References of "czarna, M"
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See detailMitochondrial function plasticity in Acanthamoeba castellanii during growth in batch culture.
Czarna, M.; Sluse, Francis ULg; jarmuszkiewicz, W.

in Journal of Bioenergetics & Biomembranes (2007), 39

The alterations in mitochondrial bioenergetics during growth in a batch culture of Acanthamoeba castellanii were studied. The capacity of cytochrome pathway-dependent respiration measured in vitro ... [more ▼]

The alterations in mitochondrial bioenergetics during growth in a batch culture of Acanthamoeba castellanii were studied. The capacity of cytochrome pathway-dependent respiration measured in vitro decreased from the intermediary phase, when cell division slowed down. The pattern of the cytochrome pathway capacity changes was paralleled from the intermediary phase by alterations in the amount of total (and reducible) membranous ubiquinone. These changes were accompanied by a decrease in mitochondrial reactive oxygen species production in vitro (when no energy-dissipating system was active), and almost no change in superoxide dismutase activity and protein level, thus indicating an equivalent need for this enzyme in oxidative stress defence in A. castellanii culture. On the other hand, a decrease in the activity and protein level of alternative oxidase and uncoupling protein was observed in vitro, when cells shifted from the exponential growth phase to the stationary phase. It turned out that the contribution of both energy-dissipating systems in the prevention of mitochondrial reactive oxygen species generation in vivo could lead to its constant level throughout the growth cycle of A. castellanii batch culture. Hence, the observed functional plasticity insures survival of high quality cysts of A. castellanii cells. [less ▲]

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See detailFatty acid efficiency profile in uncoupling of Acanthamoeba castellanii mitochondria.
Swida, A.; czarna, M.; Woyda-Polszczyca, A. et al

in Journal of Bioenergetics & Biomembranes (2006), 39

A profile of free fatty acid (FFA) specificity in Acanthamoeba castellanii mitochondrial uncoupling is described. The FFA uncoupling specificity was observed as different abilities to stimulate resting ... [more ▼]

A profile of free fatty acid (FFA) specificity in Acanthamoeba castellanii mitochondrial uncoupling is described. The FFA uncoupling specificity was observed as different abilities to stimulate resting respiration, to decrease resting membrane potential, and to decrease oxidative phosphorylation efficiency. Tested unsaturated FFA (C18-20) were more effective as uncouplers and protonophores when compared to tested saturated FFA (C8-18), with palmitic acid (C16:0) as the most active. As FFA efficiency in mitochondrial uncoupling is related to physiological changes of fatty acid composition (and thereby FFA availability) during growth of amoeba cells, it could be a way to regulate the activity of an uncoupling protein and thereby the efficiency of oxidative phosphorylation during a cell life of this unicellular organism. [less ▲]

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See detailSubstrate kinetics of the Acanthamoeba castellanii alternative oxidase and the effects of GMP.
Jarmuszkiewicz, W.; Czarna, M.; Sluse, Francis ULg

in Biochimica et Biophysica Acta-Bioenergetics (2005), 1708

In Acanthamoeba castellanii mitochondria, the apparent affinity values of alternative oxidase for oxygen were much lower than those for cytochrome c oxidase. For unstimulated alternative oxidase, the K ... [more ▼]

In Acanthamoeba castellanii mitochondria, the apparent affinity values of alternative oxidase for oxygen were much lower than those for cytochrome c oxidase. For unstimulated alternative oxidase, the K(Mox) values were around 4-5 microM both in mitochondria oxidizing 1 mM external NADH or 10 mM succinate. For alternative oxidase fully stimulated by 1 mM GMP, the KK(Mox) values were markedly different when compared to those in the absence of GMP and they varied when different respiratory substrates were oxidized (K(Mox) was around 1.2 microM for succinate and around 11 microM for NADH). Thus, with succinate as a reducing substrate, the activation of alternative oxidase (with GMP) resulted in the oxidation of the ubiquinone pool, and a corresponding decrease in K(Mox). However, when external NADH was oxidized, the ubiquinone pool was further reduced (albeit slightly) with alternative oxidase activation, and the K(Mox) increased dramatically. Thus, the apparent affinity of alternative oxidase for oxygen decreased when the ubiquinone reduction level increased either by changing the activator or the respiratory substrate availability. [less ▲]

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See detailIn phosphorylating Acanthamoeba castellanii mitochondria the sensitivity of uncoupling protein activity to GTP depends on the redox state of quinone.
Jarmuszkiewicz, W.; Swida, A.; czarna, M. et al

in Journal of Bioenergetics & Biomembranes (2005), 37

In isolated Acanthamoeba castellanii mitochondria respiring in state 3 with external NADH or succinate, the linoleic acid-induced purine nucleotide-sensitive uncoupling protein activity is able to ... [more ▼]

In isolated Acanthamoeba castellanii mitochondria respiring in state 3 with external NADH or succinate, the linoleic acid-induced purine nucleotide-sensitive uncoupling protein activity is able to uncouple oxidative phosphorylation. The linoleic acid-induced uncoupling can be inhibited by a purine nucleotide (GTP) when quinone (Q) is sufficiently oxidized, indicating that in A. castellanii mitochondria respiring in state 3, the sensitivity of uncoupling protein activity to GTP depends on the redox state of the membranous Q. Namely, the inhibition of the linoleic acid-induced uncoupling by GTP is not observed in uninhibited state 3 respiration as well as in state 3 respiration progressively inhibited by complex III inhibitors, i.e., when the rate of quinol (QH(2))-oxidizing pathway is decreased. On the contrary, the progressive decrease of state 3 respiration by declining respiratory substrate availability (by succinate uptake limitation or by decreasing external NADH concentration), i.e., when the rate of Q-reducing pathways is decreased, progressively leads to a full inhibitory effect of GTP. Moreover, in A. castellanii mitochondria isolated from cold-treated cells, where a higher uncoupling protein activity is observed, the inhibition of the linoleic acid-induced proton leak by GTP is revealed for the same low values of the Q reduction level. [less ▲]

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See detailThe effect of growth at low temperature on the activity and expression of the uncoupling protein in Acanthamoeba castellanii mitochondria.
Jarmuszkiewicz, W.; Antos, N.; swida, A. et al

in FEBS Letters (2004), 569

Mitochondria of amoeba Acanthamoeba castellanii, a non-photosynthetic soil amoeboid protozoon, possess an uncoupling protein (AcUCP) that mediates free fatty acid-activated proton re-uptake dissipating ... [more ▼]

Mitochondria of amoeba Acanthamoeba castellanii, a non-photosynthetic soil amoeboid protozoon, possess an uncoupling protein (AcUCP) that mediates free fatty acid-activated proton re-uptake dissipating the proton electrochemical gradient built up by respiration. The present study provides the first evidence that UCP could be a cold response protein in unicellulars. In mitochondria isolated from an amoeba batch culture grown temporarily at low temperature (6 degrees C), the content of AcUCP was increased and correlated with an increase in the linoleic acid (LA)-stimulated UCP-mediated carboxyatractyloside-resistant state 4 respiration, as compared to a control culture (routinely grown at 28 degrees C). Moreover, the cytochrome pathway activity was found to be insensitive to the cold exposure of amoeba cells, as indicated by respiration and membrane potential measurements as well as by an absence of change in the adenine nucleotide translocator and cytochrome oxidase expression levels. Furthermore, in mitochondria from the low-temperature-grown cells, at fixed LA concentration, the increased contribution of AcUCP activity to total mitochondrial phosphorylating respiration accompanied by lower coupling parameters was found, as was confirmed by calculation of this contribution using ADP/O measurements. [less ▲]

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See detailThe contribution of uncoupling protein and ATP synthase to state 3 respiration in Acanthamoeba castellanii mitochondria.
Jarmuszkiewicz, W.; Czarna, M.; Sluse-Goffart, C. et al

in Acta Biochimica Polonica. Polish. (2004), 51

Mitochondria of the amoeba Acanthamoeba castellanii possess a free fatty acid-activated uncoupling protein (AcUCP) that mediates proton re-uptake driven by the mitochondrial proton electrochemical ... [more ▼]

Mitochondria of the amoeba Acanthamoeba castellanii possess a free fatty acid-activated uncoupling protein (AcUCP) that mediates proton re-uptake driven by the mitochondrial proton electrochemical gradient. We show that AcUCP activity diverts energy from ATP synthesis during state 3 mitochondrial respiration in a fatty acid-dependent way. The efficiency of AcUCP in mitochondrial uncoupling increases when the state 3 respiratory rate decreases as the AcUCP contribution is constant at a given linoleic acid concentration while the ATP synthase contribution decreases with respiratory rate. Respiration sustained by this energy-dissipating process remains constant at a given linoleic acid concentration until more than 60% inhibition of state 3 respiration by n-butyl malonate is achieved. The present study supports the validity of the ADP/O method to determine the actual contributions of AcUCP (activated with various linoleic acid concentrations) and ATP synthase in state 3 respiration of A.castellanii mitochondria fully depleted of free fatty acid-activated and describes how the two contributions vary when the rate of succinate dehydrogenase is decreased by succinate uptake limitation [less ▲]

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