Volatile Organic Compounds and Metal Leaching from Composite Products Made from Fiberglass-Resin Portion of Printed Circuit Board Waste

This study focused on the volatile organic compounds (VOCs) and metal leaching from three kinds of composite products made from fiberglass-resin portion (FRP) of crushed printed circuit board (PCB) waste, including phenolic molding compound (PMC), wood plastic composite (WPC), and nonmetallic plate (NMP). Released VOCs from the composite products were quantified by air sampling on adsorbent followed by thermal desorption and GC-MS analysis. The results showed that VOCs emitted from composite products originated from the added organic components during manufacturing process. Phenol in PMC panels came primarily from phenolic resin, and the airborne concentration of phenol emitted from PMC product was 59.4 ± 6.1 μg/m³, which was lower than odor threshold of 100% response for phenol (180 μg/m³). VOCs from WPC product mainly originated from wood flour, e.g., benzaldehyde, octanal, and d-limonene were emitted in relatively low concentrations. For VOCs emitted from NMP product, the airborne concentration of styrene was the highest (633 ± 67 μg/m³). Leaching characteristics of metal ions from composite products were tested using acetic acid buffer solution and sulphuric acid and nitric acid solution. Then the metal concentrations in the leachates were tested by ICP-AES. The results showed that only the concentration of Cu (average = 893 mg/L; limit = 100 mg/L) in the leachate solution of the FRP using acetic acid buffer solution exceeded the standard limit. However, concentrations of other metal ions (Pb, Cd, Cr, Ba, and Ni) were within the standard limit. All the results indicated that the FRP in composite products was not a major concern in terms of environmental assessment based upon VOCs tests and leaching characteristics

Novel Effective Catalyst for Elemental Mercury Removal from Coal-Fired Flue Gas and the Mechanism Investigation

Mercury pollution from coal-fired power plants has drawn attention worldwide. To achieve efficient catalytic oxidation of Hg⁰ at both high and low temperatures, we prepared and tested novel IrO₂ modified Ce–Zr solid solution catalysts under various conditions. It was found that the IrO₂/Ce_0.6Zr_0.4O₂ catalyst, which was prepared using the polyvinylpyrrolidone-assisted sol–gel method, displayed significantly higher catalytic activity for Hg⁰ oxidation. The mechanism of Hg⁰ removal over IrO₂/Ce_0.6Zr_0.4O₂ was studied using various methods, and the Hg⁰ oxidation reaction was found to follow two possible pathways. For the new chemisorption–regeneration mechanism proposed in this study, the adsorbed Hg⁰ was first oxidized with surface chemisorbed oxygen species to form HgO; the HgO could desorb from the surface of catalysts by itself or react with adsorbed HCl to be release in the form of gaseous HgCl₂. O₂ is indispensable for the chemisorption process, and the doping of IrO₂ could facilitate the chemisorption process. In addition, the Deacon reaction mechanism was also feasible for Hg⁰ oxidation: this reaction would involve first oxidizing the adsorbed HCl to active Cl species, after which the Hg⁰ could react with Cl to form HgCl₂. Additionally, doping IrO₂ could significantly improve the Cl yield process. In summary, the novel IrO₂ modified catalyst displayed excellent catalytic activity for elemental mercury oxidation, and the proposed reaction mechanisms were determined reasonably

Proteomic Analysis of Two Metabolic Proteins with Potential to Translocate to Plasma Membrane Associated with Tumor Metastasis Development and Drug Targets

Metastasis is the main cause for death of breast cancer patients. However, the underlying mechanism is still poorly understood. Plasma membrane (PM) proteins play a key role in various biological processes, especially for cell migration. In this study, we used a set of well-characterized mammary mouse cell lines, 67NR, 168FARN, 4T1, representing the metastatic progression, to study the differentially expressed membrane proteins. These proteins were analyzed by a linear ion trap tandem mass spectrometry (LTQ-MS/MS) following cell surface biotinylation and streptavidin purification. A total of 1667 membrane proteins were identified, out of which 472 were characterized as differentially expressed with at least 2-fold change and <i>p</i>-value < 0.01. Functional clustering of the 472 proteins revealed that 178 of them were metabolic proteins. Finally, we focused on two metabolic proteins, fatty acid synthase (FASN) and NAD­(P)H steroid dehydrogenase-like protein (NSDHL), which were validated by Western blot and immunofluorescence. We found that FASN and NSDHL translocated to the plasma membrane from the intracellular compartment, and their expressions increased from 67NR to 4T1. This alteration of localization along with differential expressions might be necessary for metastasis development. Potentially, FASN and NSDHL could serve as drug targets in new antimetastasis therapy

Correlation between peripheral blood mononuclear cell (a) nuclear NF-κB p65 protein and uACR (b) NF-κB p65 mRNA and uACR, or (c) NF-κB p65 mRNA and eGFR.

<p>Correlation between peripheral blood mononuclear cell (a) nuclear NF-κB p65 protein and uACR (b) NF-κB p65 mRNA and uACR, or (c) NF-κB p65 mRNA and eGFR.</p

Correlation between urinary RANTES excretion rate and (a) nuclear NF-κB p65 protein, (b) NF-κB p65 mRNA or (c) eGFR.

<p>Correlation between urinary RANTES excretion rate and (a) nuclear NF-κB p65 protein, (b) NF-κB p65 mRNA or (c) eGFR.</p

Excretion rates of urinary MCP-1 and RANTES.

<p>Note: Compared with NC group **: P<0.01; compared with DN0 group ##: P<0.01; compared with DN1 group △△: P<0.01.</p

Correlation between urinary MCP-1 excretion rate and (a) nuclear NF-κB p65 protein, (b) NF-κB p65 mRNA or (c) eGFR.

<p>Correlation between urinary MCP-1 excretion rate and (a) nuclear NF-κB p65 protein, (b) NF-κB p65 mRNA or (c) eGFR.</p

Correlation between urinary MCP-1 excretion rate and uACR.

<p>Correlation between urinary MCP-1 excretion rate and uACR.</p

Identification of EFEMP2 as a Serum Biomarker for the Early Detection of Colorectal Cancer with Lectin Affinity Capture Assisted Secretome Analysis of Cultured Fresh Tissues

Early diagnosis plays a decisive role in the outcome of colorectal cancer (CRC) therapy. The ex vivo culture of fresh CRC tissues and paired normal colorectal tissues provides a feasible way to explore potential serum biomarkers for CRC early detection under near-physiological conditions. In the present work, we applied a lectin affinity based approach to enrich and increase the detection number of secreted proteins in the conditioned media of cultured tissues. The captured proteins were then analyzed by the proteomic strategy of one-dimensional gel electrophoresis coupled to liquid chromatography–tandem mass spectrometry. By quantification with label-free spectral counting, we found 123 differentially expressed secreted proteins (DESPs) with 68 DESPs up-regulated in CRC tissues. EFEMP2, one of the top 10 up-regulated DESPs, was further validated by immunohistochemistry at tissue level and enzyme-linked immunosorbent assay at serum level. We found the expression level of EFEMP2 was dramatically increased in CRC patients, even at the early stage. Moreover, the diagnostic accuracy of EFEMP2 was superior to the established CRC biomarker carcinoembryonic antigen evidenced by the area under the receiver operating characteristic curve for the two biomarkers were 0.923 and 0.728, respectively. These results indicated EFEMP2 is a promising serum biomarker for CRC early detection

Identification of EFEMP2 as a Serum Biomarker for the Early Detection of Colorectal Cancer with Lectin Affinity Capture Assisted Secretome Analysis of Cultured Fresh Tissues

Early diagnosis plays a decisive role in the outcome of colorectal cancer (CRC) therapy. The ex vivo culture of fresh CRC tissues and paired normal colorectal tissues provides a feasible way to explore potential serum biomarkers for CRC early detection under near-physiological conditions. In the present work, we applied a lectin affinity based approach to enrich and increase the detection number of secreted proteins in the conditioned media of cultured tissues. The captured proteins were then analyzed by the proteomic strategy of one-dimensional gel electrophoresis coupled to liquid chromatography–tandem mass spectrometry. By quantification with label-free spectral counting, we found 123 differentially expressed secreted proteins (DESPs) with 68 DESPs up-regulated in CRC tissues. EFEMP2, one of the top 10 up-regulated DESPs, was further validated by immunohistochemistry at tissue level and enzyme-linked immunosorbent assay at serum level. We found the expression level of EFEMP2 was dramatically increased in CRC patients, even at the early stage. Moreover, the diagnostic accuracy of EFEMP2 was superior to the established CRC biomarker carcinoembryonic antigen evidenced by the area under the receiver operating characteristic curve for the two biomarkers were 0.923 and 0.728, respectively. These results indicated EFEMP2 is a promising serum biomarker for CRC early detection