Acrylamide induced the activation of NLRP3 inflammasome via ROS-MAPKs pathways in Kupffer cells

References

• Ajizian, S., English, B. K., & Meals, E. (1999). Specific inhibitors of p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways block inducible nitric oxide synthase and tumor necrosis factor accumulation in murine macrophages stimulated with lipopolysaccharide and interferon-γ. The Journal of Infectious Diseases, 179(4), 939–944. doi: 10.1086/314659
   PubMed Web of Science ®Google Scholar
• Ali, S., Timmer, A., Bilgrami, S., Park, E., Eckmann, L., Nizet, V., & Karin, M. (2011). Anthrax toxin induces macrophage death by p38 MAPK inhibition but leads to inflammasome activation via ATP Leakage. Immunity, 35(1), 34–44. doi:10.1016/j.immuni.2011.04.015.
   PubMed Web of Science ®Google Scholar
• Berghe, V. W. (1998). P38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-kappa B p65 transactivation mediated by tumor necrosis factor. Journal of Biological Chemistry, 273(6), 3285–3290. doi: 10.1074/jbc.273.6.3285
   PubMed Web of Science ®Google Scholar
• Chessa, D., Ganau, G., & Mazzarello, V. (2015). An overview of staphylococcus epidermidis and staphylococcus aureus with a focus on developing countries. The Journal of Infection in Developing Countries, 9(6), 547–550. doi: 10.3855/jidc.6923
   Google Scholar
• Chunteng, J., Liping, J., Qiannan, L., Xiaofang, L., Tianjiao, Z., & Linlin, D. (2018). Acrolein induces NLRP3 inflammasome-mediated pyroptosis and suppresses migration via ROS-dependent autophagy in vascular endothelial cells. Toxicology, 410, 26–40. doi:10.1016/j.tox.2018.09.002.
   PubMed Web of Science ®Google Scholar
• Daniele, S., Da Pozzo, E., Zappelli, E., & Martini, C. (2015). Trazodone treatment protects neuronal-like cells from inflammatory insult by inhibiting NF-κB, p38 and JNK. Cellular Signalling, 27(8), 1609–1629. doi:10.1016/j.cellsig.2015.04.006.
   PubMed Web of Science ®Google Scholar
• Dearfield, K. L., Abernathy, C. O., Ottley, M. S., Brantner, J. H., & Hayes, P. F. (1988). Acrylamide: Its metabolism, developmental and reproductive effects, genotoxicity, and carcinogenicity. Mutation Research/Reviews in Genetic Toxicology, 195(1), 45–77. doi:10.1016/0165-1110(88)90015-2.
   Google Scholar
• Debnath, T., Kim, E. K., Nath, N., & Lee, K. G. (2017). Therapeutic effects of Ligularia stenocephala against inflammatory bowel disease by regulating Antioxidant and inflammatory mediators. Food & Agricultural Immunology, 28(6), 1–13. doi:10.1080/09540105.2017.1332008.
   Web of Science ®Google Scholar
• Dixon, L. J., Barnes, M., Tang, H., Pritchard, M. T., & Nagy, Laura. E.. (2013). Kupffer cells in the liver. Comprehensive Physiology, 3(2), 785–797. doi:10.1002/cphy.c120026.
   PubMed Web of Science ®Google Scholar
• Erkekoglu, P., & Baydar, T. (1984). Acrylamide neurotoxicity. Food & Chemical Toxicology An International Journal Published for the British Industrial Biological Research Association, 17(2), 49–57. doi: 10.1179/1476830513Y.0000000065
   Google Scholar
• Erkekoglu, P., & Baydar, T. (2010). Toxicity of acrylamide and evaluation of its exposure in baby foods. Nutrition Research Reviews, 23(2), 323–333. doi: 10.1017/S0954422410000211
   PubMed Web of Science ®Google Scholar
• Esposito, F., Nardone, A., Fasano, E., Triassi, M., & Cirillo, T. (2017). Determination of acrylamide levels in potato crisps and other snacks and exposure risk assessment through a margin of exposure approach. Food and Chemical Toxicology, 108(A), 249–256. doi:10.1016/j.fct.2017.08.006.
   PubMedGoogle Scholar
• Exon, J. H. (2006). A review of the toxicology of acrylamide. Journal of Toxicology & Environmental Health Part B, 9(5), 397–412. doi: 10.1080/10937400600681430
   PubMedGoogle Scholar
• Friedman, M. (2003). Chemistry, biochemistry, and safety of acrylamide. A review. Journal of Agricultural and Food Chemistry, 51(16), 4504–4526. doi:10.1021/jf030204+ doi: 10.1021/jf030204+
   PubMed Web of Science ®Google Scholar
• Ghonime, M. G., Shamaa, O. R., Das, S., Eldomany, R. A., Fernandes, A. T., & Alnemri, E. S. (2014). Inflammasome priming by lipopolysaccharide is dependent upon ERK signaling and proteasome function. The Journal of Immunology, 192(8), 3881–3888. doi:10.4049/jimmunol.1301974.
   PubMed Web of Science ®Google Scholar
• Guarda, G., Zenger, M., Yazdi, A. S., Schroder, K., Ferrero, I., & Menu, P. (2011). Differential expression of NLRP3 among hematopoietic cells. The Journal of Immunology, 186(4), 2529–2534. doi:10.4049/jimmunol.1002720.
   PubMed Web of Science ®Google Scholar
• Li, P. Z., Li, J. Z., Li, M., Gong, J. P., & He, K. (2014). An efficient method to isolate and culture mouse Kupffer cells. Immunology Letters, 158(1-2), 52–56. doi:10.1016/j.imlet.2013.12.002.
   PubMed Web of Science ®Google Scholar
• Liang, L., Tan, X., Zhou, Q., Zhu, Y., Tian, Y., & Yu, H. (2013). IL-1β triggered by peptidoglycan and lipopolysaccharide through TLR2/4 and ROS-NLRP3 inflammasome–dependent pathways is involved in ocular Behcet’s disease. Investigative Opthalmology & Visual Science, 54(1), 402–414. doi:10.1167/iovs.12-11047.
   PubMed Web of Science ®Google Scholar
• Liu, G. Z. (1989). Effect of acrylamide on liver function of workers. Journal of Hygienic Toxicology, 3, 197.
   Google Scholar
• Mottram, D. S., Wedzicha, B. L., & Dodson, A. T. (2002). Food chemistry: Acrylamide is formed in the Maillard reaction. Nature, 419(6906), 448–449. doi: 10.1038/419448a
   PubMed Web of Science ®Google Scholar
• Okada, M., Matsuzawa, A., Yoshimura, A., & Ichijo, H. (2014). The lysosome rupture-activated TAK1-JNK pathway regulates NLRP3 inflammasome activation. Journal of Biological Chemistry, 289(47), 32926–32936. doi:10.1074/jbc.M114.579961.
   PubMed Web of Science ®Google Scholar
• Palus, K., Obremski, K., Bulc, M., & Całka, J. (2019). The impact of low and high doses of acrylamide on the intramural neurons of the porcine ileum. Food and Chemical Toxicology, 132, 110673. doi:10.1016/j.fct.2019.110673.
   PubMed Web of Science ®Google Scholar
• Pan, X., Wu, X., Yan, D. D., Peng, C., Rao, C. L., & Yan, H. (2018). Acrylamide-induced oxidative stress and inflammatory response are alleviated by N-acetylcysteine in PC12 cells: Involvement of the crosstalk between Nrf2 and NF-κB pathways regulated by MAPKs. Toxicology Letters, 288, 55–64. doi:10.1016/j.toxlet.2018.02.002.
   PubMed Web of Science ®Google Scholar
• Pearson, G., Robinson, F., Gibson, T. B., Xu, B. E., Karandikar, M., & Berman, K. (2001). Mitogen-activated protein (MAP) kinase pathways: Regulation and physiological functions 1. Endocrine Reviews, 22(2), 153–183. doi:10.1210/edrv.22.2.0428.
   PubMed Web of Science ®Google Scholar
• Pétrilli, V., Dostert, C., Muruve, D. A., & Tschopp , J. (2007). The inflammasome: A danger sensing complex triggering innate immunity. Current Opinion in Immunology, 19(6), 615–622. doi:10.1016/j.coi.2007.09.002.
   PubMed Web of Science ®Google Scholar
• Qu, J., Yuan, Z., Wang, G., Wang, X., & Li, K. (2019). The selective NLRP3 inflammasome inhibitor MCC950 alleviates cholestatic liver injury and fibrosis in mice. International Immunopharmacology, 70, 147–155. doi:10.1016/j.intimp.2019.02.016.
   PubMed Web of Science ®Google Scholar
• Rice, J. M. (2005). The carcinogenicity of acrylamide. Mutation Research, 580(1), 3–20. doi: 10.1016/j.mrgentox.2004.09.008
   PubMed Web of Science ®Google Scholar
• Ruenz, M., Bakuradze, T., Eisenbrand, G., & Richling, E. (2016). Monitoring urinary mercapturic acids as biomarkers of human dietary exposure to acrylamide in combination with acrylamide uptake assessment based on duplicate diets. Archives of Toxicology, 90(4), 873–881. doi:10.1007/s00204-015-1494-9.
   PubMed Web of Science ®Google Scholar
• Seydi, E., Rajabi, M., Salimi, A., & Pourahmad, J. (2015). Involvement of mitochondrial-mediated caspase-3 activation and lysosomal labilization in acrylamide-induced liver toxicity. Toxicological & Environmental Chemistry, 97(5), 563–575. doi:10.1080/02772248.2015.1047671.
   Web of Science ®Google Scholar
• Shi, A., Shi, H., Wang, Y., Liu, X., Cheng, Y., & Li, H. (2018). Activation of Nrf2 pathway and inhibition of NLRP3 inflammasome activation contribute to the protective effect of chlorogenic acid on acute liver injury. International Immunopharmacology, 54, 125–130. doi:10.1016/j.intimp.2017.11.007.
   PubMed Web of Science ®Google Scholar
• Smith, T. L., Slyke, P. V., Jones, N., Dumont, D. J., & McGlade, C. J. (2018). Tie2 signalling through Erk1/2 regulates TLR4 driven inflammation. Cellular Signalling, 51, 211–221. doi:10.1016/j.cellsig.2018.08.001.
   PubMed Web of Science ®Google Scholar
• Stadler, R. H., Blank, I., Varga, N., Robert, F., Hau, J., & Guy, P. A. (2002). Acrylamide from Maillard reaction products. Nature, 419, 449–450. doi:10.1038/419449a.
   PubMed Web of Science ®Google Scholar
• Stănculeţ, N., Grigoraş, A., Avădanei, R., Floarea, S. A., Amălinei, C., & Căruntu, I. D. (2013). Relationship between Kuppfer cells, inflammation, and fibrosis in chronic hepatitis B and C. Revista Medico-chirurgicala a Societatii de Medici si Naturalisti din Iasi, 117(4), 880–889.
   PubMedGoogle Scholar
• Tan, X. T., Zhao, T., Wang, Z. H., Wang, J., Wang, Y. J., & Liu, Z. G. (2018). Acrylamide defects the expression pattern of circadian clock and mitochondrial dynamics in C57BL/6J mice liver and HepG2 cells. Journal of Agricultural and Food Chemistry, 66, 10252–10266. doi:10.1021/acs.jafc.8b02473.
   PubMed Web of Science ®Google Scholar
• Tareke, E., Rydberg, P., Karlsson, P., Eriksson, S., & Törnqvist, M. (2002). Analysis of acrylamide, a carcinogen formed in heated foodstuffs. Journal of Agricultural and Food Chemistry, 50(17), 4998–5006. doi:10.1021/jf020302f.
   PubMed Web of Science ®Google Scholar
• Wang, W., Mao, S., Yu, H., Wu, H., Shan, X., & Zhang, X. (2019). Pinellia pedatisecta lectin exerts a proinflammatory activity correlated with ROS-MAPKs/NF-κB pathways and the NLRP3 inflammasome in RAW264.7 cells accompanied by cell pyroptosis. International Immunopharmacology, 66, 1–12. doi:10.1016/j.intimp.2018.11.002.
   PubMed Web of Science ®Google Scholar
• Wang, S. Y., Wang, W., Ma, W. W., Chen, J. S., Gao, R., & Pang, Q. S. (2015). Effect of Low concentration acrylamide on serum biochemical parameters of non-neurotoxicity in occupational population. Occup Health & Emerg Rescue, 33(2), 75–77.
   Google Scholar
• Watzek, N., Scherbl, D., Schug, M., Hengstler, J., Baum, M., & Habermeyer, M. (2013). Toxicokinetics of acrylamide in primary rat hepatocytes: Coupling to glutathione is faster than conversion to glycidamide. Archives of Toxicology, 87(8), 1545–1556. doi: 10.1007/s00204-013-1054-0
   PubMed Web of Science ®Google Scholar
• Wei, Q., Li, J., Li, X., Zhang, L., & Shi, F. (2014). Reproductive toxicity in acrylamide-treated female mice. Reproductive Toxicology, 46, 121–128. doi:10.1016/j.reprotox.2014.03.007.
   PubMed Web of Science ®Google Scholar
• WHO G, FAO R. (2002). Health implications of acrylamide in food. Report of a Joint FAO/WHO Consultation. Geneva World Health Organization.
   Google Scholar
• Yu, J. W., Farias, A., Hwang, I., Fernandes-Alnemri, T., & Alnemri, E. S. (2013). Ribotoxic stress through p38 mitogen-activated protein kinase activates in vitro the human pyrin inflammasome. Journal of Biological Chemistry, 288(16), 11378–11383. doi:10.1074/jbc.M112.448795.
   PubMed Web of Science ®Google Scholar
• Zeng, W. Q., Zhang, J. Q., Li, Y., Yang, K., Chen, Y. P., & Liu, Z. J. (2013). A new method to isolate and culture rat Kupffer cells. PLoS ONE, 8(8), e70832. doi:10.1371/journal.pone.0070832.
   PubMed Web of Science ®Google Scholar
• Zuckerman, J. A. (1995). IARC monographs on the evaluation of carcinogenic risks to humans. Journal of Clinical Pathology, 48(7), 691–691. doi: 10.1136/jcp.48.7.691-a
   Google Scholar