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  • Alzheimer's disease  (3)
  • Triticum  (2)
  • calcium  (2)
  • Springer  (7)
  • American Meteorological Society (AMS)
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  • Springer  (7)
  • American Meteorological Society (AMS)
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  • 1
    Electronic Resource
    Electronic Resource
    Calmodulin-like activity in a mineralising tissue: The rat molar tooth germ (1981)
    Springer
    Calcified tissue international 33 (1981), S. 545-548 
    Details
    ISSN: 1432-0827
    Keywords: calmodulin ; calcium ; mineralisation ; tooth germ
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Calmodulin, a calcium binding protein, has been implicated in the regulation of many calcium-dependent biological processes. Since calcium has an important role in hard tissue genesis, both at intra- and extracellular levels, we anticipate that calcium binding proteins may modulate this process. The present study investigated a mineralising tissue, the rat molar tooth germ, to determine the presence of calmodulin-like activity. A heat-treated cell-free extract of tooth germs provided enhancement of Ca2+-dependent Mg2+-ATPase and 3′:5′-nucleotide phosphodiesterase activity. No enhancement occurred in the absence of calcium or in the presence of trifluoperazine. SDS-polyacrylamide gel electrophoresis of this extract revealed a protein band of approximately 18,000 mol. wt. These findings indicate the presence of calmodulin-like activity in rat molar tooth germs and support the proposal that calcium and calcium binding proteins, in particular calmodulin, have a major regulatory role in the biology of mineralising tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02409487
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Al3+-Ca2+ interactions in aluminum rhizotoxicity (1993)
    Springer
    Planta 192 (1993), S. 98-103 
    Details
    ISSN: 1432-2048
    Keywords: Aluminum toxicity ; Calcium uptake ; Growth inhibition ; Root ; Triticum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cation Al3+ is toxic to plants at micromolar concentrations and can severely inhibit root growth in solution experiments. Trivalent aluminum hydrolyzes in solution, and, apart from the Al3+ ion, which dominates speciation below pH 5.0, various mononuclear and polynuclear hydroxy-Al species can also occur (Kinraide 1991). Accumulating evidence suggests that Al3+ is the rhizotoxic species under the experimental conditions used in the present study (Kinraide 1991; Kinraide et al. 1992). The inhibition of Ca2+ uptake in roots by Al3+ has been proposed as a possible mechanism for Al3+ toxicity, and in this study the hypothesis was tested directly. Root growth and Ca2+ uptake were measured in 5-d-old seedlings of wheat (Triticum aestivum L. Thell) during exposure to Al3+ in a low-Ca2+ basal medium, and to Al3+ in the presence of added cations. Uptake of Ca2+ in whole roots and translocation to the shoot were measured using 45Ca2+, and localized measurements of net Ca2+ flux were also made at the root apex using the technique of microelectrode ion-flux estimation. Treatment with 2.64 μM AlCl3 in 226 μM CaCl2, at pH 4.5, severely inhibited root growth without affecting Ca2+ uptake. Addition of 30 mM Na2+, 3 mM Mg2+ or 50 μM tris(ethylenediamine)cobalt(III) to this Al3+ treatment restored root growth but significantly reduced Ca2+ uptake measured over the entire root system and at the root apex. The Al3+ and Ca2+ concentrations were adjusted so that the activities of the Al3+ and Ca2+ ions were constant in all solutions (1.5 μM and 200 μM, respectively). Root growth can be severely inhibited by Al3+ concentrations that do not affect Ca2+ uptake, while the addition of ameliorating cations depresses Ca2+ uptake. These results argue against the hypothesis that Al3+ inhibits root growth by reducing Ca2+ uptake.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00198698
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  • 4
    Electronic Resource
    Electronic Resource
    Root elongation in saline solution related to calcium binding to root cell plasma membranes (1997)
    Springer
    Plant and soil 191 (1997), S. 67-76 
    Details
    ISSN: 1573-5036
    Keywords: calcium ; plasma membrane ; root elongation ; salinity ; sodium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract To gain a better understanding of the relations between root elongation and the amount of Ca2+ bound to the plasma membrane (PM), melon plants were grown in aerated solutions containing different concentrations of CaCl2 with various concentrations of NaCl or mannitol. With increasing external concentrations of NaCl or mannitol, root elongation was suppressed. Addition of CaCl2 to the external medium alleviated the inhibition of root elongation by high concentrations of Na+, but not of mannitol. Root elongation in media containing high concentrations of NaCl was correlated with the computed amount of Ca2+ bound to the PM. A model describing relative root elongation (RRL) under salt stress was developed. This model takes into account the osmotic potential in the growing solution (based on the mannitol experiments) and the computed amount of Ca2+ bound to the PM. Calcium binding was calculated by applying a Gouy-Chapman-Stern sorption model using the same parameters deduced from studies on PM vesicles. This model combines electrostatic theory with competitive binding at the PM surface. The model for RRL allowed the computation of a critical value for the fraction of negative sites binding Ca2+ on the PM needed for nearly optimal (95%) root elongation. Any decrease below this critical value decreased the RRL. Root elongation of Honey Dew (salt-resistant cv.) was greater than that of Eshkolit Ha'Amaqim (salt-sensitive cv.) under NaCl stress. Nearly optimal root growth for Honey Dew and Eshkolit Ha'Amaqim occurred when 40% and 51% of total membrane charged sites were bound by Ca2+, respectively. The effect of osmotic potential on the suppression of root elongation was the same for the two cultivars. To our knowledge, this report provides the first fully quantitative estimates of PM-bound Ca2+ relative to salt toxicity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1004241506347
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  • 5
    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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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    Phosphorylation of Tau Alters Its Association with the Plasma Membrane (2000)
    Springer
    Cellular and molecular neurobiology 20 (2000), S. 497-508 
    Details
    ISSN: 1573-6830
    Keywords: tau ; phosphorylation ; signal transduction ; protein kinase C ; Alzheimer's disease
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract 1. The potential functions of the microtubule-associated protein tau have been expanded by the recent demonstration of its interaction with the plasma membrane. Since the association of tau with microtubules is regulated by phosphorylation, herein we examine whether or not the association of tau with the plasma membrane is also regulated by phosphorylation. 2. A range of tau isoforms migrating from 46 to 64 kDa was associated with crude particulate fractions derived from SH-SY-5Y human neuroblastoma cells, and were retained during the initial stages of plasma membrane purification. During the extensive washing utilized in purification of the plasma membrane, portions of each of these isoforms were depleted from the resultant purified membrane. Immunoblot analysis with phospho-dependent and -independent antibodies revealed selective depletion of phospho isoforms during membrane washing. This effect was more pronounced for the slowest-migrating (64-kDa) tau isoform. 3. This putative influence of phosphorylation on the association of tau with the plasma membrane was further probed by transfection of SH-SY-5Y human neuroblastoma cells with a tau construct that could associate with the plasma membrane but not with microtubules. Treatment with phorbol ester or calcium ionophore, both of which increased phospho-tau levels within the cytosol and plasma membrane, was accompanied by the dissociation of this tau construct from the membrane. 4. These data indicate that phosphorylation regulates the association with the plasma membrane. Dissociation from the membrane by phosphorylation may place tau at risk for hyperphosphorylation and ultimate PHF formation in a manner previously considered for tau dissociated from microtubules.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1007075115574
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