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

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.