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Journal articles on the topic 'Vitellogenin induction'

Author: Grafiati

Published: 4 June 2021

Last updated: 4 February 2022

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1

Olsson, P. E., P. Kling, C. Petterson, and C. Silversand. "Interaction of cadmium and oestradiol-17β on metallothionein and vitellogenin synthesis in rainbow trout (Oncorhynchus mykiss)." Biochemical Journal 307, no. 1 (April 1, 1995): 197–203. http://dx.doi.org/10.1042/bj3070197.

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The induction of metallothionein and vitellogenin synthesis in rainbow trout liver was studied after injection of oestradiol-17 beta alone or in combination with cadmium or zinc. Intraperitoneal injection of oestradiol-17 beta increased the liver somatic index, with subsequent induction of vitellogenin synthesis. Oestradiol-17 beta did not induce metallothionein synthesis. Injection of cadmium induced the synthesis of metallothionein mRNA and metallothionein. Injection of oestradiol-17 beta in combination with cadmium resulted in inhibition of transcription and translation of both vitellogenin and metallothionein. Chromatography of liver cytosols revealed that cadmium, when co-injected with oestradiol-17 beta, did not bind to metallothionein but would initially bind to high-molecular-mass (HMr) cytosolic proteins. In fish injected with cadmium in combination with oestradiol-17 beta, cadmium was gradually redistributed from HMr proteins to metallothionein. This resulted in induction of metallothionein synthesis and in binding of most of the cadmium to metallothionein. Induction of vitellogenin mRNA was observed 15 days after injection, as cadmium was being redistributed to newly synthesized metallothionein. These findings indicate that cadmium inhibits the transcription of vitellogenin. The binding of cadmium to these non-metallothionein proteins represses the induction of metallothionein and results in increased toxicity of the metal. Preinduction of metallothionein by zinc injections resulted in decreased cadmium sensitivity of the fish and a decrease in the repression of vitellogenin mRNA. Furthermore, a role for metallothionein in the detoxification of cadmium is indicated by the induction of vitellogenin synthesis that occurs once metallothionein has begun sequestering cadmium.

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2

Jurčíková, J., P. Mikula, R. Dobšíková, D. Némethová, and Z. Svobodová. "Effects of Metazachlor on Vitellogenin Induction in Zebrafish (Danio rerio)." Acta Veterinaria Brno 76, no. 8 (2007): S61—S66. http://dx.doi.org/10.2754/avb200776s8s061.

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The influence of metazachlor on vitellogenesis in juvenile (20 days old) zebrafish (Danio rerio) was investigated after ambient water exposure to concentrations of 0.1, 1.0 and 5.0 mg l-1 of the chloroacetanilide herbicide Butisan 400 SC containing approximately 35.6% (w/w) metazachlor. After 20 days of exposure, vitellogenin concentrations in whole-body homogenates of the fish were measured by direct sandwich ELISA. The results were compared to vitellogenin concentrations in fish from both negative (no exposure) and positive (exposed to natural oestrogen 17β-oestradiol) control groups. Exposure to Butisan 400 SC at a concentration of 5.0 mg l-1 induced vitellogenin synthesis significantly compared to the control fish (p < 0.05). The oestrogenic effect of 17β-oestradiol was confirmed.

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3

Wang, Zhenyu, Meng Sun, Hua Tian, Su Gao, Wei Wang, and Shaoguo Ru. "Estrogenic effects of monocrotophos standard on male goldfish, Carassius auratus: induction of vitellogenin synthesis and alteration of testicular ultrastructure and function." Animal Biology 64, no. 4 (2014): 311–31. http://dx.doi.org/10.1163/15707563-00002448.

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Monocrotophos has been shown to exert estrogenic effects on teleosts. However, it has not been determined whether monocrotophos itself is the component that is responsible for exerting these estrogenic activities. Therefore, this study was carried out to investigate the estrogenic effects of monocrotophos standard in male goldfish (Carassius auratus), after a 21-day semi-static toxicity test. The induction of vitellogenin synthesis in males exposed to monocrotophos was confirmed with qualitative and quantitative methods. The observed increase in endogenous estrogen levels in males exposed to monocrotophos might explain the induction of vitellogenin. Moreover, we observed a decreased gonadosomatic index, ultrastructure damage of sperm and Sertoli cells, and several alterative testicular enzyme activities in males exposed to monocrotophos, which possibly affect spermatogenesis and male fertility. Our study showed the potential estrogenic effects of monocrotophos standard may act via the induction of vitellogenin synthesis and alteration of testicular ultrastructure and function in male goldfish.

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4

Dodson, R. E., and D. J. Shapiro. "An estrogen-inducible protein binds specifically to a sequence in the 3' untranslated region of estrogen-stabilized vitellogenin mRNA." Molecular and Cellular Biology 14, no. 5 (May 1994): 3130–38. http://dx.doi.org/10.1128/mcb.14.5.3130.

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The 3' untranslated region (3'-UTR) has been implicated in the estrogen stabilization of hepatic Xenopus laevis vitellogenin mRNA. We used RNA gel mobility shift assays to demonstrate that Xenopus liver contains a factor which binds with very high specificity to a segment of the 3'-UTR of vitellogenin B1 and B2 mRNAs. We detected a single high-affinity binding site in the vitellogenin mRNA 3'-UTR and localized the binding site to a 27-nucleotide region. Since binding was abolished by proteinase K digestion, at least a component of the factor is a protein. Following estrogen administration, binding was induced approximately four- to fivefold in extracts from liver polysomes. The hepatic vitellogenin mRNA-binding protein was found in both polysomes and cytosol. Since the protein was also estrogen inducible in cytosol, this represents a genuine induction, not simply recruitment of the cytosolic protein into polysomes. UV cross-linking studies with the 27-nucleotide recognition sequence revealed bands corresponding to bound proteins with apparent molecular weights of 71,000 and 141,000. This appears to be the first example of steroid hormone-inducible proteins binding to an mRNA 3'-UTR. Its induction by estrogen and its sequence-specific binding to a region of vitellogenin mRNA important in estrogen-mediated stabilization suggest that the protein may play a role in the regulation of mRNA stability.

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5

Dodson, R. E., and D. J. Shapiro. "An estrogen-inducible protein binds specifically to a sequence in the 3' untranslated region of estrogen-stabilized vitellogenin mRNA." Molecular and Cellular Biology 14, no. 5 (May 1994): 3130–38. http://dx.doi.org/10.1128/mcb.14.5.3130-3138.1994.

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The 3' untranslated region (3'-UTR) has been implicated in the estrogen stabilization of hepatic Xenopus laevis vitellogenin mRNA. We used RNA gel mobility shift assays to demonstrate that Xenopus liver contains a factor which binds with very high specificity to a segment of the 3'-UTR of vitellogenin B1 and B2 mRNAs. We detected a single high-affinity binding site in the vitellogenin mRNA 3'-UTR and localized the binding site to a 27-nucleotide region. Since binding was abolished by proteinase K digestion, at least a component of the factor is a protein. Following estrogen administration, binding was induced approximately four- to fivefold in extracts from liver polysomes. The hepatic vitellogenin mRNA-binding protein was found in both polysomes and cytosol. Since the protein was also estrogen inducible in cytosol, this represents a genuine induction, not simply recruitment of the cytosolic protein into polysomes. UV cross-linking studies with the 27-nucleotide recognition sequence revealed bands corresponding to bound proteins with apparent molecular weights of 71,000 and 141,000. This appears to be the first example of steroid hormone-inducible proteins binding to an mRNA 3'-UTR. Its induction by estrogen and its sequence-specific binding to a region of vitellogenin mRNA important in estrogen-mediated stabilization suggest that the protein may play a role in the regulation of mRNA stability.

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6

Olsson, P. E., M. Zafarullah, and L. Gedamu. "A role of metallothionein in zinc regulation after oestradiol induction of vitellogenin synthesis in rainbow trout, Salmo gairdneri." Biochemical Journal 257, no. 2 (January 15, 1989): 555–59. http://dx.doi.org/10.1042/bj2570555.

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The regulation of metallothionein (MT) biosynthesis in rainbow-trout liver was studied after a single intraperitoneal injection of oestradiol-17 beta. Sampling was performed after 2, 7, 14, 21, 28 and 35 days. Following induction of vitellogenin synthesis in the liver, liver somatic index (LSI) rose from 1.25 to 2.00 in 14 days. Associated with the increase in LSI was an elevation of hepatic vitellogenin mRNA and zinc concentrations. The vitellogenin mRNA concentrations peaked at 7 days after treatment. The zinc concentrations increased to a peak at day 14. MT was analysed by using differential pulse polarography and a rainbow-trout MT RNA probe. The MT mRNA concentrations rose after 14 days and remained elevated at 21 and 28 days. The MT concentrations increased after 14 days and remained elevated throughout the experimental period. The concentrations of MT-bound zinc increased in association with the elevation in MT concentrations in the oestradiol-treated rainbow trout. These findings indicate that MT is involved in the regulation of zinc during the period of vitellogenin induction and that MT may function by maintaining the pool of available zinc at an appropriate concentration.

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7

An, L., J. Hu, M. Yang, F. Jin, Q. Du, and Z. Ke. "Enhanced Vitellogenin Induction of Secondary Effluents by Chlorination." Bulletin of Environmental Contamination and Toxicology 77, no. 1 (July 2006): 67–73. http://dx.doi.org/10.1007/s00128-006-1033-8.

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8

Bradley, James T., and John M. Grizzle. "Vitellogenin induction by estradiol in channel catfish, Ictalurus punctatus." General and Comparative Endocrinology 73, no. 1 (January 1989): 28–39. http://dx.doi.org/10.1016/0016-6480(89)90052-x.

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9

Celius, T., and BT Walther. "Oogenesis in Atlantic salmon (Salmo salar L.) occurs by zonagenesis preceding vitellogenesis in vivo and in vitro." Journal of Endocrinology 158, no. 2 (August 1, 1998): 259–66. http://dx.doi.org/10.1677/joe.0.1580259.

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Fish oogenesis represents pleiotropic cytodifferentiative programs including hepatic synthesis of the molecular components for both the eggshell and the oocytic energy deposits. Both hepatic processes are directly controlled by plasma levels of estradiol (E2), and injected E2 induces both biogenetic processes in prepubertal fish of both sexes. This work compares the temporal pattern of E2-induced biosynthesis of zona radiata proteins (zr-proteins) and vitellogenin in Atlantic salmon (Salmo salar L.) in vivo and in vitro. We monitored the presence of plasma zr-proteins and vitellogenin, using homologous polyclonal antiserum to zr-proteins and a monoclonal antibody to vitellogenin. Zr-proteins were induced by all E2 concentrations (0.001-1.1 mg/kg body weight (bw)) within one week of exposure while vitellogenin was not induced until two weeks post-injection and then only in plasma from fish injected with high E2 concentrations (0.4 mg or 1.1 mg/kg bw). After E2 treatment, hepatocytes isolated from male fish synthesized zr-proteins and vitellogenin in vitro. However, zr-proteins were secreted into the medium two days before vitellogenin, as measured by ELISA. The data indicate a preferential induction of zr-proteins compared with vitellogenin, both with regard to E2 sensitivity and response time to E2 treatment. These findings suggest an obligate sequence in salmon oogenesis. During sexual maturation low E2 levels at first induce only zonagenesis, while increasing levels of E2 subsequently induce both zonagenesis and vitellogenesis. In nature, the interval between zonagenesis and vitellogenesis may, therefore, be considerable. The data suggest new control mechanisms in fish oogenesis.

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10

Haché, R. J., S. P. Tam, A. Cochrane, M. Nesheim, and R. G. Deeley. "Long-term effects of estrogen on avian liver: estrogen-inducible switch in expression of nuclear, hormone-binding proteins." Molecular and Cellular Biology 7, no. 10 (October 1987): 3538–47. http://dx.doi.org/10.1128/mcb.7.10.3538.

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The stimulation of chicks or embryos with estrogen results in transient, hepatic expression of the vitellogenin gene, as well as long-term, propagatable alterations in the rapidity with which the gene can be reactivated. We examined the possibility that nuclear, type II estrogen-binding sites are involved in this long-term change in response characteristics. We demonstrate that the primary induction kinetics of type II sites in embryos and chicks correlated with the expression of the vitellogenin gene and that once their induction was triggered by estrogen, they accumulated, were propagated, and persisted for months after withdrawal of the hormone. We also show that their accumulation in the embryo was accompanied by prolonged expression of both the vitellogenin and very low-density apolipoprotein II genes, in the absence of elevated levels of type I receptor, and that the type II sites, like the classical receptor, appear to be preferentially associated with active or potentially active chromatin. Finally, we describe a regulatory mechanism, tested by computer modelling, that simulated the behavioral characteristics of these nuclear estrogen-binding sites and which may explain their role in mediating the long-term effects of estrogen.

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11

Haché, R. J., S. P. Tam, A. Cochrane, M. Nesheim, and R. G. Deeley. "Long-term effects of estrogen on avian liver: estrogen-inducible switch in expression of nuclear, hormone-binding proteins." Molecular and Cellular Biology 7, no. 10 (October 1987): 3538–47. http://dx.doi.org/10.1128/mcb.7.10.3538-3547.1987.

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The stimulation of chicks or embryos with estrogen results in transient, hepatic expression of the vitellogenin gene, as well as long-term, propagatable alterations in the rapidity with which the gene can be reactivated. We examined the possibility that nuclear, type II estrogen-binding sites are involved in this long-term change in response characteristics. We demonstrate that the primary induction kinetics of type II sites in embryos and chicks correlated with the expression of the vitellogenin gene and that once their induction was triggered by estrogen, they accumulated, were propagated, and persisted for months after withdrawal of the hormone. We also show that their accumulation in the embryo was accompanied by prolonged expression of both the vitellogenin and very low-density apolipoprotein II genes, in the absence of elevated levels of type I receptor, and that the type II sites, like the classical receptor, appear to be preferentially associated with active or potentially active chromatin. Finally, we describe a regulatory mechanism, tested by computer modelling, that simulated the behavioral characteristics of these nuclear estrogen-binding sites and which may explain their role in mediating the long-term effects of estrogen.

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12

Jones, P. D., W. M. De Coen, L. Tremblay, and J. P. Giesy. "Vitellogenin as a biomarker for environmental estrogens." Water Science and Technology 42, no. 7-8 (October 1, 2000): 1–14. http://dx.doi.org/10.2166/wst.2000.0546.

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Much recent interest has focused on “xenoestrogens” in the environment. The potential for these chemicals to disrupt hormonal function in wildlife has led to the development of techniques to monitor the effects of discharges of these compounds particularly in aquatic environments. Increases in the concentration of the egg yolk precursor protein, vitellogenin (Vtg), in the plasma of fish and other vertebrates have been identified as a potentially useful biomarker of exposure to and the effects of chemicals with estrogen like properties. Here, we review the mechanisms underlying Vtg production, methods for the analysis of Vtg, and studies that have measured Vtg production in response to chemical or effluent exposure. These studies indicate that the production of Vtg may be a useful biomarker of exposure to estrogenic chemicals but that a greater understanding of the mechanism of action of these chemicals is required. In cyprinid fishes reproductive endpoints are more sensitive to exposureto xenoestrogens than Vtg induction. These observations indicate that Vtg induction is of more use as a biomarker of exposure to xenoestrogens rather than a predictor of adverse effects.

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13

Vega-López, Armando, Laura Martínez-Tabche, Maria Lilia Domínguez-López, Ethel García-Latorre, Eva Ramón-Gallegos, and Alejandra García-Gasca. "Vitellogenin induction in the endangered goodeid fish Girardinichthys viviparus: Vitellogenin characterization and estrogenic effects of polychlorinated biphenyls." Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology 142, no. 3-4 (March 2006): 356–64. http://dx.doi.org/10.1016/j.cbpc.2005.11.009.

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14

Kim, Pan-Gyi. "Chlortetracycline Caused Vitellogenin Induction at Male Japanese Medaka (Oryzias latipes)." Korean Journal of Environmental Health Sciences 33, no. 6 (December 31, 2007): 513–16. http://dx.doi.org/10.5668/jehs.2007.33.6.513.

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15

Norberg, Birgitta. "Atlantic halibut (Hippoglossus hippoglossus) vitellogenin: induction, isolation and partial characterization." Fish Physiology and Biochemistry 14, no. 1 (February 1995): 1–13. http://dx.doi.org/10.1007/bf00004286.

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16

Boehm, K. D., R. L. Hood, and J. Ilan. "Induction of vitellogenin in primary monolayer cultures of cockerel hepatocytes." Proceedings of the National Academy of Sciences 85, no. 10 (May 1, 1988): 3450–54. http://dx.doi.org/10.1073/pnas.85.10.3450.

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17

Palumbo, A. J., J. Linares-Casenave, W. Jewell, S. I. Doroshov, and R. S. Tjeerdema. "Induction and partial characterization of California halibut (Paralichthys californicus) vitellogenin." Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 146, no. 2 (February 2007): 200–207. http://dx.doi.org/10.1016/j.cbpa.2006.10.023.

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18

Hewitt, L. M., K. R. Munkittrick, G. J. Van Der Kraak, I. M. Scott, L. P. Schleen, and M. R. Servos. "Hepatic mixed function oxygenase activity and vitellogenin induction in fish following a treatment of the lampricide 3-trifluoromethyl-4-nitrophenol (TFM)." Canadian Journal of Fisheries and Aquatic Sciences 55, no. 9 (September 1, 1998): 2078–86. http://dx.doi.org/10.1139/f98-092.

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Recent laboratory studies with nontarget fish species have shown that the lampricide 3-trifluoromethyl-4-nitrophenol (TFM) exhibits estrogenic activity through binding to rainbow trout (Oncorhynchus mykiss) hepatic estrogen receptors and induction of vitellogenin in hepatocyte cultures. In addition, mixed function oxygenase (MFO) activity associated with exposure to field formulations has been attributed in part to the presence of chloro-nitro-trifluoromethyl-dibenzo-p-dioxin impurities. To investigate the environmental effects associated with these findings, the temporal and spatial patterns of MFO activity and vitellogenin induction were monitored in three nontarget fish species following a TFM field treatment. Elevated MFO activity was detected as early as 1 day in caged rainbow trout and activity in trout, wild white sucker (Catostomus commersoni), and longnose dace (Rhinichthys cataractae) peaked 2 or 3 days after treatment. Highest activities were observed in fish exposed closest to lampricide application points and declined with increasing distance downstream. After 18 days, MFO activity was reduced but remained almost sevenfold reference values at several sites. Plasma vitellogenin was not detected in caged trout sampled 6 and 18 days post-treatment, and dioxin impurities were not detected in sediments after treatment. It was concluded that laboratory testing underestimated the duration of MFO activity under field conditions and that an assessment of formulation exposure during sensitive life stages represents an area for further study.

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19

Hyllner, Sven Johan, Birgitta Norberg, and Carl Haux. "Isolation, Partial Characterization, Induction, and the Occurrence in Plasma of the Major Vitelline Envelope Proteins in the Atlantic Halibut (Hippoglossus hippoglossus) during Sexual Maturation." Canadian Journal of Fisheries and Aquatic Sciences 51, no. 8 (August 1, 1994): 1700–1707. http://dx.doi.org/10.1139/f94-171.

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The vitelline envelope of Atlantic halibut (Hippoglossus hippoglossus) is composed mainly of two major and two minor proteins. Estradiol-17ß induces the two major vitelline envelope proteins in halibut of both sexes. These proteins were also found in plasma of vitellogenic females. The origin of the two major vitelline envelope proteins is not restricted to the ovary, as male halibut synthesize these proteins after treatment with estradiol-17ß. Individual female halibut were followed and plasma sampled from May to March. Plasma levels of estradiol-17ß increased in October, peaked in early February, and declined until the last ovulation in March. In October, the two major vitelline envelope proteins were first detected in plasma and the amount remained elevated until early March. Prior to the last ovulation, the amount decreased. Plasma vitellogenin varied in a similar way. The results provide strong evidence that the physiological regulation of the synthesis of the major vitelline envelope proteins in teleosts is controlled by the female sex steroid estradiol-17ß.

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20

Havelková, M., Z. Svobodová, J. Kolářová, J. Krijt, D. Némethová, J. Jarkovský, and R. Pospíšil. "Organic Pollutant Contamination of the River Tichá Orlice as Assessed by Biochemical Markers." Acta Veterinaria Brno 77, no. 1 (2008): 133–41. http://dx.doi.org/10.2754/avb200877010133.

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This study used biochemical markers to assess contamination at two contaminated sites (Králíky and Lichkov) and one control site (Červená Voda) on the River Tichá Orlice, a left-side tributary of the River Elbe. The brown trout (Salmo trutta fario) was selected as an indicator species. Enzymes of the first stage of xenobiotic conversion, namely cytochrome P450 (CYP 450) and ethoxyresorufin-O-deethylase (EROD) in the liver were selected as biochemical markers. Blood plasma vitellogenin concentrations were used to evaluate xenoestrogenic effects of contamination. Results were compared with the most important inductors of these markers, i.e. with organic pollutants (PCB, HCH, HCB, OCS and DDT and their metabolites in fish muscle and with PAH concentrations in bottom sediments). The highest contamination with organic pollutants was at Králíky, and this was reflected in increased cytochrome P450, EROD activity and vitellogenin concentrations. Significant differences were demonstrated in EROD activity and vitellogenin concentrations between Králíky and Červená Voda (P < 0.001). At the most contaminated site (Králíky), a significant negative correlation (rs = -0.964) between EROD activity and vitellogenin concentrations was demonstrated. This relationship was discussed from the point of view of a possible induction or inhibition of the assessed biomarkers at persistently highly contaminated sites.

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21

Prasatkaew, Witchuda, Phochit Nanthanawat, Nanthika Khongchareonporn, and Sutin Kingtong. "A monoclonal antibody against Lates calcarifer vitellogenin and a competitive ELISA to evaluate vitellogenin induction after exposure to xenoestrogen." Journal of Environmental Sciences 75 (January 2019): 325–33. http://dx.doi.org/10.1016/j.jes.2018.05.001.

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22

Lorenzen, A., WL Casley, and JL Shutt. "Avian vitellogenin: In vitro mRNA induction and comparison of nucleotide sequences." Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 124 (August 1999): S46. http://dx.doi.org/10.1016/s1095-6433(99)90182-4.

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23

Jeon, Sung-Hwan, Chulwoo Lee, Hyun-Seok Bae, Jisung Ryu, Jin-Gyun Na, and Moon-Soon Lee. "674 Vitellogenin induction by synthetic estrogen in wild Medka in Korea." Toxicology Letters 144 (September 2003): s181. http://dx.doi.org/10.1016/s0378-4274(03)90673-4.

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24

Kotaki, T. "Oosorption in the stink bug, Plautia crossota stali: induction and vitellogenin dynamics." Journal of Insect Physiology 49, no. 2 (February 2003): 105–13. http://dx.doi.org/10.1016/s0022-1910(02)00254-8.

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25

RIEGEL, ANNA TATE, SUSAN C. AITKEN, MARY BETH MARTIN, and DANIEL R. SCHOENBERG. "Differential Induction of Hepatic Estrogen Receptor and Vitellogenin Gene Transcription inXenopus laevis*." Endocrinology 120, no. 4 (April 1987): 1283–90. http://dx.doi.org/10.1210/endo-120-4-1283.

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26

Burki, Richard, Aleksei Krasnov, Kathrin Bettge, Caird E. Rexroad, Sergej Afanasyev, Mia Antikainen, Patricia Burkhardt-Holm, Thomas Wahli, and Helmut Segner. "Pathogenic infection confounds induction of the estrogenic biomarker vitellogenin in rainbow trout." Environmental Toxicology and Chemistry 31, no. 10 (August 23, 2012): 2318–23. http://dx.doi.org/10.1002/etc.1966.

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27

Shilling, A. D., and D. E. Williams. "Determining Relative Estrogenicity by Quantifying Vitellogenin Induction in Rainbow Trout Liver Slices." Toxicology and Applied Pharmacology 164, no. 3 (May 2000): 330–35. http://dx.doi.org/10.1006/taap.2000.8912.

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28

Mañanós, E., S. Zanuy, F. Le Menn, M. Carrillo, and J. Núñez. "Sea bass (Dicentrarchus labrax L.) vitellogenin. I—Induction, purification and partial characterization." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 107, no. 2 (February 1994): 205–16. http://dx.doi.org/10.1016/0305-0491(94)90041-8.

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29

Zhong, Xueping, Ying Xu, Yong Liang, Tao Liao, and Jianwei Wang. "Vitellogenin in rare minnow (Gobiocypris rarus): identification and induction by waterborne diethylstilbestrol." Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology 137, no. 3 (March 2004): 291–98. http://dx.doi.org/10.1016/j.cca.2004.02.004.

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30

Gemmill, R. M., M. Hamblin, R. L. Glaser, J. V. Racioppi, J. L. Marx, B. N. White, J. M. Calvo, M. F. Wolfner, and H. H. Hagedorn. "Isolation of mosquito vitellogenin genes and induction of expression by 20-hydroxyecdysone." Insect Biochemistry 16, no. 5 (January 1986): 761–74. http://dx.doi.org/10.1016/0020-1790(86)90112-5.

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31

Azad, I. S., and N. Al-Jandal. "Induction of vitellogenin in cultured fish: Vitellogenin gene expression response of blue fin and yellow fin breams to injected 17 -estradiol." Journal of Environmental Chemistry and Ecotoxicology 12, no. 1 (February 29, 2020): 8–16. http://dx.doi.org/10.5897/jece2019.0448.

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32

Lee Pow, Crystal S. D., Erin E. Yost, D. Derek Aday, and Seth W. Kullman. "Sharing the Roles: An Assessment of Japanese Medaka Estrogen Receptors in Vitellogenin Induction." Environmental Science & Technology 50, no. 16 (July 26, 2016): 8886–95. http://dx.doi.org/10.1021/acs.est.6b01968.

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33

Marin, Maria Gabriella, and Valerio Matozzo. "Vitellogenin induction as a biomarker of exposure to estrogenic compounds in aquatic environments." Marine Pollution Bulletin 48, no. 9-10 (May 2004): 835–39. http://dx.doi.org/10.1016/j.marpolbul.2004.02.037.

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34

Canapa, A., M. Barucca, A. Celeste, E. Olmo, and F. Regoli. "Preliminary investigations on vitellogenin m-RNA induction in some bioindicator Mediterranean fish species." Marine Environmental Research 54, no. 3-5 (September 2002): 673–77. http://dx.doi.org/10.1016/s0141-1136(02)00145-9.

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35

Comas, Daniel, Maria-Dolors Piulachs, and Xavier Bellés. "Induction of vitellogenin gene transcription in vitro by juvenile hormone in Blattella germanica." Molecular and Cellular Endocrinology 183, no. 1-2 (October 2001): 93–100. http://dx.doi.org/10.1016/s0303-7207(01)00589-5.

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36

Rose, Jon, Henrik Holbech, Christian Lindholst, Ulrik Nørum, Allan Povlsen, Bodil Korsgaard, and Poul Bjerregaard. "Vitellogenin induction by 17β-estradiol and 17α-ethinylestradiol in male zebrafish (Danio rerio)." Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology 131, no. 4 (April 2002): 531–39. http://dx.doi.org/10.1016/s1532-0456(02)00035-2.

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37

Heck, Jennifer, Duncan S. MacKenzie, David Rostal, Kathryn Medler, and David Owens. "Estrogen Induction of Plasma Vitellogenin in the Kemp's Ridley Sea Turtle (Lepidochelys kempi)." General and Comparative Endocrinology 107, no. 2 (August 1997): 280–88. http://dx.doi.org/10.1006/gcen.1997.6930.

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38

Carnevali, Oliana, and Gilberto Mosconi. "In vitro induction of vitellogenin synthesis in Rana esculenta: Role of the pituitary." General and Comparative Endocrinology 86, no. 3 (June 1992): 352–58. http://dx.doi.org/10.1016/0016-6480(92)90060-w.

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39

Edwards, Gordon C., Ralph P. Braun, and Gerard R. Wyatt. "Induction of vitellogenin synthesis in Locusta migratoria by the juvenile hormone analog, pyriproxyfen." Journal of Insect Physiology 39, no. 7 (July 1993): 609–14. http://dx.doi.org/10.1016/0022-1910(93)90043-q.

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40

Davis, Lori K., Bradley K. Fox, Chhorn Lim, Naoshi Hiramatsu, Craig V. Sullivan, Tetsuya Hirano, and E. Gordon Grau. "Induction of vitellogenin production in male tilapia (Oreochromis mossambicus) by commercial fish diets." Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 154, no. 2 (October 2009): 249–54. http://dx.doi.org/10.1016/j.cbpa.2009.06.009.

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41

Tabata, A., N. Watanabe, I. Yamamoto, Y. Ohnishi, M. Itoh, T. Kamei, Y. Magara, and Y. Terao. "The effect of bisphenol A and chlorinated derivatives of bisphenol A on the level of serum vitellogenin in Japanese medaka (Oryzias latipes)." Water Science and Technology 50, no. 5 (September 1, 2004): 125–32. http://dx.doi.org/10.2166/wst.2004.0319.

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2,2-bis (4-hydroxyphenyl) propane or Bisphenol A (BPA), has been reported to behave as an endocrine disrupter below acute toxic levels, and is widely present in the water environment. Although BPA is easily chlorinated, very little is reported on the effect of chlorinated BPA to the aquatic organisms. In this study, the estrogenic activities of BPA and its chlorinated derivatives were evaluated by the induction of vitellogenin (VTG) in the serum of mature male Japanese medaka. In addition, the effect of sodium hypochlorite on the decomposition of BPA was tested. The relative potencies of estrogenic activities of chlorinated BPA descended in the order 3,3′-diClBPA>BPA≥3-ClBPA>3,3′,5-triClBPA, and no estrogenic activity was observed in 3,3′,5,5′-tetraClBPA. Lowest Observed Effect Concentration (LOEC) and No Observed Effect Concentration (NOEC) for both 3-ClBPA and 3,3′-diClBPA were 500 μg/L and 200 μg/L, respectively. LOEC for 3,3′,5-triClBPA was >500 μg/L. When BPA was reacted with sodium hypochlorite (24 hours; residual chlorine at 1 ppm), however, complete decomposition of BPA and its chlorinated derivatives was observed. The decrease in BPA and its chlorinated derivatives paralleled the decrease in estrogenic potency evaluated by the induction of vitellogenin (VTG) in the serum of mature male Japanese medaka.

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42

Flouriot, G., F. Pakdel, B. Ducouret, and Y. Valotaire. "Influence of xenobiotics on rainbow trout liver estrogen receptor and vitellogenin gene expression." Journal of Molecular Endocrinology 15, no. 2 (October 1995): 143–51. http://dx.doi.org/10.1677/jme.0.0150143.

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ABSTRACT Rainbow trout hepatocyte primary culture was used to test the influence of some xenobiotics on the expression of two genes implicated in reproduction, those for the estrogen receptor (ER) and vitellogenin (Vg). We showed that chlordecone, nonylphenol, a polychlorobiphenol (PCB) mixture (Aroclor 1245) and lindane were able to induce ER and Vg mRNA accumulation. Antiestrogens, 4-hydroxytamoxifen and ICI 164,384, prevented the effects of the xenobiotics, indicating that the induction of gene expression is mediated by the ER. Among these four xenobiotics, only chlordecone and nonylphenol were able to displace the binding of [3H]estradiol to ER-enriched COS-1 extracts, and to activate an estrogen-dependent reporter gene (ERE-TK-CAT) cotransfected with an expression vector containing ER cDNA. The results suggest that chlordecone and nonylphenol are direct inducers of rainbow trout ER and Vg gene expression, whereas PCBs and lindane act through their hepatic metabolites. Moreover, pentachlorophenol acts as an antagonist of the induction by estradiol of rainbow trout ER and Vg gene expression.

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43

Huang, Da-Ji, and Hon-Cheng Chen. "Effects of Chlordane and Lindane on Testosterone and Vitellogenin Levels in Green Neon Shrimp (Neocaridina denticulata)." International Journal of Toxicology 23, no. 2 (March 2004): 91–95. http://dx.doi.org/10.1080/10915810490435604.

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The purpose of this study was to investigate the acute toxicity of chlordane and lindane as well as their endocrine disruption effect on green neon shrimp ( Neocaridina denticulata), a common habitant in freshwater system of eastern Asia and Hawaii. First, the organisms were exposed to chlordane and lindane to estimate the 96-h LC50(96-h median lethal concentration). Then, levels of testosterone and vitellogenin in hemolymph of N. denticulata after exposure to sublethal concentrations of chlordane (1 ng/L and 10 ng/L) and lindane (0.1 μg/L and 1 μg/L) were also examined. The 96-h LC50 values obtained from the results of acute exposure were 127.03 (130.11–122.35) ng/L and 9.36 (8.00–10.96) μg/L for chlordane and lindane, respectively. Furthermore, reductions of testosterone concentration were observed in both chlordane- and lindane-treated shrimps, whereas induction of vitellogenin-like protein was only apparent in chlordane-treated shrimps. Thus, it is concluded that chlordane and lindane may probably show some disruption endocrine functions on N. denticulata.

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44

Palmer, Brent D., and Sylvia K. Palmer. "Vitellogenin Induction by Xenobiotic Estrogens in the Red-Eared Turtle and African Clawed Frog." Environmental Health Perspectives 103 (May 1995): 19. http://dx.doi.org/10.2307/3432407.

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Barse, A. V., T. Chakrabarti, T. K. Ghosh, A. K. Pal, Neeraj Kumar, R. P. Raman, and S. B. Jadhao. "Vitellogenin Induction and Histo-metabolic Changes Following Exposure of Cyprinus carpio to Methyl Paraben." Asian-Australasian Journal of Animal Sciences 23, no. 12 (October 25, 2010): 1557–65. http://dx.doi.org/10.5713/ajas.2010.10118.

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46

Foran, C. M., C. D. Metcalfe, T. L. Metcalfe, and W. H. Benson. "Influence of exposure history on vitellogenin induction in medaka: a case of ‘estrogen memory’?" Marine Environmental Research 50, no. 1-5 (July 2000): 196. http://dx.doi.org/10.1016/s0141-1136(00)00178-1.

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47

Larsson, D. G. J., H. Berg, P. E. Olsson, and L. Förlin. "Induction of vitellogenin in eelpout (Zoarces viviparus) and perch (Perca fluviatilis) by environmental estrogens." Marine Environmental Research 46, no. 1-5 (July 1998): 175. http://dx.doi.org/10.1016/s0141-1136(98)00047-6.

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48

Palmer, B. D., and S. K. Palmer. "Vitellogenin induction by xenobiotic estrogens in the red-eared turtle and African clawed frog." Environmental Health Perspectives 103, suppl 4 (May 1995): 19–25. http://dx.doi.org/10.1289/ehp.95103s419.

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49

Zhang, Y., Q. Qu, D. Sun, X. Liu, L. Suo, and Y. Zhang. "Vitellogenin in Amur sturgeon (Acipenser schrenckii): induction, purification and changes during the reproductive cycle." Journal of Applied Ichthyology 27, no. 2 (March 28, 2011): 660–65. http://dx.doi.org/10.1111/j.1439-0426.2011.01698.x.

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50

Jena, Bipulendu, Jyotirmaya Mohanty, Radha C. Das, Sushil K. Garnayak, and Samiran Nandi. "Induction, purification and partial characterization of vitellogenin in an Indian major carpCatla catla(Ham.)." Aquaculture Research 44, no. 12 (July 5, 2012): 1901–11. http://dx.doi.org/10.1111/j.1365-2109.2012.03195.x.

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