5% is highlighted starting with the first day postselleck exposure. The presence of infiltrating macrophages in the hepatic parenchyma, also noted at this early time point (Figure 2B), can account for the increased AOPP level. AOPP are formed subsequent to Table 1 Protein oxidative alterations Time (days) AOPP PSH CP Control Exposed Control Exposed Control Exposed 1 100 ± 13 183.5 ± 17** 100 ± 3 87.2 ± 10* 100 ± 13 98.4 ± 11 3 100 ± 16 191.5 ± 21** 100 ± 9 65 ± 5** 100 ± 12 102.3 ± 10 7 100 ± 10

208.9 ± 14** 100 ± 6 51 ± 13** 100 ± 9 90.9 ± 17 Carbonyl derivates of proteins (CP), advanced oxidation protein products (AOPP), and protein thiol groups (PSH) in liver of fish after 1, 3, and 7 days of silicon-based QDs exposure. Results are presented expressed as percent from controls ± RSD GW4869 solubility dmso (n = 6); * P < 0.05; ** P < 0.01. neutrophil myeloperoxidase activation, by the action of hypochlorite that selectively attacks proteins, aiming primarily at the lysine, tryptophan, selleckchem cysteine, and methionine residues. Current literature supports the role of protein thiol groups as prime ROS targets. In fact, PSH can scavenge 50% to 75% of intracellular generated ROS, suffering reversible or irreversible oxidations during this process [68]. Our data showed that PSH

were reduced in the liver of fish IP injected with Si/SiO2 QDs (Table 1). After 1 day, the PSH level diminished by about 13% while, for longer periods, the decrease Glycogen branching enzyme was amplified, i.e., it was reduced by 35% after 3 days and by 49% after 7 days. The continuous decrease of PSH over the 7-day period may imply that sufficient PSHs were available to be oxidized and thus explain the protection from more severe protein oxidative damage, such as carbonylation. Our current results indicated that protein carbonylation is not a characteristic alteration in silicon-based QD-induced oxidative stress in the liver since protein

carbonyls maintained at a basal level (Table 1). Our previous results indicated a decrease in PSH content in the kidney of C. gibelio[70], while in white muscle tissue, this parameter remained unchanged after QDs administration [71]. These differences are probably due to the QDs in vivo distribution, since the liver is a main target Figure 4 GPX and GST specific activities in liver of Carassius gibelio injected with silicon-based QDs. Results are expressed as percent from controls ± RSD (n = 6); * P ≤ 0.05; ** P ≤ 0.01. of QDs accumulation and the kidney is involved in the nanoparticles clearance, whereas white muscle accumulated QDs to a lesser extent due to its poor vascularization. Antioxidant defense system The liver enzymatic antioxidant defense is modulated in response to the redox status changes initiated by Si/SiO2 QDs. Figure 5 shows the different responses of SOD and CAT to silicon-based QDs accumulation in the liver of C. gibelio. These differences may be explained on the account of their functions. SOD activity increased by 40.