Differential proteome of the striatum from A30P α-Synuclein transgenic mouse model of parkinson´s disease

Parkinson´s disease (PD) is a multifactorial, neurodegenerative disease where etiopathogenesis are not fully understood. Mutations in α-Synuclein (α-Syn) were the first genetic defect linked to PD. They are deposited in Lewy bodies (LBs) characteristic for PD. Some experiments had showed that A30P mutant a-Syn have high toxicity than wide-type α-Syn. Here we used A30Pα-Syn transgenic mice model to analysed proteome changes of the striatum 11 months after the birth. Striata were removed and after digesting the proteins we used isotope labelling method to mark different group of peptides. Strong-cation exchange (SCX) liquid chromatography (LC) was integrated with peptide separation as the first dimension of the two-dimensional LC tandem mass spectrometry workflow. In this work, electrospray ionization (ESI) quadrupole time-of-flight (QTOF) mass spectrometer was explored as a means of detecting the Ms/Ms spectrogram. Agilent Spectrum Mill software was used to analysed the results. A total of 660 proteins were quantified. 280 proteins were down-regulated and 77 proteins were up-regulated.