Abstract
We analyzed a number of 2-DE protein spots in Long-Evans Cinnamon (LEC) rats as an animal model for human Wilson's disease using matrix-assisted laser desorption/ionization (MALDI)-time of flight mass spectrometry (TOF-MS). Livers from LEC and WKAH/Hkm (control) rats of 12 and 16 weeks of age were separately homogenized and performed with 2-DE. Protein spots of 2-DE were analyzed by using image analysis software to compare the changes in protein quantities. Seventeen protein spots were found to be different between the two strains of 12 and 16 weeks of age. In detail, four protein spots increased by 1.5 times in LEC rats, compared with control. The two protein spots were determined as fructose-1-6-bisphosphatase and argininosuccinate-synthase. On the other hand, 12 protein spots decreased by 2 times (n=8) and by 1.5 times (n=4) in LEC rats. All identified proteins (10 of 12) were belonging to a group of superoxide dismutase (SOD), such as catalase, glutathione-transferase, peroxisome. Interestingly,one protein spot of 35 kDa was completely disappeared in LEC rats of 4-16 weeks of age, whereas it was positive in control. Finally, increase and decrease patterns of the 17 protein spots identified in 12 and 16 weeks LEC rats were similarly observed in the younger LEC rats of 4, 8 and 10 weeks of age. These results suggest that decrease in the expression of SOD proteins may be related with a cause and/or progress of Wilson's disease. [J Physiol Sci. 2007;57 Suppl:S131]
