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  • Chemistry  (2)
  • Veratrum alkaloid  (2)
  • bradykinin B2 receptor  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Biosynthesis of rubijervine in Veratrum grandiflorum
    Amsterdam : Elsevier
    Phytochemistry 14 (1975), S. 1295-1301 
    Details
    ISSN: 0031-9422
    Keywords: 22,26-epiminocholestane alkaloid ; Liliaceae ; Veratrum alkaloid ; Veratrum grandiflorum ; biosynthesis ; hakurirodine ; rubijervine
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/S0031-9422(00)98615-1
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Biosynthesis of rubijervine in Veratrum grandiflorum
    Amsterdam : Elsevier
    Phytochemistry 14 (1975), S. 1295-1301 
    Details
    ISSN: 0031-9422
    Keywords: 22,26-epiminocholestane alkaloid ; Liliaceae ; Veratrum alkaloid ; Veratrum grandiflorum ; biosynthesis ; hakurirodine ; rubijervine.
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/S0031-9422(00)98615-1
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Bradykinin enhances GLUT4 translocation through the increase of insulin receptor tyrosine kinase in primary adipocytes: evidence that bradykinin stimulates the insulin signalling pathway (1996)
    Springer
    Diabetologia 39 (1996), S. 412-420 
    Details
    ISSN: 1432-0428
    Keywords: Keywords Bradykinin ; bradykinin B2 receptor ; glucose uptake ; tyrosine kinase ; insulin receptor ; insulin receptor substrate-1 ; adipocyte ; GLUT4.
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary It has been suggested that bradykinin stimulates glucose uptake in experiments in vivo and in cultured cells. However, its mechanism has not yet been fully elucidated. In this study, the effects of bradykinin on the insulin signalling pathway were evaluated in isolated dog adipocytes. The bradykinin receptor binding study revealed that dog adipocytes possessed significant numbers of bradykinin receptors (Kd = 83 pmol/l, binding sites = 1.7 × 104 site/cell). Reverse transcription-polymerase chain reaction amplification showed the mRNA specific for bradykinin B2 receptor in the adipocytes. Bradykinin alone did not increase 2-deoxyglucose uptake in adipocytes; however, in the presence of insulin (10–7 mol/l) it significantly increased 2-deoxyglucose uptake in a dose-dependent manner. Bradykinin also enhanced insulin stimulated GLUT4 translocation from the intracellular fraction to the cell membrane, and insulin induced phosphorylation of the insulin receptor β subunit and insulin receptor substrate-1 (IRS-1) without affecting the binding affinities or numbers of cell surface insulin receptors in dog adipocytes. The time-course of insulin stimulated phosphorylation of the insulin receptor β subunit revealed that phosphorylation reached significantly higher levels at 10 min, and stayed at the higher levels until 120 min in the presence of bradykinin, suggesting that bradykinin delayed the dephosphorylation of the insulin receptor. It is concluded that bradykinin could potentiate insulin induced glucose uptake through GLUT4 translocation. This effect could be explained by the potency of bradykinin to upregulate the insulin receptor tyrosine kinase activity which stimulates phosphorylation of IRS-1, followed by GLUT4 translocation. [Diabetologia (1996) 39: 412–420]
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00400672
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Bradykinin enhances GLUT4 translocation through the increase of insulin receptor tyrosine kinase in primary adipocytes: evidence that bradykinin stimulates the insulin signalling pathway (1996)
    Springer
    Diabetologia 39 (1996), S. 412-420 
    Details
    ISSN: 1432-0428
    Keywords: Bradykinin ; bradykinin B2 receptor ; glucose uptake ; tyrosine kinase ; insulin receptor ; insulin receptor substrate-1 ; adipocyte ; GLUT4
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary It has been suggested that bradykinin stimulates glucose uptake in experiments in vivo and in cultured cells. However, its mechanism has not yet been fully elucidated. In this study, the effects of bradykinin on the insulin signalling pathway were evaluated in isolated dog adipocytes. The bradykinin receptor binding study revealed that dog adipocytes possessed significant numbers of bradykinin receptors (Kd=83 pmol/l, binding sites = 1.7×104 site/cell). Reverse transcription-polymerase chain reaction amplification showed the mRNA specific for bradykinin B2 receptor in the adipocytes. Bradykinin alone did not increase 2-deoxyglucose uptake in adipocytes; however, in the presence of insulin (10−7 mol/l) it significantly increased 2-deoxyglucose uptake in a dose-dependent manner. Bradykinin also enhanced insulin stimulated GLUT4 translocation from the intracellular fraction to the cell membrane, and insulin induced phosphorylation of the insulin receptor Β subunit and insulin receptor substrate-1 (IRS-1) without affecting the binding affinities or numbers of cell surface insulin receptors in dog adipocytes. The time-course of insulin stimulated phosphorylation of the insulin receptor Β subunit revealed that phosphorylation reached significantly higher levels at 10 min, and stayed at the higher levels until 120 min in the presence of bradykinin, suggesting that bradykinin delayed the dephosphorylation of the insulin receptor. It is concluded that bradykinin could potentiate insulin induced glucose uptake through GLUT4 translocation. This effect could be explained by the potency of bradykinin to upregulate the insulin receptor tyrosine kinase activity which stimulates phosphorylation of IRS-1, followed by GLUT4 translocation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00400672
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Characterisation of TiN films prepared by electron shower, arc ion-plating and sputtering methods (1995)
    New York, NY [u.a.] : Wiley-Blackwell
    Advanced Materials for Optics and Electronics 5 (1995), S. 191-198 
    Details
    ISSN: 1057-9257
    Keywords: TiN ; adhesion ; PVD ; electron shower ; arc ion plating ; sputtering ; wear ; surface ; morphology ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Electrical Engineering, Measurement and Control Technology , Physics
    Notes: It has been found that TiN films with high wear resistance and high adhesion can be prepared by electron shower deposition and arc ion plating on glass and austenitic stainless steel (SUS 316) substrates. The high wear resistance is principally explained by the grain size and surface morphology. Fine {100}-faceted crystals (10-150 nm) grew on the surface. The typical morphology of the crystals was triangular pyramidal. The crystallite size was changed by the bias voltage. Faceted crystals produced by arc ion plating were rounded and smoothed by a change in bias, but were unaltered in samples prepared by the electron shower process. The fine faceted surfaces had higher wear resistance than the granularly rounded ones. When TiO2 was formed at the interface of the glass substrate, the adhesion was lowered. The high-adhesion film prepared by electron shower deposition contained a small amount of TiO2 at the interface.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/amo.860050403
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    The effect of copper(II) on the Crystallization of α-FeOOH (1972)
    Weinheim : Wiley-Blackwell
    Zeitschrift für anorganische Chemie 391 (1972), S. 86-96 
    Details
    ISSN: 0044-2313
    Keywords: Chemistry ; Inorganic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Der Einfluß von Kupfer(II) auf die Kristallisation von α-FeOOHα-FeOOH wurde in mehreren Proben ohne und mit Zusatz von Cu(II)-Ionen (bis zu 5 Atom-%) unter bestimmten Bedingungen dargestellt und röntgeno-graphisch, durch BET, DTA und elektronenmikroskopisch untersucht. Durch Zusatz von 2,5 Atom-% wird die Kristallisation des α-FeOOH vollständig verhindert. Geringe Cu-Zusätze verzögern die Kristallisation. Das Wachsen der Partikel- und Kristallitgrößen von reinem und Cu-dotiertem α-FeOOH unterscheidet sich. Nach der Theorie des Autors wird der Einfluß der Cu2+-Ionen auf die Verzerrung des Koordinationsgitters diskutiert. Es besteht vermutlich ein Zusammenhang zür korrosionshemmenden Wirkung von Kupferzusätzen im Stahl.
    Notes: Various α-FeOOH samples have been prepared with or without addition of Cu(II) (0-5% Cu/Fe) and examined by X-ray diffraction, BET surface area determination, electron-microscopical observation and DTA. Doping with Cu in suitable amounts impedes completely the formation of α-FeOOH. The mechanism of growth, based on the changes of particle size and crystallite dimension, appears to be different between pure and Cu-doped α-FeOOH. The reason of the remarkable effect of Cu on the crystallization process of α-FeOOH is discussed. The effect of Cu is likely relevant to the role of Cu added to anticorrosive steel used in atmospheric environment.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/zaac.19723910111
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    Paper (German National Licenses)
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