title: Crystalline silica Min-U-Sil 5 induces oxidative stress in human bronchial epithelial cells BEAS-2B by reducing the efficiency of antiglycation and antioxidant enzymatic defenses.
abstract: Reactive oxygen species (ROS) play an important role as mediators of pulmonary damage in mineral dust-induced diseases. Studies carried out to date have largely focused on silica-induced production of ROS by lung phagocytes. In this study we investigated the hypothesis that crystalline silica Min-U-Sil 5 can induce elevations in intracellular ROS in human bronchial epithelial cells BEAS-2B, via an indirect mechanism that involves ROS-inducing intracellular factors, through a reduction of antiglycation (glyoxalase enzymes) and antioxidant (paraoxonase 1 and glutathione-S-transferases) enzymatic defenses. The results show that crystalline silica Min-U-Sil 5 causes a significant reduction in the efficiency of antiglycation and antioxidant enzymatic defenses, paralleled by an early and extensive ROS generation, thus preventing the cells from an efficient scavenging action, and eliciting oxidative damage. These results confirm the importance of ROS in development of crystalline silica-induced oxidative stress and emphasize the pivotal role of antiglycation/antioxidant and detoxifying systems in determining the level of protection from free radicals-induced injury for cells exposed to crystalline silica Min-U-Sil 5.
authors.affiliation: Department of Experimental Medicine, University of Perugia, via del Giochetto 06123, Perugia, Italy. cinzia.antognelli@unipg.it
authors.forename: Cinzia
authors.initials: C
authors.lastname: Antognelli
authors.forename: Angela
authors.initials: A
authors.lastname: Gambelunghe
authors.forename: Chiara
authors.initials: C
authors.lastname: Del Buono
authors.forename: Nicola
authors.initials: N
authors.lastname: Murgia
authors.forename: Vincenzo N
authors.initials: VN
authors.lastname: Talesa
authors.forename: Giacomo
authors.initials: G
authors.lastname: Muzi
mesh_terms: D043303:Aryldialkylphosphatase / Q000037:antagonists & inhibitors / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism; D001980:Bronchi / Q000187:drug effects* / Q000201:enzymology*; D002460:Cell Line; D002470:Cell Survival / Q000187:drug effects; D004847:Epithelial Cells / Q000187:drug effects / Q000201:enzymology; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007791:Lactoylglutathione Lyase / Q000037:antagonists & inhibitors / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism; D015227:Lipid Peroxidation / Q000187:drug effects; D008171:Lung Diseases / Q000139:chemically induced* / Q000201:enzymology*; D018384:Oxidative Stress / Q000187:drug effects* / Q000502:physiology; D011765:Pyruvaldehyde / Q000378:metabolism; D017382:Reactive Oxygen Species / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012822:Silicon Dioxide / Q000633:toxicity*; D013869:Thiolester Hydrolases / Q000037:antagonists & inhibitors / Q000096:biosynthesis / Q000235:genetics / Q000378:metabolism; D000099301:Hydroxyacylglutathione Hydrolase
chemical_list: D043303:Aryldialkylphosphatase; D005982:Glutathione Transferase; D007791:Lactoylglutathione Lyase; D011765:Pyruvaldehyde; D017382:Reactive Oxygen Species; D012822:Silicon Dioxide; D013869:Thiolester Hydrolases; D000099301:Hydroxyacylglutathione Hydrolase; C468406:PON1 protein, human