Proteomic identification of the differentially expressed proteins in human lung epithelial cells by airborne particulate matter

Abstract

Exposure to airborne PM₁₀, particulate matter with a median aerodynamic diameter of less than 10 µm, is known to be associated with a number of adverse health effects. To gain a better understanding of the cytotoxic mechanism and to develop protein biomarker candidates for PM₁₀-induced toxicity, proteomic analyses were performed in human lung epithelial cells. Two-dimensional gel electrophoresis (2-DE) was followed by matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF MS) to analyze the proteins differentially expressed by exposure to PM₁₀. Analysis of 2-DE gels revealed more than 1270 protein spots in the cells, of which 36 showed changes of more than 2-fold on exposure to PM₁₀ (up-regulation, n = 6; down-regulation, n = 30). The glycolytic enzyme pyruvate kinase, which also plays a role in tumor metabolism, showed a marked increase in expression, whereas the cytoskeleton-related vinculin and anti-inflammatory annexin 1 showed marked decreases in expression.

Genomic instability of gold nanoparticle treated human lung fibroblast cells

“…Studies which employ this proteomic technique have been used in experiments involving silica nanoparticles [20], multi-walled carbon nanotubes [21], titanium dioxide nanoparticles [22], airborne particulate matter [23] and silver nanoparticles [24] but there are few on AuNPs [25].…”

Predictive and Prognostic Biomarkers of Respiratory Diseases due to Particulate Matter Exposure

“…A number of kinases are associated with inflammatory response 52. Many studies have shown that inflammatory response is related to PM exposure 53. It has been reported that bacteria-derived endotoxin bound to the surface of PM particle is one of the causative agent in PM-mediated lung injury 54–56.…”

Toxicoproteomic identification of TiO2nanoparticle-induced protein expression changes in mouse brain

“…After isoelectric focusing, the strips were soaked twice for 20 min each in equilibration buffer (6 M urea, 2% w/v SDS, 20% v/v glycerol, 5 mM tributylphosphine, 2.5% acrylamide, 0.01% bromophenol blue, 0.375 M Tris-HCl, pH 8.8). The seconddimension SDS-PAGE was performed in 8Á16% gradient polyacrylamide gels without a stacking gel, at 108C for 2 h at 5 mA/gel and then at 18 mA/gel (Bartkowiak et al 2009;Choi et al 2009;Jeon et al 2011;Park et al 2010). Protein bands were visualized by staining with Coomassie Brilliant Blue G-250.…”