have been triggered by the abruptly decreased heart rate occurred. Recurrence of polymorphic ventricular tachycardia was prevented by an increase in pacing rate.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 292 (1998), S. 181-189 
    ISSN: 1432-0878
    Keywords: Key words Microtubules ; Microfilaments ; Neurofilaments ; Neuronal development
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The use of modern techniques involving gene transfer and functional knock-out strategies has lead to new concepts of the way in which cytoskeletal elements interact to produce the unique morphologies of neurons. This review presents these concepts and discusses their implications for neuronal development, especially with respect to the role of microtubules, microfilaments, and neurofilaments.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 28 (1994), S. 143-154 
    ISSN: 0886-1544
    Keywords: microtubule-associated proteins ; microtubule nucleation ; tubulin ; cytoskeleton ; axon ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The neuronal microtubule-associated protein tau has been implicated in the development of axonal morphology including the organization of microtubules into a uniformly oriented array of microtubules commonly referred to as “bundle.” Determination of the functional organization of tau has revealed that regions of tau protein which flank the microtubule-binding domain affect the bundling of microtubules in vitro with a microtubule-binding fragment of tau being most effective [Brandt and Lee, 1993: J. Biol. Chem. 268:3414-3419]. In order to study the relation of microtubule bundles that form in vitro to those observed in the axon, we determined the orientation of individual microtubules in bundles and the effects of bundling on microtubule assembly and stability in cell-free assembly reactions. Here we report that bundles induced by a microtubule-binding fragment of tau contain randomly oriented microtubules as determined by using the difference in growth rates at microtubule plus and minus ends. We demonstrate that in vitro bundling increases microtubule growth (about 30%), stabilizes microtubules against dilution- and cold-induced disassembly, and allows microtubule nucleation despite the absence of a tau region which has previously been shown to be required for tau-dependent microtubule nucleation. We conclude that conditions that stabilize microtubules can lead to bundle formation and allow microtubule assembly by a mechanism different from that employed by microtubule-associated proteins. The data also support the view that additional mechanisms besides the action of tau and tubulin exist in order to organize microtubules in the axon. © 1994 Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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