Proteome Profile of Extratemporal Structures in Amygdala Kindling Mesial Temporal Lobe Epilepsy Rat Model: A Preliminary Study

Background: Mesial temporal lobe epilepsy is the most prevalent type of human epilepsy and its pathogenesis still remains unknown. Structures outside the temporal lobe may also play critical roles in the disease’s progress. Objective: The aim of this study was to investigate proteome alterations and to identify differentially expressed proteins in frontoparietal cortex and thalamus regions of 6-month-old amygdala-kindled WAG/Rij rats as a mesial temporal lobe epilepsy model by using bottom-up proteomics approach. Method: Protein extraction from the tissues was followed by two-dimensional gel electrophoresis. Proteins were identified by peptide mass fingerprinting analysis using MALDI-TOF MS followed by MASCOT database search. Results: 58 and 47 proteins were identified in frontoparietal cortex and thalamus, respectively. Differentially expressed proteins in frontoparietal cortex were all up-regulated in the kindled groups compared to kindled-resistant group (p<0.05). These proteins were; Fabp4, Gamma-enolase, Annexin AI, Rab-15, RAB6-interacting golgin, PGAM1, DAB-2 and Fructose-bisphosphate aldolase C. In thalamus, BDNF (in spot 13), TRAPPC2L, Ras-related protein Rab-2A, GTP-binding protein REM 2 and Calcyclin-binding protein were up-regulated (p<0.05); and BDNF (in spot 9), kif3a, Parvalbumin alpha were down-regulated in the kindled groups compared to the kindled-resistant group (p<0,05). Conclusion: In this study, we identified proteins that might have roles in enabling or complicating mesial temporal lobe epilepsy progress. The potential of these proteins as biomarkers needs further research.