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Acta Physiologica 2012; Volume 206, Supplement 693
Joint FEPS and Spanish Physiological Society Scientific Congress 2012
9/8/2012-9/11/2012
Santiago de Compostela, Spain
THE AMYLOID PEPTIDE REDUCES THE PHOSPHORYLATION OF A VOLTAGE-DEPENDENT ANION-CHANNEL INVOLVED IN APOPTOSIS
Abstract number: P21
Fernandez1 C, Marin1 R
1Laboratory of Cellular Neurobiology, Dept. Physiology, , School of Medicine, La Laguna University, La Laguna 38320, Tenerife, Spain
Objectives:
The voltage-dependent anion-channel (VDAC) is a mitochondrial porin related to apoptosis. It has also been found at the plasma membrane, where it participates in extrinsic apoptotic pathways, and in the modulation of amyloid beta toxicity, a parameter of the pathology of Alzheimer's disease (AD). Following the line of post-translational profile characterization of VDAC, we analyzed the modulation of its phosphorylation state, following exposure to the beta-amyloid peptide at different times.
Materials:
Characterization of post-translational profile was obtained by two-dimensional electrophoresis, while the time-course experiments were performed using one-dimensional electrophoresis tests, followed by western-blot analysis. Quantitative data expressed as mean ± standard error (SEM) were obtained using the program Statistix V.7 by one-way ANOVA (p<0.05).
Results:
Different phosphorylated forms of this channel have been identified in immortalized neuronal cells. This post-transductional pattern has been confirmed in membrane fractions of different brain areas from male and female mouse brain, where no differences in VDAC amount have been detected. In the time-course experiments, we established a dose-time modification of VDAC phosphoisoforms as the result of beta-amyloid induced toxicity. These results evidence a reduction of the channel phosphorylation at short-time exposures. We also observed that VDAC phosphorylation state was recovered back at longer beta-amyloid exposures.
Conclusions:
Different phosphorylated forms of VDAC were constitutively present in the neuronal membrane in either cell lines or immortalized neural brain areas of male and female mice. Exposure to beta-amyloid peptide seems to cause changes in the phosphorylation pattern of this porin at the neuronal membrane. This phenomenon could be of great interest in relation to the mechanisms developed by the beta amyloid peptide in neuronal death programmes.
Acknowledgments:
Supported by grants SAF2010-22114-CO2-01/02 (RM). C.F holds a fellowship from ACIISI.
To cite this abstract, please use the following information:
Acta Physiologica 2012; Volume 206, Supplement 693 :P21