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

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  • Published: Jan 24, 2011
  • Channels: Electrophoresis
thumbnail image: Journal Highlight: Proteomic identification of the differentially expressed proteins in human lung epithelial cells by airborne particulate matter

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

Journal of Applied Toxicology, 2011, 31, 45 - 52
Yu Mi Jeon, Bu Soon Son, Mi Young Lee

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.

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Release of airborne particles

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