The differentially abundant peptides were identified by nano-LC-ESI-Orbitrap MS. These measurements were carried out on a Ultimate 3000 nano LC system (Dionex, Germering, Germany) online coupled to a hybrid linear ion trap/Orbitrap MS (LTQ Orbitrap XL; Thermo Fisher Scientific, Germany). Five mL digest were loaded on to a C18 trap column (C18 PepMap, 300 mm ID 65 mm, 5 mm particle size, 100 Å pore size; Dionex, The Netherlands) and desalted for 10 minutes using a flow rate of 20 mL/min 0.1% TFA. Then the trap column was switched online with the analytical column (PepMap C18, 75 mm ID 6150 mm, 3 mm particle and 100 Å pore size; Dionex, The Netherlands) and peptides were eluted with following binary gradient: 0%-25% solvent B in 120 min and 25%-50% solvent B in further 60 minutes, where solvent A consist of 2% acetonitrile and 0.1% formic in water and solvent B consists of 80% acetonitrile and 0.08% formic acid in water. Column flow rate was set to 300 nL/ min. For MS detection a data dependent acquisition method was used: high resolution survey scan from 400-1800 Th. was performed in the Orbitrap (value of target of automatic gain control AGC 10 6 , resolution 30,000 at 400 m/z; lock mass was set to 445.120025 u (protonated (Si(CH 3 ) 2 O) 6 ) [15] ). Based on this survey scan the 5 most intensive ions were consecutively isolated (AGC target set to 10 4 ions) and fragmented by collision-activated dissociation (CAD) applying 35% normalized collision energy in the linear ion trap. After precursors were selected for MS/MS, they were excluded for further MS/MS spectra for 3 minutes. The MS/MS identifications were obtained using in the Bioworks 3.2 (peak picking by Extract_msn, default settings) software package (Thermo Fisher Scientific, Germany), and its' SEQUEST feature, using minimum XC scores of 1.8, 2.2 and 3.75 for reliable identification of single, double and triple charged ions respectively in the UniProt-database (version 56.0, human taxonomy (20069 entries)). Carboxymethylation of Cysteine (+57.021 u) as fixed and oxidation of Methionine (+15.996 u) as variable modifications and tryptic cleavage were considered. The number of allowed missed cleavages was 2, the mass tolerance for precursor ions was 10 ppm and for fragment ions 0.5 Da. The cut-off for mass differences with the theoretical mass of the identified peptides was set at 2 ppm.