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  • Articles  (3)
  • Alzheimer's disease  (2)
  • Calcium displacement  (1)
  • Springer  (3)
  • American Association of Petroleum Geologists
  • 2010-2014
  • 1995-1999  (2)
  • 1990-1994  (1)
  • 1970-1974
  • 1905-1909
  • Biology  (3)
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  • Articles  (3)
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  • Springer  (3)
  • American Association of Petroleum Geologists
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  • 2010-2014
  • 1995-1999  (2)
  • 1990-1994  (1)
  • 1970-1974
  • 1905-1909
    • +
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  • Biology  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Al3+-Ca2+ interactions in aluminum rhizotoxicity (1993)
    Springer
    Planta 192 (1993), S. 104-109 
    Details
    ISSN: 1432-2048
    Keywords: Aluminum toxicity ; Calcium displacement ; Electrical potential ; Root ; Triticum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Several mineral rhizotoxicities, including those induced by Al3+, H+, and Na+, can be relieved by elevated Ca2+ in the rooting medium. This leads to the hypothesis that the toxic cations displace Ca2+ from transport channels or surface ligands that must be occupied by Ca2+ in order for root elongation to occur. In this study with wheat (Triticum aestivum L.) seedlings, we have determined, in the case of Al3+, that (i) Ca2+, Mg2+, and Sr2+ are equally ameliorative, (ii) that root elongation does not increase as Ca2+ replaces Mg2+ or Sr2+ in the rooting media, and (iii) that rhizotoxicity is a function solely of Al3+ activity at the root-cell membrane surface as computed by a Gouy-Chapman-Stern model. The rhizotoxicity was indifferent to the computed membrane-surface Ca2+ activity. The rhizotoxicity induced by high levels of tris(ethylenediamine)cobaltic ion (TEC3+), in contrast to Al3+, was specifically relieved by Ca2+ at the membrane surface. The rhizotoxicity induced by H+ exhibited a weak specific response to Ca2+ at the membrane surface. We conclude that the Ca2+-displacement hypothesis fails in the case of Al3+ rhizotoxicity and that amelioration by cations (including monovalent cations) occurs because of decreased membrane-surface negativity and the consequent decrease in the membrane-surface activity of Al3+. However, TEC3+, but not Al3+, may be toxic because it inhibits Ca2+ uptake. The nature of the specific H+-Ca2+ interaction is uncertain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00198699
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  • 2
    Electronic Resource
    Electronic Resource
    The Order of Exposure of Tau to Signal Transduction Kinases Alters the Generation of “AD-Like” Phosphoepitopes (1999)
    Springer
    Cellular and molecular neurobiology 19 (1999), S. 223-233 
    Details
    ISSN: 1573-6830
    Keywords: tau ; kinases ; signal transduction ; Alzheimer's disease ; phosphorylation ; paired helical filaments
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. The individual and sequential influence of protein kinase C (PKC), protein kinase A (PKA) and mitogen-activated protein kinase (MAP kinase) on human brain tau was examined. 2. A range of PKC concentrations generated certain phosphoepitopes common with paired helical filaments. These epitopes were masked by higher PKC concentrations, suggesting the presence of multiple tau phosphorylation sites for which PKC exhibited differing affinities and/or conformational alterations in tau induced by sequential PKC-mediated phosphorylation. 3. Prior phosphorylation by PKC enhanced the nature and extent of AD-like tau antigenicity generated by subsequent incubation with MAP kinase yet inhibited that generated by subsequent incubation with PKA. 4. Dephosphorylation of tau prior to incubation with kinases significantly altered the influence of individual and multiple kinase incubation on tau antigenicity in a site-specific manner, indicating that prior in situ phosphorylation events markedly influenced subsequent cell-free phosphorylation. 5. In addition to considerations of the potential impact of tau phosphorylation by individual kinases, these findings extend previous studies which indicate that tau antigenicity, and, presumably, its behavior in situ, is influenced by the sequential and convergent influences of multiple kinases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006977127422
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  • 3
    Electronic Resource
    Electronic Resource
    Hyperactivation of Mitogen-Activated Protein Kinase Increases Phospho-Tau Immunoreactivity Within Human Neuroblastoma: Additive and Synergistic Influence of Alteration of Additional Kinase Activities (1999)
    Springer
    Cellular and molecular neurobiology 19 (1999), S. 249-260 
    Details
    ISSN: 1573-6830
    Keywords: MAP kinase ; tau ; protein kinase C ; wortmannin ; PD98059 ; neuroblastoma ; Alzheimer's disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mitogen-activated protein (MAP) kinase phosphorylates tau in cell-free analyses, but whether or not it does so within intact cells remains controversial. In the present study, microinjection of MAP kinase into SH-SY-5Y human neuroblastoma cells increased tau immunoreactivity toward the phosphodependent antibodies PHF-1 and AT-8. In contrast, treatment with a specific inhibitor of MAP kinase (PD98059) did not diminish “basal” levels of these immunoreactivities in otherwise untreated cells. These findings indicate that hyperactivation of MAP kinase increases phospho-tau levels within cells, despite that MAP kinase apparently does not substantially influence intracellular tau phosphorylation under normal conditions. These findings underscore that results obtained following inhibition of kinase activities do not necessarily provide an indication of the consequences accompanying hyperactivation of that same kinase. Several studies conducted in cell-free systems indicate that exposure of tau to multiple kinases can have synergistic effects on the nature and extent of tau phosphorylation. We therefore examined whether or not such effects could be demonstrated within these cells. Site-specific phospho-tau immunoreactivity was increased in additive and synergistic manners by treatment of injected cells with TPA (which activates PKC), calcium ionophore (which activates calcium-dependent kinases), and wortmannin (which inhibits PIP3 kinase). Alteration in total tau levels was insufficient to account for the full extent of the increase in phospho-tau immunoreactivity. These additional results indicate that multiple kinase activities modulate the influence of MAP kinase on tau within intact cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006981228331
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