Disruptive environmental chemicals and cellular mechanisms that confer resistance to cell death

Carcinogenesis, 2015, Vol. 36, Supplement 1, S89–S110 doi:10.1093/carcin/bgv032 Review review Disruptive environmental chemicals and cellular mechanisms that confer resistance to cell death Department of Chemistry and Biochemistry, Yeungnam University, Gyeongsan 712-749, South Korea, 1Sultan Zainal Abidin University, Malaysia, 2Plant Biotechnologies Inc, St. Albert AB, Canada, 3Computer Science Department, Southern Illinois University, Carbondale, IL 62901, USA, 4Department of Urology, University of California Davis, Sacramento, CA 95817, USA, 5 Department of Pharmacology and Toxicology, University of Vienna, Austria, 6 University of Puerto Rico, Medical Sciences Campus, School of Public Health, Nutrition Program, San Juan Puerto Rico 00936-5067, USA, 7Department of Anatomy, College of Medicine, Yeungnam University, Daegu, 705-717, South Korea, 8School of Biomedical Science, The Chinese University Of Hong Kong, Hong Kong, China, 9Siriraj Center of Excellence for Stem Cell Research, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok 10700, Thailand, 10Department of Otolaryngology/Head and Neck Surgery, Head and Neck Cancer Research Division, Johns Hopkins University School of Medicine, Baltimore, MD 21231, USA, 11Department of Pharmaceutical Sciences, Mary Babb Randolph Cancer Center, West Virginia University, Morgantown, WV 26506, USA, 12Department of Molecular Medicine and Medical Biotechnology, Federico II University of Naples, 80131 Naples, Italy, 13Department of Molecular and Experimental Medicine, MEM 180, The Scripps Research Institute, La Jolla, CA 92037, USA, 14Department of Biology, Jackson State University, Jackson, MS 39217, USA, 15Department of Pathology, Kuwait University, Safat 13110, Kuwait, 16Department of Experimental and Clinical Medicine, University of Firenze, Firenze, 50134, Italy, 17 Department of Environmental and Radiological Health Sciences, Colorado state University/ Colorado School of Public Health, Fort Collins, CO 80523-1680, USA, 18Center for Environmental Carcinogenesis and Risk Assessment, Environmental Protection and Health Prevention Agency, Bologna, 40126, Italy, 19Faculty of Medicine and Health Sciences, Universiti Putra Malaysia, Serdang, Selangor 43400, Malaysia, 20Institute of Molecular Genetics, National Research Council, Pavia, 27100, Italy, 21Toxicology Research Division, Bureau of Chemical Safety Food Directorate, Health Products and Food Branch Health Canada, Ottawa, Ontario, K1A0K9, Canada, 22Urology Department, Kasr Al-Ainy School of Medicine, Cairo University, El Manial, Cairo, 12515, Egypt, 23Molecular Oncology Program, Lombardi Comprehensive Cancer Center, Georgetown University Medical Center, Washington DC, 20057, USA, 24Advenced Molecular Science Research Centre, King George’s Medical University, Lucknow, Uttar Pradesh, 226003, India, 25Mediterranean Institute of Oncology, Viagrande, 95029, Italy, 26Department of Internal Medicine, Korea Cancer Center Hospital, Seoul 139-706, South Korea, 27Environmental and Molecular Toxicology, Environmental Health Science Center, Oregon State University, Corvallis, OR 97331, USA and 28Getting to Know Cancer, Truro, Nova Scotia, Canada *To whom correspondence should be addressed. Tel: +82 53 810 3015; Fax: +82 53 810 4619; Email: Received: February 23, 2014; Revised: January 28, 2015; Accepted: February 3, 2015 © The Author 2015. Published by Oxford University Press. All rights reserved. For Permissions, please email: . S89 Kannan Badri Narayanan, Manaf Ali1, Barry J.Barclay2, Qiang (Shawn) Cheng3, Leandro D’Abronzo4, Rita Dornetshuber-Fleiss5, Paramita M.Ghosh4, Michael J.Gonzalez Guzman6, Tae-Jin Lee7, Po Sing Leung8, Lin Li8, Suidjit Luanpitpong9, Edward Ratovitski10, Yon Rojanasakul11, Maria Fiammetta Romano12, Simona Romano12, Ranjeet K.Sinha13, Clement Yedjou14, Fahd Al-Mulla15, Rabeah Al-Temaimi15, Amedeo Amedei16, Dustin G.Brown17, Elizabeth P.Ryan17, Anna Maria Colacci18, Roslida A.Hamid19, Chiara Mondello20, Jayadev Raju21, Hosni K.Salem22, Jordan Woodrick23, A.Ivana Scovassi20, Neetu Singh24, Monica Vaccari18, Rabindra Roy23, Stefano Forte25, Lorenzo Memeo25, Seo Yun Kim26, William H.Bisson27, Leroy Lowe28, Hyun Ho Park* S90 | Carcinogenesis, 2015, Vol. 36, Supplement 1 Abstract Cell death is a process of dying within biological cells that are ceasing to function. This process is essential in regulating organism development, tissue homeostasis, and to eliminate cells in the body that are irreparably damaged. In general, dysfunction in normal cellular death is tightly linked to cancer progression. Specifically, the up-regulation of prosurvival factors, including oncogenic factors and antiapoptotic signaling pathways, and the down-regulation of proapoptotic factors, including tumor suppressive factors, confers resistance to cell death in tumor cells, which supports the emergence of a fully immortalized cellular phenotype. This review considers the potential relevance of ubiquitous environmental chemical exposures that have been shown to disrupt key pathways and mechanisms associated with this sort of dysfunction. Specifically, bisphenol A, chlorothalonil, dibutyl phthalate, dichlorvos, lindane, linuron, methoxychlor and oxyfluorfen are discussed as prototypical chemical disruptors; as their effects relate to resistance to cell death, as constituents within environmental mixtures and as potential contributors to environmental carcinogenesis. Introduction AIF apoptosis-inducing factor APAF apoptosis-activating factor-1 BH BCL-2 homology BPA bisphenol A CAR constitutive androstane receptor CDK cyclin-dependent kinase CSCs cancer stem cells DBP dibutyl phthalate DD death domain DDT dichlorodiphenyltrichloroethane DEHP diethylhexyl phthalate DISC death-inducing signaling complex 4EBP1 4E binding protein 1 EGFR epidermal growth factor receptor; ERK extracellular signal-regulated kinase FADD Fas-associated death domain protein FLIP FADD-like apoptosis regulator GJIC gap junctional intracellular communication IAP inhibitor of apoptosis protein JNK C-Jun N-terminal kinase LH luteinizing hormone MDM2 murine double minute 2 mRNA messenger RNA mtDNA mitochondrial DNA mTOR mammalian target of rapamycin MXC methoxychlor NADPH nicotinamide adenine dinucleotide phosphate NF-κB nuclear factor-κB PI3K phosphoinositide 3-kinase; PIDD TP53-induced protein with death domain PP peroxisome proliferators PPAR-α peroxisome proliferator-activated receptor-α PTEN phosphatase and tensin homolog PXR pregnane X receptor RAIDD RIP-associated Ich-1/Ced-3-homologue protein with a death domain RB retinoblastoma RIP receptor-interacting protein ROS reactive oxygen species RTK receptor tyrosine kinase SMAC second mitochondrial activator of caspases TGF-β transforming growth factor-β tumor necrosis factor TNF TP tumor protein TRADD TNF receptor-1-associated death domain TRAIL TNF-related apoptosis apoptosis-inducing ligand receptor XIAP X-linked inhibitor of apoptosis protein Can (...truncated)