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Binitha, R. N.
- Impact of Sewage Effluents on Osmoregulation in a Freshwater Teleost, Anabas testudineus
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1 Department of Zoology, University College, Palayam, Trivandrum-695034, Kerala, IN
1 Department of Zoology, University College, Palayam, Trivandrum-695034, Kerala, IN
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Journal of Endocrinology and Reproduction, Vol 15, No 1&2 (2011), Pagination: 27-36Abstract
This study investigated the impact of sewage effluents of the polluted river, Parvathyputhenar in Trivandrum city, Kerala, India, on the activities of osmoregulatory enzymes such as Na+/K+ and Ca2+ ATPases, the concentration of sodium and potassium ion content in the gill and on the chloride cells (CCs) and pavement cells (PCs) that regulate ions transport in the gill epithelium of a freshwater fish. The results indicate a significant (P<0.05) decrease in the activity of branchial Na+/K+ ATPase and Ca2+ ATPase in the fish exposed to sewage effluents for 7, 14 and 28 days and the fish caught from the polluted river. When the fish caught from the polluted river were kept in normal pond water in the laboratory for 30, 60 and 90 days, the enzyme's activities were gradually increased and almost restored to the control level. Scanning electron microscopic analysis of gill epithelium showed noticeable changes in the surface area morphology of CCs and PCs in the fish exposed to sewage effluents. Exposure to the sewage effluents drastically altered the size and characteristic "finger print" pattern of PCs and also reduced number of CCs in the gill epithelium. As the ATPases play an important role in maintenance of functional integrity of gill epithelium it is suggested that measurement of the activities of ATPases may be used as a biomarker of exposure to sewage effluents. This work is highly pertinent in the context of increased level and effect of endocrine disrupting chemicals present in the aquatic systems, which are increasing day by day.Keywords
Sewage Effluents, Na+/K+ ATPase, Ca2+ ATPase, Chloride Cells, Pavement Cells.- Oxidative Stress Responses of a Freshwater Teleost, Anabas testudineus, to an Endocrine Disruptor, Bisphenol A
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1 Department of Zoology, University College, Thiruvananthapuram-695034, Kerala, IN
1 Department of Zoology, University College, Thiruvananthapuram-695034, Kerala, IN
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Journal of Endocrinology and Reproduction, Vol 19, No 1 (2015), Pagination: 7-19Abstract
Bisphenol-A (BPA), an industrial chemical used to manufacture polycarbonate plastic, is considered as a potent estrogenic endocrine disruptor. A majority of xenobiotics exert their toxic effect by causing generation of reactive oxygen species, leading to oxidative stress. Reports regarding oxidative stress responses to BPA in fish are scanty. From this viewpoint, in the present study, a freshwater fish, Anabas testudineus, was exposed to sub-lethal concentrations of BPA (2.5, 5.0,&7.5 mg/l), for different time periods (7, 15&30 days). Four major enzymes of the fish's antioxidant defense system viz., catalase (CAT), superoxide dismutase (SOD), glutathione peroxidase (Se-GPx), and glutathione-S-transferase (GST), and the non-enzymatic antioxidant glutathione (GSH) were chosen as biomarkers to examine the effects of BPA. The activities of SOD, GPx and GSH were elevated to significant levels, while CAT and GST activities were decreased significantly suggesting oxidative stress in BPAexposed fish. Reactive oxygen species are known to cause DNA fragmentation. Hence, DNA fragmentation assay was also done. The severity of DNA fragmentation in fish exposed to 7.5 mg/L BPA (30days) was remarkably increased (p<0.05 vs control) and this was revealed in gel electrophoresis analysis also. The results clearly show that BPA is a pollutant with oxidative potential, also with a potential for DNA fragmentation. The potential risks of this compound to nature and human populations are significant since the production of BPA related compounds is increasing dramatically each year.Keywords
Endocrine Disruptor, Oxidative Stress, DNA Fragmentation, BPA, Antioxidants.References
- Agergaard N, Jensen PT. (1982) Procedure for blood glutathione peroxidase determination in cattle and swine. Acta Vet Scand. 23: 515-27.
- Ahmad I, Oliveira M, Pacheco M, Santos MA. (2005) Anguilla anguilla L. oxidative stress biomarkers responses to copper exposure with or without β-naphthoflavone pre-exposure. Chemosphere 61: 267-75.
- Almeida EA, Dainy ACD, Gomes OF, Medeiros MHG, Mascio PD. (2005) Oxidative stress in digestive gland and gill of the mussel (Perna perna) exposed to air and re-submerged. J Exp Mar Biol Ecol. 318: 1-30.
- Amrutha BV, Soorya SR, Aruna Devi C, Gireesh Kumar G, Jeyalekshmi G, Francis S. (2014) Aroclor-1254 induced oxidative stress respones in a freshwater fish Anabas testudineus (Bloch). J Aquat Biol Fisheries 2: 42-51.
- Ansaldo M, Luquet CM, Evelson PA, Polo JM, Llesuy S. (2000) Antioxidant levels from different Antarctic fish caught around South Georgia Island and Shag rocks. Polar Biol. 23: 160-5.
- Ates B, Orun I, Talas ZS, Durmaz G, Yilmaz I. (2008) Effects of sodium selenite on some biochemical parameters of rainbow trout (Oncorhynchus mykiss) exposed to Pb2+ and Cu2+. Fish Physiol Biochem. 34: 53-9.
- Athanasios V, Thomais V, Manos D, Michael S. (2006) Molecular biomarkers of oxidative stress in aquatic organisms in relation to toxic environmental pollutants. Ecotoxicol Environ Saf. 64: 178-9.
- Atli G, Alptekin O, Tukel S, Canli M. (2006) Response of catalase activity to Ag+, Cd+, Cr2+, Cu2- and Zn2+ in five tissues of freshwater fish Oreochromis niloticus. Comp Biochem Physiol. C. Pharmacol Toxicol. 143: 218-224.
- Avci A, Kacmaz M, Durak I. (2005) Peroxidation in muscle and liver tissues from fish in a contaminated river due to a petroleum refinery industry. Ecotoxicol Environ Saf. 6: 101-5.
- Barata C, Varo I, Navarro JC, Arun S, Porte C. (2005) Antioxidant enzyme activities and lipid peroxidation in the freshwater cladoceran Daphnia magna exposed to redox cycling compounds. Comp Biochem Physiol. C. Toxicol Pharmacol. 140: 175-86.
- Benke GM, Cheevar KC. (1974) The comparative toxicity, acetylcholinesterase action and metabolism of methyl parathion and parathion in sunfish and mice. Toxicol Appl Pharmacol. 28: 97-109.
- Bindhumol V, Chitra KC, Mathur PP. (2003) Bisphenol-A induces reactive oxygen species generation in the liver of male rats. Toxicology 188: 117-24.
- Biswas S, Chida AS, Rahman I. (2006) Redox modifications of protein-thiols: emerging role in cell signalling. Biochem Pharmacol. 71: 551-64.
- Black MC, Ferrell JR, Horning RC, Martin LK. (1996) DNA strand breakage in freshwater mussels (Anodonta grandis) exposed to lead in the laboratory and field. Environ Toxicol Chem. 15: 802-8.
- Bradford MM. (1976) Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 72: 248-54.
- Burridge, E. (2003) Bisphenol A: Product profile. Eur Chem News. 14-20, 17.
- Chaudhry AS, Jabeen F. (2010) Assessing metal, protein, and DNA profiles in Labeo rohita from the Indus River in Mianwali, Pakistan. Environ Monit Assess 51: 121-35.
- Cheek AO, Brouwer TH, Carroll S, Manning S, Mclachlan JA, Brouwer M. (2001) Experimental evaluation of vitellogenin as a predictive biomarker for reproductive disruption. Environ Health Perspect. 109: 681-90.
- Connell D, Lam P, Richardson B, Wu R. (1999) Introduction to Ecotoxicology. Oxford: Blackwell. 135.
- Di Giulio RT, Hinton DE. (2008) Reactive oxygen species and oxidative stress. In: Di Giulio RT, Hinton DE (eds) The Toxicology of Fishes. New York: CRC Press, Taylor & Francis. Ch. 6.
- Ding F, Song WH, Guo J, Gao ML, Hu WX. (2009) Oxidative stress and structure-activity relationship in the zebrafish (Danio rerio) under exposure to paclobutrazol. J Environ Sci Health 44: 44-50.
- Doherty VF, Ogunkuade OO, Kanife JC. (2010) Biomarkers of oxidative stress and heavy metal levels as indicators of environmental pollution in some selected fishes in Lagos, Nigeria. American-Eurasian J Agric Environ Sci. 7: 359-65.
- Donnelly ET, McClure N, Lewis SE. (1999) The effect of ascorbate and alphatocopherol supplementation in vitro on DNA integrity and hydrogen peroxide-induced DNA damage in human spermatozoa. Mutagenesis 14: 505-12.
- Duncan DB. (1955) Multiple range and multiple F- test. Biometrics 11: 1-42.
- Farombi EO, Ajimoko YR, Adelowo OA. (2007) Biomarkers of oxidative stress and heavy metals as indicators of environmental pollution in African catfish (Clarias gariepinus) from Nigeria Ogun River. Int J Environ Res Pub Health 4: 158-65.
- Farombi EO, Ajimoko YR, Adelowo OA. (2008) Effect of butachlor on antioxidant enzyme status and lipid peroxidation in freshwater African catfish (Clarias gariepinus). Int J Environ Res Pub Health. 5: 423-427.
- Focazio MJ, Kolpin DW, Barnes KK, Furlong ET, Meyer MT, Zaugg SD, Barber LB, Thurman ME. (2008) A national reconnaissance for pharmaceuticals and other organic wastewater contaminants in the United States–II untreated drinking water sources. Sci Total Environ. 402: 201-16.
- Frasco MF, Guilhermino L. (2002) Effects of dimethoate and beta-naphthoflavone on selected biomarkers of Poecilia reticulata. Fish Physiol Biochem. 26: 149-56.
- Gul S, Belge-Kurutas E, Yildiz E, Sahan A, Doran F. (2004) Pollution correlated modifications of liver antioxidant systems and histopathology of fish (Cyprinidae) living in Seyhan Dam Lake, Turkey. Environ Int.. 30: 605-9.
- Habig WH, Pabst MJ, Jakoby WB. (1974) Glutathione-S-transferases: The first enzymatic step in mercapturic acid formation. J Biol Chem. 249: 7130–9.
- Hansen BH, Romma S, Softeland LIR, Olsvik PA, Andersen RA. (2006) Induction and activity of oxidative stress-related proteins during water-borne Cu-exposure in brown trout (Salmo trutta). Chemosphere 65: 1704-14.
- Hasselberg L, Meier S, Svardal A. (2004a) Effects of alkylphenols on redox status in first spawning Atlantic cod (Gadus morhua). Aquat Toxicol. 69: 95-105.
- Hasselberg L, Meier S, Svardal A, Hegelund T, Celander MC. (2004b). Effects of alkylphenols on CYP1A and CYP3A expression in first spawning Atlantic cod (Gadus morhua). Aquat Toxicol. 67: 303-13.
- Hoff PT, Van Dongen W, Esmans EL, Blust R, De Coen WM. (2003) Evaluation of the toxicological effects of perflurooctane sulfonic acid in the common carp (Cyprinus carpio). Aquat Toxicol. 62: 349-59.
- Howdeshell KL, Peterman PH, Judy BM, Taylor JA, Orazio CE, Ruhlen RL. (2003) Bisphenol A is released from used polycarbonate animal cages into water at room temperature. Environ Health Perspect. 111: 1180-7.
- Hughes EM, Gallagher EP. (2004) Effects of 17-[beta] estradiol and 4- nonylphenol on phase II electrophilic detoxification pathways in largemouth bass (Micropterus salmoides) liver. Comp Biochem Physiol. 137: 237-47.
- Iwasa M, Maeno Y, Inoue H, Koyama H, Matoba R. (1996) Induction of apoptotic cell death in rat thymus and spleen after a bolus injection of methamphetamine. Int J Leg Med. 109: 23-8.
- Kadar E, Costa V, Santos RS. (2005) Distribution of microessential (Fe, Cu, Zn) and toxic (Hg) metals in tissues of two nutritionally distinct hydrothermal shrimps. Sci Total Environ. 71: 65-70.
- Kakkar P, Das B, Viswanathan PN. (1984) A modified spectroscopic assay of superoxide dismutase. Indian Biochem Biophys. 21: 130-2.
- Kamunde C, Clayton C, Wood C. (2002) Waterborne versus dietary copper uptake in rainbow trout and the effects of previous waterborne copper exposure. Am J Physiol Regul. Integr Comp Physiol. 283: 69-78.
- Kang JH, Kondo F. (2002) Determination of bisphenol A in canned pet foods. Res Vet Sci. 73: 177-82.
- Krea S, Zaja R, Calic V, Terzic S, Grubesic MS, Ahel N. (2007) Hepatic biomarker response to organic contamination in feral chub (Letrciscus cephalus) – Laboratory characterisation and field study in the Sava River, Croatia. Environ Toxicol Chem. 26: 2620-33.
- Lawrence RA, Burck RA. (1976) Glutathione peroxidase activity in selenium-deficient rat liver. Biochem Biophys Res Commun. 71: 952-58.
- Letcher RJ, Sanderson JT, Bokkers A, Giesy JP, van den Berg M. (2005) Effects of bisphenol A-related diphenolalkanes on vitellogenin production in male carp (Cyprinus carpio) hepatocytes and aromatase (CYP19) activity in human H295R adrenocortical carcinoma cells. Toxicol Appl Pharmacol. 209: 95-104.
- Levy G, Lutz I, Kruger A, Kloas W. (2004) Bisphenol A induces feminization in Xenopus laevis tadpoles. Environ Res. 94: 102-11.
- Lide DR. (2004) CRC Handbook of Chemistry and Physics, 85th ed. New York: CRC Press.
- Livingstone D. (2001) Contaminant-stimulated reactive oxygen species production and oxidative damage in aquatic organisms. Marine Pollut Bull. 42: 656-66.
- Lushchak VI, Bagnyukova TV. (2006) Effects of different environmental oxygen level on free radical processes in fish. Comp Biochem Physiol. 144: 283-9.
- Maehly AC, Chance B. (1954) The assay of catalase and peroxide. In: Glick D (ed) Methods of Biochemical Analysis I. Interscience: New York. 1: 357.
- Mendum T, Stole E, Van Benschoten H, Warner JC. (2010) Concentration of bisphenol A in thermal paper. Green Chem Lett Rev. 4: 81-6.
- Metwally MAA, Fouad IM. (2008) Biochemical changes induced by heavy metal pollution in marine fishes at Khomse Coast, Libya. Global Veterinaria. 2: 308-11.
- Oehlmann J, Schulte-Oehlmann U, Bachmann J, Oetken M, Lutz I, Kloas W. (2006) Bisphenol A induces superfeminization in the ramshorn snail Marisa cornuarietis (Gastropoda: Prosobranchia) at environmentally relevant concentrations. Environ Health Perspect. 114: 127-33.
- Orbea A, Fahimi H, Cajaraville M. (2000) Immunolocalization of four antioxidant enzymes in digestive glands of mollusks and crustaceans and fish liver. Histochem Cell Biol. 114: 393-404.
- Orun I, Ates, B, Selamoglu Z, Yazlak H, Ozturk E, Yilmaz I., (2005) Effects of various sodium selenite concentrations on some biochemical and hematological parameters of rainbow trout (Oncorhynchus mykiss). Environ Bull. 14: 18-22.
- Pandey S, Ahmad I, Parvez S, Bin-Hafeez B, Haque R, Raisuddin S. (2001) Effect of endosulfan on antioxidants of freshwater fish Channa punctatus Bloch: Protection against lipid peroxidation by copper pre-exposure. Arch Environ Contam Toxicol. 41: 345-52.
- Papagiannis I, Kagalou I, Leonardos J, Petridis D, Kalfakakou V. (2004) Copper and zinc in four freshwater fish species from Lake Pamvotis, Greece. Environ Int. 30: 357-62.
- Pavlica M, Klobucas GIV, Mojas N, Erben R, Papes, D. (2001) Detection of DNA damage in haemocytes of Zebra mussel using comet assay. Mut Res. 490: 209-14.
- Potts RJ, Notarianni LJ, Jefferies TM. (2000) Seminal plasma reduces exogenous oxidative damage to human sperm, determined by the measurement of DNA strand breaks and lipid peroxidation. Mut Res. 447: 249-56.
- Rashid H, Ahmad F, Rahman S, Ansari RA, Bhatia K, Kaur M, Islam F, Raisuddin S. (2009) Iron deficiency augments bisphenol A-induced oxidative stress in rats. Toxicol. 256: 7-12.
- Sagara Y, Dargusch R, Chambers D, Davis J, Schubert D, Maher P. (1998) Cellular mechanisms of resistance to chronic oxidative stress. Free Rad Biol Med. 24: 1375–89.
- Sanchez W, Pallulel O, Meunier L, Coquery M, Porcher JM, Ait-Aissa S. (2005) Copper-induced oxidative stress in three-spined stickleback: relationship with hepatic metal levels. Environ Toxicol Pharmacol. 19: 177-83.
- Sies H. (1999) Gluthatione and its role in cellular functions. Free Rad Biol Med. 27: 916-22.
- Soorya SR, Aruna Devi C, Binitha RN, Amrutha BV, Jeyalekshmi G, Francis S. (2012) Oxidative stress experienced by freshwater fish Anabas testudineus exposed to sewage effluents of Parvathyputhenar, Kerala. In: Biju Kumar A (ed) Biodiversity Utilization and Threats. New Delhi, India: Narendra Publishing House. pp 769-80.
- Stanic B, Andric N, Zoric S, Grubor-Lajsic G, Kovacevic R. (2006) Assessing pollution in the Danube River near Novi Sad (Serbia) using several biomarkers in starlet (Acipenser ruthenus L.). Ecotoxicol Environ Saf. 65: 395-402.
- Steinert SA. (1999) DNA damage as a bivalve biomarker. Biomarkers 4: 492-6.
- Suzuki T, Nakagawa Y, Takano I, Yaguchi K, Yasuda K. (2004) Environmental fate of bisphenol A and its biological metabolites in river water and their xeno-estrogenic activity. Environ Sci Technol. 38: 2389-96.
- Tjalkens RB, Valeriojr IG, Awasthi YC, Petersen DR. (1998) Association of GST induction and lipid peroxides in two inbred strains of mice subjected to chronic iron overload. Toxicol App Pharmacol. 151: 174-81.
- Twigg J, Fulton N, Gomez E, Irvine DS, Aitken RJ. (1998) Analysis of the impact of intracellular reactive oxygen species generation on the structural and functional integrity of human spermatozoa: lipid peroxidation, DNA fragmentation and effectiveness of antioxidants. Human Reprod. 13: 1429-36.
- Uguz C, Iscan M, Erguven A, Isgor B, Togan I. (2003) The bioaccumulation of nonylphenol and its adverse effect on the liver of rainbow trout (Onchorynchus mykiss). Environ Res. 92: 262-70.
- Wolozin B, Iwasaki K, Vito P, Ganjei JK, Lacana E, Sunderland T. (1996) Participation of presenilin 2 in apoptosis: enhanced basal activity conferred by an Alzheimer mutation. Sci. 89: 433-38.
- Yilmaz HR, Turkoz Y, Yukse, E, Orun I. (2006) An investigation of antioxidant enzymes activities in liver of Cyprinus carpio taken from different stations in the Karakaya Dam Lake. Int J Sci Tech. 1: 1-6.
- Role of Steroid Hormones on NA+-K+ Atpase Activity and Expression of ER and PR in the Brain of Oreochromis mossambicus
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1 Department of Zoology, University College, Palayam, Trivandrum 695 034, IN
2 Department of Zoology, University of Kerala, Kariavottom, Trivandrum 695 581, IN
1 Department of Zoology, University College, Palayam, Trivandrum 695 034, IN
2 Department of Zoology, University of Kerala, Kariavottom, Trivandrum 695 581, IN
Source
Journal of Endocrinology and Reproduction, Vol 7, No 1&2 (2003), Pagination: 41-42Abstract
Over the past decade, it has become evident that the brain is a steroidogenic organ. The actions of hormones in the brain play important roles during early development and in the process of sexual differentiation. The effects of steroid hormones on dendritic morphology, synaptic function and ionic conductance have been implicated in the regulation of behaviour in both vertebrates and invertebrates.- Homology in the Binding Patterns of Human and Rat Androgen Receptors with various Ligands
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1 Department of Zoology, Sacred Heart College (Autonomous), Thevara - 682013, Kochi, Kerala, IN
2 Department of Zoology, Mar Athanasius College (Autonomous), Kothamangalam - 686666, Kerala, IN
3 Department of Zoology, Marian College of Arts and Science, Kazhakuttom, Trivandrum - 695582, Kerala, IN
1 Department of Zoology, Sacred Heart College (Autonomous), Thevara - 682013, Kochi, Kerala, IN
2 Department of Zoology, Mar Athanasius College (Autonomous), Kothamangalam - 686666, Kerala, IN
3 Department of Zoology, Marian College of Arts and Science, Kazhakuttom, Trivandrum - 695582, Kerala, IN
Source
Journal of Endocrinology and Reproduction, Vol 26, No 1 (2022), Pagination: 35-44Abstract
Scientists routinely use in-vivo animal experiments to study the reproductive and endocrine effects of various chemicals in humans. Rats are being used as the most suitable animal model for such investigations. Use of animal models to envisage the mode of action of a particular chemical in humans is questionable unless we can explain the binding similarities. In this study, an in-silico docking was employed to visualise if androgens and their agonists bind with androgen receptors of humans and rats in a similar pattern using BIOVIA Discovery Studio 2018. Amino acid residues involved in bond formation, nature of bonding, LibDock score and bond distances were calculated to compare the binding affinities. It was found that ASN 705, GLN 711, ARG 752 and THR 877 were the major amino acid residues in hydrogen bonding of selected ligands with both human and rat androgen receptors. Thus, the present study answers numerous questions that may arise while selecting rats as laboratory animal models to validate the androgenic effects of chemicals in humans.Keywords
Androgen Agonist, Androgen Receptors, Biovia Discovery Studio, In-Silico Docking, Laboratory Animal ModelsReferences
- Li J, Al-Azzawi F. Mechanism of androgen receptor action. Maturitas. 2009; 63(2):142-8. https://doi.org/10.1016/j.maturitas.2009.03.008. PMid:19372015.
- Gao W, Bohl CE, Dalton JT. Chemistry and Structural Biology of Androgen Receptor. Chem Rev. 2005; 105(1):3352-70. https://doi.org/10.1021/cr020456u. PMid:16159155 PMCid:PMC2096617.
- Christiansen AR, Lipshultz LI, Hotaling JM, Pastuszak AW. Selective androgen receptor modulators: The future of androgen therapy? Transl Androl Urol. 2020; 9(Suppl 2):S135-48. https://doi.org/10.21037/tau.2019.11.02. PMid:32257854 PMCid:PMC7108998.
- Zhi L, Martinborough E. Chapter 17. Selective androgen receptor modulators (SARMs). Annu Rep Med Chem. 2001; 36(10):169-80. https://doi.org/10.1016/S0065-7743(01)36057-8.
- Choi SM, Lee B. Comparative safety evaluation of selective androgen receptor modulators and anabolic androgenic steroids. Expert Opin Drug Saf. 2015; 14(11):1773-85. https://doi.org/10.1517/14740338.2015.1094052. PMid:26401842.
- Pop A, Drugan T, Gutleb AC, et al. Estrogenic and anti‐estrogenic activity of butylparaben, butyl-ated hydroxyanisole, butylated hydroxytoluene and propyl gal-late and their binary mixtures on two estrogen responsive cell lines (T47D-Kbluc, MCF-7). J Appl Toxicol. 2018; 38(7):944-57. https://doi.org/10.1002/jat.3601. PMid:29460325.
- Pop A, Drugan T, Gutleb AC, et al. Individual and combined in vitro (anti)androgenic effects of certain food additives and cosmetic preservatives. Toxicol In Vitro. 2016; 32:269-77. https://doi.org/10.1016/j.tiv.2016.01.012. PMid:26812027.
- Hwan GK, Jeong SH, Joon HC, et al, Evaluation of estrogenic and androgenic activity of butylated hydroxyanisole in immature female and castrated rats. Toxicology. 2005; 213(1-2):147-56. https://doi.org/10.1016/j.tox.2005.05.027. PMid:16023279.
- Lynch C, Sakamuru S, Huang R, et al. Identifying environmental chemicals as agonists of the androgen receptor by using a quantitative high-throughput screening platform. Toxicology. 2017; 385:48-58. https://doi.org/10.1016/j.tox.2017.05.001. PMid:28478275 PMCid: PMC6135100.
- Schrader TJ, Cooke GM. Examination of selected food additives and organochlorine food contaminants for androgenic activity in vitro. Toxicol Sci. 2000; 53(2):278-88. https://doi.org/10.1093/toxsci/53.2.278. PMid:10696776.
- Orton F, Ermler S, Kugathas S, et al. Mixture effects at very low doses with combinations of anti-androgenic pesticides, antioxidants, industrial pollutant and chemicals used in personal care products. Toxicol Appl Pharmacol. 2014; 278(3):201-8. https://doi.org/10.1016/j.taap.2013.09.008. PMid:24055644.
- Parks LG, Lambright CS, Orlando EF, et al. Masculinization of female mosquitofish in kraft mill effluent- contaminated Fenholloway River water is associated with androgen receptor agonist activity. Toxicol Sci. 2001; 267(62):257-67. https://doi.org/10.1093/toxsci/62.2.257. PMid:11452138.
- OECD. OECD Series on Testing and Assessment. OECD Publishing. 2018. https://doi.org/10.1787/9789264304796- en.
- Owens JW, Gray LE, Zeiger E, et al. The OECD Program to Validate the Rat Hershberger Bioassay to Screen Compounds for in Vivo Androgen and Antiandrogen Responses: Phase 2 Dose-Response Studies. Environ Health Perspect. 2007; 115(5):671-8. https://doi.org/10.1289/ehp.9666.PMid:17520051 PMCid:PMC1867976.
- Freyberger A, Ahr HJ. Development and standardization of a simple binding assay for the detection of compounds with affinity for the androgen receptor. Toxicology. 2004; 195(2-3):113-26. https://doi.org/10.1016/j.tox.2003.09.008. PMid:14751668.
- Yamasaki K, Sawaki M, Noda S, et al. Comparison of the Hershberger assay and androgen receptor binding assay of twelve chemicals. Toxicology. 2004; 195(2-3):177-86. https://doi.org/10.1016/j.tox.2003.09.012. PMid:14751673.
- Mansouri K, Kleinstreuer N, Abdelaziz AM, et al. CoMPARA: Collaborative modeling project for androgen receptor activity. Environ Health Perspect. 2020; 128(2):27002. https://doi.org/10.1289/EHP5580. PMid:32074470 PMCid:PMC7064318.
- Kleinstreuer NC, Ceger P, Watt ED, et al. Development and Validation of a Computational Model for Androgen Receptor Activity. Chem Res Toxicol. 2017; 30(4):946-64. https://doi.org/10.1021/acs.chemrestox.6b00347. PMid:27933809 PMCid:PMC5396026.
- Maria Maddalena Calabretta, Antonia Lopreside Laura Montali LC, Roda A, Michelini and E. A Genetically Encoded Bioluminescence Intracellular Nanosensor for Androgen Receptor Activation Monitoring in 3D cell Models. Sensors (Basel). 2021; 21(3):893. https://doi.org/10.3390/s21030893. PMid:33572727 PMCid:PMC7865915.
- Kiani NA, Shang MM, Zenil H, Tegner J. Predictive systems toxicology. Methods Mol Biol. 2018; 1800:535-57. https://doi.org/10.1007/978-1-4939-7899-1_25. PMid:29934910.
- Yu M, Lee J, Lee Y, Na D. 2-D chemical structure image-based in silico model to predict agonist activity for androgen receptor. BMC Bioinformatics. 2020; 21(Suppl 5):1-8. https://doi.org/10.1186/s12859-020-03588-1. PMid: 33106158 PMCid:PMC7586653.
- Lubahn DB, Joseph DR, Sar M, et al. The human androgen receptor: Complementary deoxyribonucleic acid cloning, sequence analysis and gene expression in prostate. Mol Endocrinol. 1988; 2(12):1265-75. https://doi.org/10.1210/mend-2-12-1265. PMid:3216866.
- Yang L, Li W, Zhao Y, Zhong S, et al. Computational Study of Novel Natural Inhibitors Targeting O6-Methylguanine-DNA Methyltransferase. World Neurosurg. 2019; 130:e294-e306. https://doi.org/10.1016/j.wneu.2019.05.264. PMid:31203065.
- Habib H, Haider MR, Sharma S, et al. Molecular interactions of vinclozolin metabolites with human estrogen receptors 1GWR-α and 1QKM and androgen receptor 2AM9-β: Implication for endocrine disruption. Toxicol Mech Methods. 2020; 30(5):370-07. https://doi.org/10.1080/15376516.2020.1747123. PMid:32208804.
- Sack JS, Kish KF, Wang C, et al. Crystallographic structures of the ligand-binding domains of the androgen receptor and its T877A mutant complexed with the natural agonist dihydrotestosterone. Proc Natl Acad Sci USA. 2001; 98(9):4904-09. https://doi.org/10.1073/pnas.081565498. PMid:11320241 PMCid:PMC33136.
- Farla P, Hersmus R, Geverts B, et al. The androgen receptor ligand-binding domain stabilizes DNA binding in living cells. J Struct Biol. 2004; 147(1):50-61. https://doi.org/10.1016/j.jsb.2004.01.002. PMid:15109605.
- Schauwaers K, De Gendt K, Saunders PTK, et al. Loss of androgen receptor binding to selective androgen response elements causes a reproductive phenotype in a knockin mouse model. Proc Natl Acad Sci USA. 2007; 104(12):4961-6. https://doi.org/10.1073/pnas.0610814104. PMid:17360365 PMCid:PMC1829247.
- Claessens F, Verrijdt G, Schoenmakers E, et al. Selective DNA binding by the androgen receptor as a mechanism for hormone-specific gene regulation. J Steroid Biochem Mol Biol. 2001; 76(1-5):2330. https://doi.org/10.1016/S0960-0760(00)00154-0.
- Marhefka CA, Moore BM, Bishop TC, et al. Homology modeling using multiple molecular dynamics simulations and docking studies of the human androgen receptor ligand binding domain bound to testosterone and nonsteroidal ligands. J Med Chem. 2001; 44(11):1729-40. https://doi.org/10.1021/jm0005353. PMid:11356108.
- Matias PM, Donner P, Coelho R, et al. Structural evidence for ligand specificity in the binding domain of the human androgen receptor: Implications for pathogenic gene mutations. J Biol Chem. 2000; 275(34):26164-71. https://doi.org/10.1074/jbc.M004571200. PMid:10840043.
- Weikum ER, Liu X, Ortlund EA. The nuclear receptor superfamily: A structural perspective. Protein Sci. 2018; 27(11):1876-92. https://doi.org/10.1002/pro.3496. PMid:30109749 PMCid:PMC6201731.
- Zhou W, Duan M, Fu W, et al. Discovery of novel androgen receptor ligands by structure-based virtual screening and bioassays. Genomics, Proteomics and Bioinformatics. The Authors; 2018; 16(6):416-427. https://doi.org/10.1016/j.gpb.2018.03.007. PMid:30639122 PMCid:PMC6411960.
- Sakkiah S, Kusko R, Pan B, et al. Structural changes due to antagonist binding in ligand binding pocket of androgen receptor elucidated through molecular dynamics simulations. Front Pharmacol. 2018; 9:492. https://doi.org/10.3389/fphar.2018.00492. PMid:29867496 PMCid:PMC5962723.