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  • Ehrlich ascites tumor cells  (2)
  • Septic shock  (2)
  • kinetics  (2)
  • 1
    ISSN: 1432-1238
    Keywords: Septic shock ; Cyclic GMP ; Guanylyl cyclase ; Human ; Atrial natriuretic peptide ; Vascular resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Objective To investigate the increase in plasma cyclic GMP (cGMP) concentrations in humans with hyperkinetic septic shock (SS) and to evaluate its relationship to low systemic vascular resistance (SVR). Design Prospective clinical investigation. Setting Medical intensive care unit of a university hospital. Patients 22 patients with documented SS requiring hemodynamic resuscitation, respiratory support and —in some cases — hemodialysis. Measurements and results Hemodynamic data were recorded at admission time and then twice a-day during the following 72 h. We simultaneously measured cyclic GMP, atrial natriuretic peptides (ANP), creatininemia and platelet counts. At admission time, higher plasma cGMP concentrations were observed in patients with SS (11.84±1.52 pmol·ml−1) than in healthy controls (1.77±0.18 pmol·ml−1,p〈0.0001), in septicemia patients without circulatory failure (3.28±0.36 pmol·ml−1,p〈0.005) or in patients with hyperkinetic non-septic shock (3.6±0.7 pmol·ml−1,p〈0.02). In contrast, there was no significant difference between patients with SS and controls with anuria from non-septic origin. Also ANP concentrations were higher in patients with SS than in others. In addition, cGMP levels correlated negatively with SVR during the first 48 h of the study, and positively with creatininemia later when renal function worsened. However, they did not correlate significantly with ANP. Conclusion These data demonstrate that a significant increase in plasma cGMP concentrations occurs during human SS and that it correlates with the decline in peripheral vascular resistance in the absence, but not in the presence, of severe renal failure. Furthermore, the increase in cGMP levels cannot be ascribed solely to enhanced ANP-induced particulate guanylyl cyclase activity. Thus, our results suggest the occurrence of another endogenous source of cGMP during hyperkinetic SS.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of cancer research and clinical oncology 113 (1987), S. 298-300 
    ISSN: 1432-1335
    Keywords: Ehrlich ascites tumor cells ; DNA over-replication ; Anaerobiosis ; G2M phase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary G2-enriched fractions of Ehrlich ascites tumor cells (up to 80%–85% G2 cells) separated from anaerobically and aerobically cultured asynchronous populations by centrifugal elutriation revealed the same growth characteristics after recultivation under standard conditions: a significant proportion of cells with increased DNA (DNA content〉4C) emerged. Interruption of DNA synthesis by deprivation of oxygen may account for polyploidisation (over-replication) of DNA but other mechanisms must be taken into consideration.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Intensive care medicine 18 (1992), S. 309-311 
    ISSN: 1432-1238
    Keywords: Methylene blue ; Septic shock ; Human ; Multiorgan failure ; Nitric oxide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We report the hemodynamic improvements induced by intravenous methylene blue (MB), a guanylate cyclase inhibitor, in 2 patients with hyperdynamic septic shock treated with norepinephrine (NE) infusion, mechanical ventilation an hemodialysis. MB injection augmented the low vascular resistance, mean arterial pressure and induced a slight decrease of cardiac index, without any change of heart rate and pulmonary artery wedge pressure. Plasma cyclic GMP levels decreased without a significant change of atrial natriuretic factor levels. MB (2 mg·kg−1) induced a longer lasting improvement of circulatory failure without deleterious side effects, but did not prevent the occurrence of delayed multiorgan failure or subsequent death. These data suggest that in patients, severe sepsis-induced loss of vascular responsiveness to NE involves activation of soluble guanylate cyclase, possibly stimulated by enhanced nitric oxide production. Furthermore, these observations support the concept that pharmacological blockade of guanylate cyclase may improve hemodynamics but not survival rates.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-1335
    Keywords: Ehrlich ascites tumor cells ; Methylglyoxal ; Glucosone ; Galactosone ; Growth inhibition ; DNA synthesis ; Protein Synthesis ; Energy Metabolism
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. Proliferation of in vitro grown Ehrlich ascites tumor cells is completely inhibited by 0.2–0.4 mM methylglyoxal and 1–2mM glucosone or galactosone without severely affecting viability (dye exclusion test); no phase-specific arrest of cell growth is observed. 2. Incorporation of [14C] thymidine into the acid-insoluble fraction of the cells decreases within a few minutes to less than 50% of that in controls in the presence of 0.4 mM methylglyoxal, and 2 mM glucosone or galactosone causes a comparable inhibition of DNA synthesis after 2 h or 4 h, respectively. 3. The action of 0.4 mM methylglyoxal inhibits incorporation of [14C] leucine within a few minutes by more than 70%, while 2 mM glucosone and galactosone are significantly less effective (50%–60% inhibition after 12 h). 4. While methylglyoxal and galactosone do not severely affect lactate production of the cells, 2 mM glucosone reduces glycolysis by 60%–70%; ATP/ADP ratios did not fall below 3.5 in the presence of the inhibitors (controls 4–6). 5. It is suggested that the reaction potentialities of the oxaldehyde function of the inhibitors play an important role in their growth-inhibitory acitivity, besides exerting a specific effect on hexokinase (glucosone) and UTP-trapping activity.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Journal of fluorescence 6 (1996), S. 165-168 
    ISSN: 1573-4994
    Keywords: Cation binding ; fluorescence decay ; kinetics ; binding constants ; Na,K-ATPase ; eosin Y
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Time-resolved fluorescence and binding studies have been carried out on Na,K-ATPase in the presence of the fluorescent dye eosin Y to obtain thermodynamic and kinetic parameters for the interaction of the enzyme with different cations. Eosin Y binding is indicated by a 3 ns fluorescence decay process and is observed only in the presence of mono- and divalent cations. This type of cation binding is interpreted as a nonselective electrostatic interaction, with negatively charged groups of the enzyme providing a high-affinity eosin Y binding site. Eosin Y binding is observed only under conditions where the enzyme exists in the conformational state F1. The kinetic parameters of eosin Y binding have been determined employing stopped-flow fluorometry.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-4994
    Keywords: Na,K-ATPase ; fluorescent inhibitor ; kinetics ; energy transfer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The interaction between the fluorescent ouabain derivative DEDO and purified renal Na,K-ATPase (isolated from different animal species) is investigated. Equilibrium binding studies provide a pK value of about 7.5 and a stoichoimetric coefficient of 1. Nonmodified ouabain exhibits the same affinity to the rabbit enzyme; the enzyme originating from the other sources binds DEDO 10 times less strongly than ouabain. Kinetic studies indicate that this is the consequence of a 10 times higher dissociation rate constant of the complexes formed with DEDO. The fluorescence emission intensity of DEDO is enhanced, being dependent on the enzyme source. The single decay time of DEDO is 3 ns in the absence and 21 ns in the presence of the rabbit enzyme and 14 ns in the presence of the pig renal enzyme. This result suggests that the fluorophore of DEDO is bound to a very hydrophobic environment of the enzyme. Further characterization of the static fluorescence spectra provides evidence for energy transfer between Trp residues of the enzyme and DEDO. Distance estimations suggest that one or two Trp residues are likely to be located in the proximity of the fluorophore.
    Type of Medium: Electronic Resource
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