Proteomic profiling of differentially expressed proteins after exposure to asbestos

Muscat, J.E. & Wynder, E.L. Cigarette smoking, asbestos exposure, and malignant mesothelioma. Cancer Res. 51, 2263–2267 (1991). Scherpereel, A. et al. Guidelines of the european respiratory society and the european society of thoracic surgeons for the management of malignant pleural mesothelioma. Eur. Respir. J. 35, 479–495 (2010). Kanarek, M.S. Mesothelioma from chrysotile asbestos: update. Ann. Epidemiol. 21, 688–697 (2011). LaDou, J. et al. The case for a global ban on asbestos. Environ. Health Perspect. 118, 897–901 (2010). Mossman, B.T. et al. Pulmonary endpoints (lung carcinomas and asbestosis) following inhalation exposure to asbestos. J. Toxicol. Environ. Health B Crit. Rev. 14, 76–121 (2011). Agents Classified by the IARC Monographs, Volumes 1–107. http://monographs.iarc.fr/ENG/Classification/. Dopp, E. et al. ROS-mediated genotoxicity of asbestos-cement in mammalian lung cells in vitro. Part. Fibre Toxicol. 2, 9 (2005). Liu, G., Beri, R., Mueller, A. & Kamp, D.W. Molecular mechanisms of asbestos-induced lung epithelial cell apoptosis. Chem. Biol. Interact. 188, 309–318 (2010). Kumagai-Takei, N. et al. Asbestos induces reduction of tumor immunity. Clin. Dev. Immunol. 2011, 481439 (2011). Yang, H. et al. Programmed necrosis induced by asbestos in human mesothelial cells causes high-mobility group box 1 protein release and resultant inflammation. Proc. Natl. Acad. Sci. U. S. A. 107, 12611–12616 (2010). Palomäki, J. et al. Long, needle-like carbon nanotubes and asbestos activate the NLRP3 inflammasome through a similar mechanism. ACS Nano 5, 6861–6870 (2011). Ilavská, S. et al. Immunological monitoring in workers occupationally exposed to asbestos. Toxicology 206, 299–308 (2005). Matsuzaki, H. et al. Asbestos-induced cellular and molecular alteration of immunocompetent cells and their relationship with chronic inflammation and carcinogenesis. J. Biomed. Biotechnol. 2012, 492608 (2012). Maeda, M. et al. Reduction of CXC chemokine receptor 3 in an in vitro model of continuous exposure to asbestos in a human T-cell line, MT-2. Am. J. Respir. Cell Mol. Biol. 45, 470–479 (2011). Liu, W., Ernst, J.D. & Broaddus, V.C. Phagocytosis of crocidolite asbestos induces oxidative stress, DNA damage, and apoptosis in mesothelial cells. Am. J. Respir. Cell Mol. Biol. 23, 371–378 (2000). Chiapello, M., Daghino, S., Martino, E. & Perotto, S. Cellular response of Fusarium oxysporum to crocidolite asbestos as revealed by a combined proteomic approach. J. Proteome Res. 9, 3923–3931 (2010). Calderwood, S.K., Khaleque, M.A., Sawyer, D.B. & Ciocca, D.R. Heat shock proteins in cancer: chaperones of tumorigenesis. Trends Biochem. Sci. 31, 164–172 (2006). Arrigo, A.P. et al. Hsp27 (HspB1) and alphaB-crystallin (HspB5) as therapeutic targets. FEBS Lett. 581, 3665–3674 (2007). Shao, L., Perez, R.E., Gerthoffer, W.T., Truog, W.E. & Xu, D. Heat shock protein 27 protects lung epithelial cells from hyperoxia-induced apoptotic cell death. Pediatr. Res. 65, 328–333 (2009). Martin-Ventura, J.L. et al. Identification by a differential proteomic approach of heat shock protein 27 as a potential marker of atherosclerosis. Circulation 110, 2216–2219 (2004). D’Amours, O., Frenette, G., Fortier, M., Leclerc, P. & Sullivan, R. Proteomic comparison of detergent-extracted sperm proteins from bulls with different fertility indexes. Reproduction 139, 545–556 (2010). Yamamoto, Y. et al. Proteomic identification of protein targets for 15-deoxy-Δ (12,14)-prostaglandin J2 in neuronal plasma membrane. PLoS One 6, e17552 (2011). Gómez-Puertas, P., Martín-Benito, J., Carrascosa, J.L., Willison, K.R. & Valpuesta, J.M. The substrate recognition mechanisms in chaperonins. J. Mol. Recognit. 17, 85–94 (2004). Satish, L. et al. Differential expression of chaperonin containing T-complex polypeptide (CCT) subunits during fetal and adult skin wound healing. Cell Stress Chaperones 13, 527–533 (2008). Read, J.A., Winter, V.J., Eszes, C.M., Sessions, R.B. & Brady, R.L. Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins 43, 175–185 (2001). Guo, W.Z. et al. Lovastatin changes activities of lactate dehydrogenase A and B genes in rat myocardial cells. Chin. Med. J. 124, 423–428 (2011). Trédan, O. et al. Validation of prognostic scores for survival in cancer patients beyond first-line therapy. BMC Cancer 11, 95 (2011). Weiser, B., Gonye, G., Sykora, P., Crumm, S. & Cahill, A. Chronic ethanol feeding causes depression of mitochondrial elongation factor Tu in the rat liver: implications for the mitochondrial ribosome. Am. J. Physiol. Gastrointest. Liver Physiol. 300, G815–822 (2011). Xu, C., Wang, J., Li, J. & Fang, R. Expression of elongation factor (EF)-Tu is correlated with prognosis of gastric adenocarcinomas. Int. J. Mol. Sci. 12, 6645–6655 (2011). Wells, J., Henkler, F., Leversha, M. & Koshy, R. A mitochondrial elongation factor-like protein is over-expressed in tumours and differentially expressed in normal tissues. FEBS Lett. 358, 119–125 (1995). Hamrita, B. et al. An elongation factor-like protein (EF-Tu) elicits a humoral response in infiltrating ductal breast carcinomas: an immunoproteomics investigation. Clin. Biochem. 44, 1097–1104 (2011). Aasheim, H.C., Loukianova, T., Deggerdal, A. & Smeland, E.B. Tissue specific expression and cDNA structure of a human transcript encoding a nucleic acid binding [oligo(dC)] protein related to the premRNA binding protein K. Nucleic Acids Res. 22, 959–964 (1994). Bomsztyk, K., Denisenko, O. & Ostrowski, J. hnRNP K: one protein multiple processes. Bioessays 26, 629–638 (2004). Zhang, Z., Huang, L., Zhao, W. & Rigas, B. Annexin 1 induced by anti-inflammatory drugs binds to NF-kappaB and inhibits its activation: anticancer effects in vitro and in vivo. Cancer Res. 70, 2379–2388 (2010). Jia, Y. et al. Regulation of lung fibroblast activation by annexin A1. J. Cell. Physiol. 228, 476–484 (2013). D’Acquisto, F., Perretti, M. & Flower, R.J. Annexin-A1: a pivotal regulator of the innate and adaptive immune systems. Br. J. Pharmacol. 155, 152–169 (2008). Elsner, M. et al. MALDI imaging mass spectrometry reveals COX7A2, TAGLN2 and S100-A10 as novel prognostic markers in Barrett’s adenocarcinoma. J. Proteomics 75, 4693–4704 (2012). Rho, J.H., Roehrl, M.H. & Wang, J.Y. Tissue proteomics reveals differential and compartment-specific expression of the homologs transgelin and transgelin-2 in lung adenocarcinoma and its stroma. J. Proteome Res. 8, 5610–5618 (2009). Yoshino, H. et al. The tumour-suppressive function of miR-1 and miR-133a targeting TAGLN2 in bladder cancer. Br. J. Cancer 104, 808–818 (2011). Peklak-Scott, C., Smitherman, P.K., Townsend, A.J. & Morrow, C.S. Role of glutathione S-transferase P1-1 in the cellular detoxification of cisplatin. Mol. Cancer Ther. 7, 3247–3255 (2008). Schnekenburger, M. et al. Increased glutathione Stransferase P1-1 expression by mRNA stabilization in hemin-induced differentiation of K562 cells. Biochem. Pharmacol. 68, 1269–1277 (2004). Schnekenburger, M. et al. Expression of glutathione S-transferase P1-1 in differentiating K562: role of GATA-1. Biochem. Biophys. Res. Commun. 311, 815–821 (2003). Klamt, F. et al. Oxidant-induced apoptosis is mediated by oxidation of the actin-regulatory protein cofilin. Nat. Cell Biol. 11, 1241–1246 (2009). Hsieh, Y.C. et al. Methyl antcinate A from Antrodia camphorata induces apoptosis in human liver cancer cells through oxidant-mediated cofilin- and Bax-triggered mitochondrial pathway. Chem. Res. Toxicol. 23, 1256–1267 (2010). Seo, Y.N., Lee, Y.J. & Lee, M.Y. Differential gene expression by chrysotile in human bronchial epithelial cells. Animal Cells Syst. 16, 95–103 (2012). Kim, J.J., Kim, Y.H. & Lee, M.Y. Proteomic characterization of differentially expressed proteins associated with no stress in retinal ganglion cells. BMB Rep. 42, 456–461 (2009). Choi, K.M. & Lee, M.Y. Effect of freezing stress on the proteome expression of Antarctic green microalga. Mol. Cell. Toxicol. 8, 163–169 (2012). Park, S.K., Seo, J.B. & Lee, M.Y. Proteomic profiling of hempseed proteins from Cheungsam. Biochim. Biophys. Acta 1824, 374–382 (2012). Park, S.K., Jeon, Y.M., Son, B.S., Youn, H.S. & Lee, M.Y. Proteomic analysis of the differentially expressed proteins by airborne nanoparticles. J. Appl. Toxicol. 31, 463–470 (2011). Choi, K.M. & Lee, M.Y. Differential protein expression associated with heat stress in Antarctic microalga. BioChip J. 6, 271–279 (2012).