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Modig, Carina
Publications (10 of 11) Show all publications
Asnake, S., Modig, C. & Olsson, P.-E. (2019). Species differences in ligand interaction and activation of estrogen receptors in fish and human. Journal of Steroid Biochemistry and Molecular Biology, Article ID 105450.
Open this publication in new window or tab >>Species differences in ligand interaction and activation of estrogen receptors in fish and human
2019 (English)In: Journal of Steroid Biochemistry and Molecular Biology, ISSN 0960-0760, E-ISSN 1879-1220, article id 105450Article in journal (Refereed) Epub ahead of print
Abstract [en]

Estrogen receptor (ER) sequences vary between species and this suggests that there are differences in the ligand-specificity, leading to species-specific effects. This would indicate that it is not possible to generalize effects across species. In this study, we investigated the differences in activation potencies and binding affinities of ER´s alpha (α) and beta (β) in human, zebrafish and sea bream to elucidate species differences in response to estradiol, estrone, estriol and methyltestosterone. In vitro analysis showed that estradiol had the highest activity for all the ER´s except for human ERβ and seabream ERβ2. Alignment of the ligand binding domain and ligand binding pocket (LBP) residues of the three species showed that different residues were involved in the LBPs which led to differences in pocket volume, affected binding affinity and orientation of the ligands. By combining in silico and in vitro results, it was possible to identify the ligand specificities of ER´s. The results demonstrated that the human ER´s show lower resolution in ligand-dependent activation, suggesting higher promiscuity, than the zebrafish and seabream ER´s. These results show species-specificity of ER´s and suggest that species-specific differences must be taken into consideration when studying different exposure scenarios.

Place, publisher, year, edition, pages
Pergamon Press, 2019
Keywords
In silico, ligand binding pocket, ligand resolution, ligand specificity, species-specific
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:oru:diva-75906 (URN)10.1016/j.jsbmb.2019.105450 (DOI)31437548 (PubMedID)
Available from: 2019-09-09 Created: 2019-09-09 Last updated: 2019-09-09Bibliographically approved
Pradhan, A., Asnake, S., Kharlyngdoh, J. B., Modig, C. & Olsson, P.-E. (2015). In silico and biological analysis of anti-androgen activity of the brominated flame retardants ATE, BATE and DPTE in zebrafish. Chemico-Biological Interactions, 233, 35-45
Open this publication in new window or tab >>In silico and biological analysis of anti-androgen activity of the brominated flame retardants ATE, BATE and DPTE in zebrafish
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2015 (English)In: Chemico-Biological Interactions, ISSN 0009-2797, E-ISSN 1872-7786, Vol. 233, p. 35-45Article in journal (Refereed) Published
Abstract [en]

The brominated flame retardants (BFRs) 1,2-dibromo-4-(1,2-dibromoethyl)cyclohexane (TBECH or DBE-DCBH) and allyl 2,4,6-tribromophenyl ether (ATE or TBP-AE) are alternative BFRs that have been introduced to replace banned BFRs. TBECH is a potential endocrine disrupter in human, chicken and zebrafish and in a recent study we showed that ATE, along with the structurally similar BFR 2,3-dibromopropyl 2,4,6-tribromophenyl ether (DPTE or TBP-DBPE) and its metabolite 2-bromoallyl 2,4,6-tribromophenyl ether (BATE or TBP-BAE) are potential endocrine and neuronal disrupters in human. In this study we analyzed ATE, BATE and DPTE for zebrafish androgen receptor (zAR) modulating properties. In silico analysis with two softwares, Molecular Operating Environment (MOE) and Internal Coordinate Mechanics (ICM), showed that ATE, BATE and DPTE bind to zAR. In vitro AR activation assay revealed that these three BFRs down-regulate 11-ketotestosterone (KT) mediated zAR activation. Exposure to 10 mu M DPTE resulted in reduced hatching success and like TBECH, BATE and DPTE at 10 mu M also had teratogenic properties with 20% and 50% back-bone curvature respectively. Gene transcription analysis in zebrafish embryos as well as in juveniles showed down-regulation of the androgen receptor and androgen response genes, which further support that these BFRs are androgen antagonists and potential endocrine disrupting compounds. Genes involved in steroidogenesis were also down-regulated by these BFRs. In view of this, the impact of these BFRs on humans and wildlife needs further analysis.

Keywords
Gene regulation; Steroidogenesis; TBP-AE; TBP-BAE; TBP-DBPE; Teratogenesis
National Category
Biological Sciences
Research subject
Biology
Identifiers
urn:nbn:se:oru:diva-44811 (URN)10.1016/j.cbi.2015.03.023 (DOI)000354139600004 ()25818047 (PubMedID)2-s2.0-84926156248 (Scopus ID)
Funder
Knowledge Foundation
Note

Funding Agency:

Örebro University

Available from: 2015-06-03 Created: 2015-06-03 Last updated: 2017-10-18Bibliographically approved
Asnake, S., Pradhan, A., Kharlyngdoh, J. B., Modig, C. & Olsson, P.-E. (2015). The brominated flame retardants TBP-AE and TBP-DBPE antagonize the chicken androgen receptor and act as potential endocrine disrupters in chicken LMH cells. Toxicology in Vitro, 29(8), 1993-2000
Open this publication in new window or tab >>The brominated flame retardants TBP-AE and TBP-DBPE antagonize the chicken androgen receptor and act as potential endocrine disrupters in chicken LMH cells
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2015 (English)In: Toxicology in Vitro, ISSN 0887-2333, E-ISSN 1879-3177, Vol. 29, no 8, p. 1993-2000Article in journal (Refereed) Published
Abstract [en]

Increased exposure of birds to endocrine disrupting compounds has resulted in developmental and reproductive dysfunctions. We have recently identified the flame retardants, ally1-2,4,6-tribromophenyl ether (TBP-AE), 2-3-dibromopropy1-2,4,6-tribromophenyl ether (TBP-DBPE) and the TBP-DBPE metabolite 2-bromoallyI-2,4,6-tribromophenyl ether (TBP-BAE) as antagonists to both the human androgen receptor (AR) and the zebrafish AR. In the present study, we aimed at determining whether these compounds also interact with the chicken AR. In silico modeling studies showed that TBP-AE, TBP-BAE and TBP-DBPE were able to dock into to the chicken AR ligand-binding pocket. In vitro transfection assays revealed that all three brominated compounds acted as chicken AR antagonists, inhibiting testosterone induced AR activation. In addition, qRT-PCR studies confirmed that they act as AR antagonists and demonstrated that they also alter gene expression patterns of apoptotic, anti-apoptotic, drug metabolizing and amino acid transporter genes. These studies, using chicken LMH cells, suggest that TBP-AE, TBP-BAE and TBP-DBPE are potential endocrine disrupters in chicken.

Place, publisher, year, edition, pages
Elsevier, 2015
Keywords
EDC, Avian, Signaling pathways, ATE, BATE, DPTE, DBE-DBCH, TBECH
National Category
Pharmacology and Toxicology Biological Sciences
Research subject
Biology
Identifiers
urn:nbn:se:oru:diva-47080 (URN)10.1016/j.tiv.2015.08.009 (DOI)000364892000004 ()26318274 (PubMedID)2-s2.0-84940502384 (Scopus ID)
Funder
Swedish Research Council, 20110183
Note

Funding Agency:

Örebro University J61900

Available from: 2015-12-15 Created: 2015-12-15 Last updated: 2018-01-10Bibliographically approved
Asnake, S., Pradhan, A., Banjop-Kharlyngdoh, J., Modig, C. & Olsson, P.-E. (2014). 1,2-dibromo-4-(1,2 dibromoethyl) cyclohexane (TBECH)-mediated steroid hormone receptor activation and gene regulation in chicken LMH cells. Environmental Toxicology and Chemistry, 33(4), 891-899
Open this publication in new window or tab >>1,2-dibromo-4-(1,2 dibromoethyl) cyclohexane (TBECH)-mediated steroid hormone receptor activation and gene regulation in chicken LMH cells
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2014 (English)In: Environmental Toxicology and Chemistry, ISSN 0730-7268, E-ISSN 1552-8618, Vol. 33, no 4, p. 891-899Article in journal (Refereed) Published
Abstract [en]

The incorporation of brominated flame retardants into industrial and household appliances has increased their occurrence in the environment, resulting in deleterious effects on wildlife. With the increasing restraints on available compounds, there has been a shift to using brominated flame retardants that has seen the production of alternative brominated flame retardants such as 1,2-dibromo-4-(1,2 dibromoethyl) cyclohexane (TBECH), which has been detected in the environment. In previous in silico and in vitro studies the authors have shown that TBECH can activate both the human androgen receptor (hAR) and the zebrafish AR (zAR) suggesting that it is a potential endocrine disruptor. The present study was aimed at determining the interaction of TBECH with the chicken AR (cAR). In the present study, TBECH bound to cAR, but in vitro activation assay studies using the chicken LMH cell line showed it had a potency of only 15% compared with testosterone. Sequence difference between ARs from different species may contribute to the different responses to TBECH. Further quantitative reverse-transcriptase polymerase chain reaction (qRT-PCR) analysis showed that TBECH interacted with and altered the expression of both thyroid receptors and estrogen receptors. In addition, the qRT-PCR analysis showed that TBECH altered the transcription pattern of genes involved in inflammatory, apoptotic, proliferative, DNA methylation, and drug-metabolizing pathways. This demonstrates that TBECH, apart from activating cAR, can also influence multiple biological pathways in the chicken.

Place, publisher, year, edition, pages
Hoboken: Wiley-Blackwell, 2014
Keywords
Endocrine disruptor, Diastereomer, Enantiomer, Quantitative polymerase chain reaction (qPCR), Gene regulation
National Category
Environmental Sciences
Research subject
Enviromental Science; Biology
Identifiers
urn:nbn:se:oru:diva-34941 (URN)10.1002/etc.2509 (DOI)000333538700020 ()2-s2.0-84897431931 (Scopus ID)
Funder
Swedish Research Council
Note

Funding Agency:

Örebro University

Available from: 2014-05-05 Created: 2014-05-05 Last updated: 2017-12-05Bibliographically approved
Carvalho, R. N., Arukwe, A., Ait-Aissa, S., Bado-Nilles, A., Balzamo, S., Baun, A., . . . Lettieri, T. (2014). Mixtures of chemical pollutants at European legislation safety concentrations: how safe are they?. Toxicological Sciences, 141(1), 218-233
Open this publication in new window or tab >>Mixtures of chemical pollutants at European legislation safety concentrations: how safe are they?
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2014 (English)In: Toxicological Sciences, ISSN 1096-6080, E-ISSN 1096-0929, Vol. 141, no 1, p. 218-233Article in journal (Refereed) Published
Abstract [en]

The risk posed by complex chemical mixtures in the environment to wildlife and humans is increasingly debated, but has been rarely tested under environmentally relevant scenarios. To address this issue, two mixtures of 14 or 19 substances of concern (pesticides, pharmaceuticals, heavy metals, polyaromatic hydrocarbons, a surfactant, and a plasticizer), each present at its safety limit concentration imposed by the European legislation, were prepared and tested for their toxic effects. The effects of the mixtures were assessed in 35 bioassays, based on 11 organisms representing different trophic levels. A consortium of 16 laboratories was involved in performing the bioassays. The mixtures elicited quantifiable toxic effects on some of the test systems employed, including i) changes in marine microbial composition, ii) microalgae toxicity, iii) immobilization in the crustacean Daphnia magna, iv) fish embryo toxicity, v) impaired frog embryo development, and vi) increased expression on oxidative stress-linked reporter genes. Estrogenic activity close to regulatory safety limit concentrations was uncovered by receptor-binding assays. The results highlight the need of precautionary actions on the assessment of chemical mixtures even in cases where individual toxicants are present at seemingly harmless concentrations.

Keywords
bioassays, effects, mixtures, ecotoxicology, biomarkers
National Category
Environmental Sciences
Research subject
Enviromental Science
Identifiers
urn:nbn:se:oru:diva-38654 (URN)10.1093/toxsci/kfu118 (DOI)000342990200026 ()24958932 (PubMedID)
Note

Funding Agencies:

RADAR 265721

French Office Water and Aquatic Environment

French Ministry for Ecology and Sustainable Development P181 DRC50

Available from: 2014-11-17 Created: 2014-11-17 Last updated: 2018-09-07Bibliographically approved
Kling, P., Modig, C., Mujahed, H., Khalaf, H., von Hofsten, J. & Olsson, P.-E. (2013). Differential regulation of the rainbow trout (Oncorhynchus mykiss) MT-A gene by nuclear factor interleukin-6 and activator protein-1. BMC Molecular Biology, 14(1), 28
Open this publication in new window or tab >>Differential regulation of the rainbow trout (Oncorhynchus mykiss) MT-A gene by nuclear factor interleukin-6 and activator protein-1
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2013 (English)In: BMC Molecular Biology, ISSN 1471-2199, E-ISSN 1471-2199, Vol. 14, no 1, p. 28-Article in journal (Refereed) Published
Abstract [en]

BACKGROUND: Previously we have identified a distal region of the rainbow trout (Oncorhynchus mykiss) metallothionein-A (rtMT-A) enhancer region, being essential for free radical activation of the rtMT-A gene. The distal promoter region included four activator protein 1 (AP1) cis-acting elements and a single nuclear factor interleukin-6 (NF-IL6) element. In the present study we used the rainbow trout hepatoma (RTH-149) cell line to further examine the involvement of NF-IL6 and AP1 in rtMT-A gene expression following exposure to oxidative stress and tumour promotion.

RESULTS: Using enhancer deletion studies we observed strong paraquat (PQ)-induced rtMT-A activation via NF-IL6 while the AP1 cis-elements showed a weak but significant activation. In contrast to mammals the metal responsive elements were not activated by oxidative stress. Electrophoretic mobility shift assay (EMSA) mutation analysis revealed that the two most proximal AP1 elements, AP11,2, exhibited strong binding to the AP1 consensus sequence, while the more distal AP1 elements, AP13,4 were ineffective. Phorbol-12-myristate-13-acetate (PMA), a known tumor promoter, resulted in a robust induction of rtMT-A via the AP1 elements alone. To determine the conservation of regulatory functions we transfected human HepG2 cells with the rtMT-A enhancer constructs and were able to demonstrate that the cis-elements were functionally conserved. The importance of NF-IL6 in regulation of teleost MT is supported by the conservation of these elements in MT genes from different teleosts. In addition, PMA and PQ injection of rainbow trout resulted in increased hepatic rtMT-A mRNA levels.

CONCLUSIONS: These studies suggest that AP1 primarily is involved in PMA regulation of the rtMT-A gene while NF-IL6 is involved in free radical regulation. Taken together this study demonstrates the functionality of the NF-IL6 and AP-1 elements and suggests an involvement of MT in protection during pathological processes such as inflammation and cancer.

Place, publisher, year, edition, pages
BioMed Central, 2013
National Category
Natural Sciences
Identifiers
urn:nbn:se:oru:diva-32846 (URN)10.1186/1471-2199-14-28 (DOI)000329740300001 ()24341438 (PubMedID)2-s2.0-84890304314 (Scopus ID)
Funder
Knowledge FoundationKnut and Alice Wallenberg Foundation
Available from: 2013-12-19 Created: 2013-12-19 Last updated: 2018-05-21Bibliographically approved
Modig, C., Raldúa, D., Cerdà, J. & Olsson, P.-E. (2008). Analysis of vitelline envelope synthesis and composition during early oocyte development in gilthead seabream (Sparus aurata). Molecular Reproduction and Development, 75(8), 1351-1360
Open this publication in new window or tab >>Analysis of vitelline envelope synthesis and composition during early oocyte development in gilthead seabream (Sparus aurata)
2008 (English)In: Molecular Reproduction and Development, ISSN 1040-452X, E-ISSN 1098-2795, Vol. 75, no 8, p. 1351-1360Article in journal (Refereed) Published
Abstract [en]

The oocyte vitelline envelope (VE) of gilthead seabream is composed of four known zona pellucida (ZP) proteins, ZPBa, ZPBb, ZPC, and ZPX. We have previously shown that the gilthead seabream ZP proteins are differentially transcribed in liver and ovary, with the expression in liver being under estrogenic control. However, although mRNA was found in both liver and ovary, only low ZPBa protein levels were detected in liver and plasma. Using isoform-specific ZP antibodies we show that ZPBa and ZPX translation products are present in the cytosol of stage I and II oocytes. In addition, the zpBa and zpX mRNAs were detected in early developing oocytes. During oocyte growth (vitellogenesis), the VE increased in thickness (>10 µm), and we show that the four ZP isoforms are present in different regions of the VE. ZPX was detected closest to the oocyte plasma membrane while the intermediate region was composed of ZPBa, ZPBb, and ZPC. At the outer layer, only ZPC was detected. When oocytes reach the fully grown stage they resume meiosis and hydration. As the oocyte expands, thinning to 4 µm, the VE acquire a striped and compact appearance at the electron microscopy level. This study provides further evidence for the oocyte origin of some ZP proteins in the gilthead seabream and suggests that the ZP proteins are differentially distributed within the VE. Mol. Reprod. Dev. 75: 1351-1360, 2008.

Place, publisher, year, edition, pages
New York: Wiley-Liss, 2008
Keywords
Amino Acid Sequence, Animals, Blotting; Western, Egg Proteins/genetics/*metabolism, Electrophoresis; Polyacrylamide Gel, Enzyme-Linked Immunosorbent Assay, Immunohistochemistry, Liver/metabolism, Membrane Glycoproteins/genetics/*metabolism, Microscopy; Electron, Molecular Sequence Data, Oocytes/*growth & development, Protein Isoforms/metabolism, RNA; Messenger/*metabolism, Receptors; Cell Surface/genetics/*metabolism, Sea Bream/*physiology, Vitelline Membrane/*growth & development/*metabolism/ultrastructure, Vitellogenesis/*physiology
National Category
Natural Sciences Biological Sciences
Research subject
biologi
Identifiers
urn:nbn:se:oru:diva-3556 (URN)10.1002/mrd.20876 (DOI)18247334 (PubMedID)
Available from: 2008-12-09 Created: 2008-12-09 Last updated: 2017-12-14Bibliographically approved
Modig, C., Modesto, T., Canario, A., Cerdà, J., von Hofsten, J. & Olsson, P.-E. (2006). Molecular characterization and expression pattern of zona pellucida proteins in gilthead seabream (Sparus aurata). Biology of Reproduction, 75(5), 717-725
Open this publication in new window or tab >>Molecular characterization and expression pattern of zona pellucida proteins in gilthead seabream (Sparus aurata)
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2006 (English)In: Biology of Reproduction, ISSN 0006-3363, E-ISSN 1529-7268, Vol. 75, no 5, p. 717-725Article in journal (Refereed) Published
Abstract [en]

The developing oocyte is surrounded by an acellular envelope that is composed of 2-4 isoforms of zona pellucida (ZP) proteins. The ZP proteins comprise the ZP1, ZP2, ZP3, and ZPX isoforms. While ZP1 (ZPB) and ZP3 (ZPC) are present in all species, ZP2 (ZPA) is not found in teleost fish and ZPX is not found in mammals. In the present study, we identify and characterize the ZP1, ZP3 and ZPX isoforms of gilthead seabream. Furthermore, by analyzing the conserved domains, which include the external hydrophobic patch and the internal hydrophobic patch, we show that ZP2 and ZPX are closely related isoforms. ZP proteins are synthesized in either the liver or ovary of most teleosts. Only in rainbow trout has it been shown that zp3 has dual transcription sites. In gilthead seabream, all four mRNA isoforms are transcribed in both the liver and ovary, with zp1a, zp1b, and zp3 being highly expressed in the liver, and zpx being primarily expressed in the ovary. However, determination of the ZP proteins in plasma showed high levels of ZP1b, ZP3, and ZPX, with low or non-detectable levels of ZP1a. In similarity to other teleost ZPs, the hepatic transcription of all four ZP isoforms is under estrogenic control. Previously, we have shown that cortisol can potentiate estrogen-induced ZP synthesis in salmonids, and now we show that this is not the case in the gilthead seabream. The present study shows for the first time the endocrine regulation of a teleost ZPX isoform, and demonstrates the dual-organ transcriptional activities of all the ZP proteins in one species.

National Category
Biological Sciences
Research subject
Biology
Identifiers
urn:nbn:se:oru:diva-8831 (URN)10.1095/biolreprod.106.050757 (DOI)16855211 (PubMedID)
Available from: 2009-12-18 Created: 2009-12-18 Last updated: 2017-12-12Bibliographically approved
von Hofsten, J., Modig, C., Larsson, A., Karlsson, J. & Olsson, P.-E. (2005). Determination of the expression pattern of the dual promoter of zebrafish fushi tarazu factor-1a following microinjections into zebrafish one cell stage embryos. General and Comparative Endocrinology, 142(1-2), 222-226
Open this publication in new window or tab >>Determination of the expression pattern of the dual promoter of zebrafish fushi tarazu factor-1a following microinjections into zebrafish one cell stage embryos
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2005 (English)In: General and Comparative Endocrinology, ISSN 0016-6480, E-ISSN 1095-6840, Vol. 142, no 1-2, p. 222-226Article in journal (Refereed) Published
Abstract [en]

The zebrafish fushi tarazu factor-1a (ff1a) is a transcription factor belonging to the NR5A subgroup of nuclear receptors. The NR5A receptors bind DNA as monomers and are considered to be orphans due to their ability to promote transcription of downstream genes without ligands. In zebrafish, four ff1 homologues (Ff1a, Ff1b, Ff1c, and Ff1d) have been identified so far. The gene coding for Ff1a is driven by two separate promoters, and give rise to four splice variants. Ff1a is expressed in the somites and pronephric ducts during somitogenesis and in the brain, liver, and mandibular arch during later embryonic stages. In adults the gene is highly expressed in gonads, liver, and intestine, but can be detected in most tissues. The broad variety of embryonic expression domains indicates several important developmental features. One of the mammalian fushi tarazu factor-1 genes, steroidogenic factor-1 (SF-1), is essential for the development of gonads and adrenals. SF-1 is together with Sox9, WT1, and GATA4 a positive transcriptional regulator of human anti-mullerian hormone (AMH) and thereby linked to the male sex-determining pathway. The zebrafish ff1a dual promoter contains several GATA binding sites and E-boxes, a site for DR4, XFD2, MyoD, Snail, HNF3, S8, and an HMG-box recognition site for Sox9. In a first attempt to dissect the ff1a promoter in vivo we have produced first generation transgenes in order to determine the correlation between the expression of the endogenous ff1a gene and the microinjected ff1a dual promoter coupled to the pEGFP reporter vector. Our results show that the microinjected constructs are expressed in the correct tissues.

National Category
Biological Sciences
Research subject
Biology
Identifiers
urn:nbn:se:oru:diva-8836 (URN)10.1016/j.ygcen.2004.12.020 (DOI)15862566 (PubMedID)
Available from: 2009-12-18 Created: 2009-12-18 Last updated: 2018-02-02Bibliographically approved
Olsson, P.-E., Berg, A. H., von Hofsten, J., Grahn, B., Hellqvist, A., Larsson, A., . . . Thomas, P. (2005). Molecular cloning and characterization of a nuclear androgen receptor activated by 11-ketotestosterone. Reproductive biology and endocrinology, 3:37
Open this publication in new window or tab >>Molecular cloning and characterization of a nuclear androgen receptor activated by 11-ketotestosterone
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2005 (English)In: Reproductive biology and endocrinology, ISSN 1477-7827, Vol. 3:37Article in journal (Refereed) Published
Abstract [en]

Although 11-ketotestosterone is a potent androgen and induces male secondary sex characteristics in many teleosts, androgen receptors with high binding affinity for 11-ketotestosterone or preferential activation by 11-ketotestosterone have not been identified. So, the mechanism by which 11-ketotestosterone exhibits such high potency remains unclear. Recently we cloned the cDNA of an 11-ketotestosterone regulated protein, spiggin, from three-spined stickleback renal tissue. As spiggin is the only identified gene product regulated by 11-ketotestosterone, the stickleback kidney is ideal for determination of the mechanism of 11-ketotestosterone gene regulation. A single androgen receptor gene with two splicing variants, belonging to the androgen receptor-beta subfamily was cloned from stickleback kidney. A high affinity, saturable, single class of androgen specific binding sites, with the characteristics of an androgen receptor, was identified in renal cytosolic and nuclear fractions. Measurement of ligand binding moieties in the cytosolic and nuclear fractions as well as to the recombinant receptor revealed lower affinity for 11-ketotestosterone than for dihydrotestosterone. Treatment with different androgens did not up-regulate androgen receptor mRNA level or increase receptor abundance, suggesting that auto-regulation is not involved in differential ligand activation. However, comparison of the trans-activation potential of the stickleback androgen receptor with the human androgen receptor, in both human HepG2 cells and zebrafish ZFL cells, revealed preferential activation by 11-ketotestosterone of the stickleback receptor, but not of the human receptor. These findings demonstrate the presence of a receptor preferentially activated by 11-ketotestosterone in the three-spined stickleback, so far the only one known in any animal.

National Category
Biological Sciences
Research subject
Biology
Identifiers
urn:nbn:se:oru:diva-8835 (URN)10.1186/1477-7827-3-37 (DOI)16107211 (PubMedID)
Available from: 2009-12-18 Created: 2009-12-18 Last updated: 2017-10-18Bibliographically approved
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