Poster
# 19
Poster |
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6th Internet World Congress for Biomedical Sciences |
María Dolores Mayas-Torres(1), José Manuel Martínez-Martos(2), María Jesús Ramírez-Expósito(3), María Jesús García-López(4), Isabel Prieto-Gómez(5), Garbiñe Arechaga-Maza(6), Manuel Ramírez-Sánchez(7)
(1)(2)(4)(5)(6)(7)Unit of Physiology. University of Jaén - Jaén. Spain
(3)Unit of Physiology. University of Jaen - Jaén. Spain
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[Neuroscience] |
[Physiology] |
Effects of ethanol on the bioenergetic behavior of synaptosomes.
The effects of ethanol on mitochondrial activity of mouse frontal cortex synaptosomes show the following results: Ethanol induces a dose-dependent increase of mitochondrial activity. In this way, ethanol 25 mM increases the activity in a 39.14% (p<0.01). Ethanol 50 mM produces a significant increase (p<0.01) in a 53.61% and ethanol 100 mM in a 58.92% (p<0.01) (Figure 1A).
Depolarization with K+ 25 mM induces an increase of mitochondrial activity in a 22.51% (p<0.01). The simultaneous incubation of synaptosomes with K+ 25 mM and ethanol 25 mM or 50 mM increases significantly (p<0.01) the activity in a 36.52% and 46.43% respectively. Otherwise, ethanol 100 mM do not modify mitochondrial activity, when compared with the control values (Figure 1B).
Parameters of oxidative stress.
The analysis of the ethanol effects on the free radical generation shows the following results: Ethanol 25 mM do not produce modifications in luminol chemiluminiscence when compared with control values. Ethanol 50 mM increases luminol chemiluminiscence in a 19.37% (p<0.05), while ethanol 100 mM induces a significant increase (p<0.05) of luminol chemiluminiscence in a 19.04% (Figure 2A).
Depolarization with K+ 25 mM does not modify luminol chemiluminiscence. In addition, the simultaneous incubation of synaptosomes with K+ 25 mM and ethanol does not change luminol chemiluminiscence either (Figure 2B).
Using lucigenin as the enhancer of the chemiluminiscence signal, the results obtained are: Ethanol 25 mM induces a light increase of 18.05% (p<0.05), while ethanol 50 mM and 100 mM do not modify lucigenin chemiluminiscence, when compared with the control values (Figure 3A). Depolarization with K+ 25 mM increases significantly (p<0.05) in a 16.94% lucigenin chemiluminiscence vs. the control values. However, the simultaneous incubation of synaptosomes with ethanol under depolarized conditions with K+ 25 mM 4), does not produce significant differences when compared with control values (Figure 3B).
The effects of ethanol on lipid peroxidation (TBARS content) of mouse frontal cortex synaptosomes showed the following results: Ethanol 25 mM decreased TBARS content in a 13.55% (p<0.01). Otherwise, ethanol 50 mM and 100 mM of ethanol did not modify significantly control values (Figure 4A). Depolarization of synaptosomes with K+ 25 mM or the simultaneous incubation of synaptosomes with K+ 25 mM and ethanol at the different concentrations did not change TBARS content when compared with the control values (Figure 4B).
Neither ethanol at the different concentrations used nor depolarization of synaptosomes with K+ 25 mM nor the simultaneous incubation of synaptosomes with K+ 25 mM and ethanol at different concentrations (25, 50, y 100 mM) did modify carbonyl content of synaptosomal proteins (Figures 5A and 5B).
Effects of ethanol on AlaAP.
The analysis of the effects of ethanol on basal AlaAP activity shows the following results: AlaAP activity is inhibited in a dose-dependent manner by ethanol (figure 6A). Thus, a ethanol 25 mM induces a significant inhibition (p<0.01) of 13.16% in relation to the control. Ethanol 50 mM decreases this activity in a 19 % (p<0.01), and ethanol 100 mM produces an inhibición of 49.29% (p<0.01).
The stimulation of synaptosomes with K+ 25 mM decreases significantly (p<0.01) AlaAP activity in a 23.5% (figure 6B). The simultaneous incubation of synaptosomes with K+ 25 mM and ethanol decreases AlaAP activity (figure 6B). Thus, ethanol 25mM induces a significant inhibition of 58.95% in presence of K+ 25 mM, while ethanol 50 mM and 100 mM induce an inhibition of 22.74% and 40.33% (p<0.01) respectively, when compared with depolarized values of AlaAP activity (figure 6B).
Effects of ethanol of ArgAP.
The analysis of the effects of ethanol on basal ArgAP activity shows the following results: Ethanol produces an inhibition of this enzymatic activity, with exception of ethanol 50 mM that increases ArgAP activity significantly (p<0.01) in a 67.2%. Thus, ethanol 25 mM decreases ArgAP in a 16.19% (p<0.01) while ethanol 100 mM leads to an inhibition of 39.82% (p<0.01) (figure 7A).
Depolarization of synaptosomes with K+ 25 mM does not modify the enzymatic activity (figure 7B). The simultaneous incubation of synaptosomes with K+ 25 mM and ethanol produces a decrease of ArgAP activity except for ethanol 25 mM. The presence of K+ 25 mM and ethanol 50 mM decreases the enzymatic activity in a 26.75% (p<0.01) and the stimulation of synaptosomes with K+ 25 mM in presence of ethanol 100 mM produces a significant decrease (p<0.01) in ArgAP activity of 39.13% in relation to the depolarized values (figure 7B).
Effects of ethanol on CysAP.
Ethanol induces the inhibition of CysAP in a dose-dependent manner (figure 8A). Thus, ethanol 25 mM induces a significant (p<0.01) inhibition of CysAP activity in a 43.98% in relation to the control values. The inhibition produced by ethanol 50 mM is about 10.15% (p<0.01), and the inhibition due to ethanol 100 mM is 44.3% (p<0.01) (Figure 8A).
Stimulation of synaptosomes with K+ 25 mM does not modify CysAP activity (figure 8B). In the same way, this activity was not modified by the simultaneous incubation of synaptosmes with K+ 25 mM and ethanol 25 mM. When ethanol is 50 mM, depolarization produces a decrease of CysAp activity in a 10.29% (p<0.01). Ethanol 100 mM decreases significantly (p<0.01) CysAP activity in a 42.14% in relation to the depolarized values (Figure 8B).
Effects of ethanol on LeuAP.
The analysis of ethanol effects on basal LeuAP activity shows the following results: Ethanol 25 and 100 mM produces a significant inhibitions (p<0.01) of this activity in a 24.5 and 36.87% respectively (figure 9A). On the other hand, ethanol 50 mM induces an increase of 104.05% (p<0.01) in relation to the control values.
Depolarization of synaptosomes with K+ 25 mM does not modify significantly the control values of LeuAP (figure 9B), but the simultaneous incubation of synaptosomes with K+ 25 mM and ethanol 25 mM produces a significant decrease (p<0.01) of this activity in a 10.43% in relation to the depolarized values. The presence of K+ 25 mM and ethanol 50 mM induces a inhibition of 28.1% (p<0.01). In the same way, ethanol 100 mM decreases LeuAP activity in a 55.2% (p<0.01) when is applied simultaneously with the stimulation of synaptosomes with K+ 25 mM (figure 9B).
Effects of ethanol on TyrAP.
The analysis of the effects of ethanol on basal TyrAP activity shows the following results: Differents concentrations of ethanol decreases this activity except for the concentration 50 mM that does not modify LeuAP. Thus, ethanol 25 mM produces a decrease in a 41% (p<0.01) (figure 10A) and ethanol 100 mM in a 49.29% (p<0.01) in relation to the control values.
Depolarization of synaptosomes with K+ 25 mM produces an inhibition of 6.53% (p<0.01) in the TyrAP activity (figure 10B). The simultaneous incubation of synaptosomes with K+ 25 mM and ethanol 25 mM does not modify the control values of TyrAP. The presence of K+ 25 mM and ethanol 50 mM induces a significant inhibition (p<0.01) of 10.87% in relation to the depolarized values. The stimulation of synaptosomes with K+ 25 mM in presence of ethanol 100 mM induces a significant inhibition (p<0.01) of the TyrAP activity in a 50.95%. (figure 10B).
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[Physiology] |
