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  • Articles  (6)
  • Chemistry and Pharmacology  (6)
  • 1
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Information in neurons flows from synapses, through the dendrites and cell body (soma), and, finally, along the axon as spikes of electrical activity that will ultimately release neurotransmitters from the nerve terminals. However, the dendrites of many neurons also have a secretory role, ...
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  • 2
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 325 (1987), S. 813-816 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Figure 1 illustrates the time course of vasopressin (AVP) and oxytocin (OT) release from isolated nerve terminals in the presence or absence of 10~7 M relaxin. An increase in hormone secretion was induced by depolarizing the isolated nerve terminals (neurosecretosomes) with 100 mM K+ for 10 min. ...
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  • 3
    ISSN: 1573-4935
    Keywords: Neurosecretion ; Vasopressin ; Guanine nucleotides ; G-proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In SLO-permeabilized isolated nerve endings from the rat neurohypophysis, GTP, guanosine 5′[y-thio]triphosphate (GTPyS) and guanosine 5′(ßy-imido]triphosphate (GMPPNP) inhibit the Ca2+-evoked vasopressin release. Pretreatment with pertussis toxin enhances the inhibitory effects of both GTP-analogues. Omission of Mg2+ overcomes the effect of GMPPNP and reverses the inhibitory effect of GTP and GTPyS. In the absence of Mg2+, GTP and GTPyS now potentiate Ca2+-evoked secretion.
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  • 4
    ISSN: 1573-4935
    Keywords: neurosecretion ; nerve endings ; stimulus-secretion coupling ; secretion ; exocytosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In the present paper we discuss the properties of a recently developed preparation of isolated neurosecretory nerve endings obtained from the rate neurohypophysis. These nerve terminals release two neurohormones, oxytocin and vasopressin, which are easily assayed by radioimmunoassay. Depolarization-induced secretion is dependent on the same parameters as those regulating release from the whole neural lobe. The isolated nerve endings can be permeabilized by means of digitonin; a treatment which gives direct access to the cytoplasm allowing the study of the minimal requirements for inducing neuropeptide release. Furthermore, some nerve endings are large enough to allow the use of the patch-clamp technique. In the present paper we present evidences which show that the isolated neurohypophysial nerve terminals represent a protent tool for studying the mechanism of stimulus-secretion.
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Bioscience reports 8 (1988), S. 471-483 
    ISSN: 1573-4935
    Keywords: exocytosis ; secretion ; neuropeptides ; vasopressin ; neurohypophysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Neurohypophysial hormones are packed in secretory granules which are stored in nerve endings and in dilatations called nerve swellings. Although it was originally believed that the nerve swellings were storage compartments and that release occurred solely from the nerve terminals, the present paper demonstrates that secretion can occur to the same extent from both nerve endings and nerve swellings.
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  • 6
    ISSN: 1573-9023
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Summary Intracellular Ca2+ concentrations ([Ca2+]i) were measured in single-cultured human epithelial intestinal HT-29-D4 cells by digital microscopy using the Ca2+-sensitive fluorescent dye Fura-2. Exposure of these cells to HIV-1 surface-envelope glycoprotein gp120, or to a soluble form of its precursor (gp160), resulted in a significant, dose-dependent rise in [Ca2+]i. gp120 or gp160 specifically abrogated the [Ca2+]i response to the neuropeptide agonist neurotensin, which is a stimulator of chloride secretion via inositol trisphosphate-mediated Ca2+ mobilization. By contrast, upon exposure to neurotensin gp120 failed to show any increase in [Ca2+]i within the same cells, suggesting that both neurotensin and gp120 stimulate a common pathway of [Ca2+]i mobilization. gp120-/gp160-induced [Ca2+]i responses were abolished by preincubation with neutralizing antibodies directed against the third variable domain of gp120. These antibodies inhibited the binding of gp120/gp160 to galactosylceramide (GalCer), the alternative HIV-1 receptor in HT-29-D4 cells. Furthermore, HT-29-D4 cells displayed an important increase in [Ca2+]i to anti-GalCer mAb alone, which rendered the cells insensitive to gp120. By contrast, HT-29-D4 cells became insensitive to anti-GalCer mAb after exposure to gp120. These data indicate that HIV-1 may directly alter enterocytic functions through interaction with the GalCer receptor.
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