Fate and behavior of ZnO- and Ag-engineered nanoparticles and a bacterial viability assessment in a simulated wastewater treatment plant.

The fate and behaviour assessment of ZnO- and Ag-engineered nanoparticles (ENPs) and bacterial viability in a simulated wastewater treatment plant (WWTP) fed with municipal wastewater was investigated through determination of ENPs stability at varying pH and continuous exposure of ENPs to wastewater, respectively. The ENPs were introduced to a 3-L bioreactor (simulated WWTP) with a hydraulic residence time (HRT) of 6 h at a dose rate of 0.83 mg/min for 240 h. The stability of the ENPs was found to be dependent on their dissolution and aggregation at different pH, where ZnO ENPs exhibited the highest dissolution at low pH compared to Ag ENPs. The results also showed that both ENPs had high affinity for the sewage sludge as they undergo aggregation under typical wastewater conditions. Results of effluent monitored daily showed mean COD removal efficiencies of 71 ± 7% and 74 ± 8% for ZnO and Ag ENPs in test units, respectively. The treated effluent had low mean concentrations of Zn (1.39 ± 0.54 mg/L) and Ag (0.12 ± 0.06 mg/L); however, elevated mean concentrations of Zn (54 ± 39 mg/g dry sludge) and Ag (57 ± 42 mg/g dry sludge) were found in the sludge - suggesting removal of the ENPs from the wastewater by biosorption and biosolid settling mechanisms. Using X-ray diffraction (XRD) and transmission electron microscopy (TEM), the mineral identities of ZnO and Ag ENPs in the sludge from the test units were found comparable to those of commercial ENPs, but larger due to agglomeration. The bacterial viability assessment after exposure to ENPs using the Live/Dead BacLight kit, although not quantitatively assessed, suggested high resilience of the bacteria useful for biodegradation of organic material in the simulated wastewater treatment system.

Extracellular superoxide dismutase in biology and medicine.

Accumulated evidence has shown that reactive oxygen species (ROS) are important mediators of cell signaling events such as inflammatory reactions (superoxide) and the maintenance of vascular tone (nitric oxide). However, overproduction of ROS such as superoxide has been associated with the pathogenesis of a variety of diseases including cardiovascular diseases, neurological disorders, and pulmonary diseases. Antioxidant enzymes are, in part, responsible for maintaining low levels of these oxygen metabolites in tissues and may play key roles in controlling or preventing these conditions. One key antioxidant enzyme implicated in the regulation of ROS-mediated tissue damage is extracellular superoxide dismutase (EC-SOD). EC-SOD is found in the extracellular matrix of tissues and is ideally situated to prevent cell and tissue damage initiated by extracellularly produced ROS. In addition, EC-SOD is likely to play an important role in mediating nitric oxide-induced signaling events, since the reaction of superoxide and nitric oxide can interfere with nitric oxide signaling. This review will discuss the regulation of EC-SOD and its role in a variety of oxidant-mediated diseases.

Depletion of pulmonary EC-SOD after exposure to hyperoxia.

Extracellular superoxide dismutase (EC-SOD) is highly expressed in lung tissue. EC-SOD contains a heparin-binding domain that is sensitive to proteolysis. This heparin-binding domain is important in allowing EC-SOD to exist in relatively high concentrations in specific regions of the extracellular matrix and on cell surfaces. EC-SOD has been shown to protect the lung against hyperoxia in transgenic and knockout studies. This study tests the hypothesis that proteolytic clearance of EC-SOD from the lung during hyperoxia contributes to the oxidant-antioxidant imbalance that is associated with this injury. Exposure to 100% oxygen for 72 h resulted in a significant decrease in EC-SOD levels in the lungs and bronchoalveolar lavage fluid of mice. This correlated with a significant depletion of EC-SOD from the alveolar parenchyma as determined by immunofluorescence and immunohistochemistry. EC-SOD mRNA was unaffected by hyperoxia; however, there was an increase in the ratio of proteolyzed to uncut EC-SOD after hyperoxia, which suggests that hyperoxia depletes EC-SOD from the alveolar parenchyma by cutting the heparin-binding domain. This may enhance hyperoxic pulmonary injury by altering the oxidant-antioxidant balance in alveolar spaces.

Purification and characterization of mouse soluble receptor for advanced glycation end products (sRAGE).

The receptor for advanced glycation end products (RAGE) is a member of the immunoglobulin superfamily of cell surface proteins that has been implicated as a progression factor in a number of pathologic conditions from chronic inflammation to cancer to Alzheimer's disease. In such conditions, RAGE acts to facilitate pathogenic processes. Its secreted isoform, soluble RAGE or sRAGE, has the ability to prevent RAGE signaling by acting as a decoy. sRAGE has been used successfully in animal models of a range of diseases to antagonize RAGE-mediated pathologic processes. In humans, sRAGE results from alternative splicing of RAGE mRNA. This study was aimed to determine whether the same holds true for mouse sRAGE and, in addition, to biochemically characterize mouse sRAGE. The biochemical characteristics examined include glycosylation and disulfide patterns. In addition, sRAGE was found to bind heparin, which may mediate its distribution in the extracellular matrix and cell surfaces of tissues. Finally, our data indicated that sRAGE in the mouse is likely produced by carboxyl-terminal truncation, in contrast to the alternative splicing mechanism reported in humans.