cDNA Cloning of a Novel Androgen Receptor Subtype
There has been general acceptance that only one type of androgen receptor (AR) exists in an individual. This contrasts with other members of the nuclear receptor superfamily where multiple forms have been reported (e.g. estrogen receptor α/β, thyroid hormone receptor α/β, etc.). We have previously i...
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| Veröffentlicht in: | The Journal of biological chemistry 1999-09, Vol.274 (36), p.25205-25209 |
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| container_issue | 36 |
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| container_title | The Journal of biological chemistry |
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| creator | Ikeuchi, Toshitaka Todo, Takashi Kobayashi, Tohru Nagahama, Yoshitaka |
| description | There has been general acceptance that only one type of androgen receptor (AR) exists in an individual. This contrasts with other members of the nuclear receptor superfamily where multiple forms have been reported (e.g. estrogen receptor α/β, thyroid hormone receptor α/β, etc.). We have previously identified 11-ketotestosterone (a potent androgen in teleosts) as the spermatogenesis-inducing hormone of the Japanese eel and have cloned its receptor (eAR1) cDNA from eel testis. Here we report on the cloning of a cDNA encoding a second type of AR (eAR2) from the eel testis and the functional characterization of the encoded protein. This cDNA contains a complete open reading frame encoding 797 amino acid residues. The amino acid sequence of eAR2 shows high homology with other ARs, including eAR1, in the DNA-binding (98–88%) and ligand-binding (59–85%) domains, whereas the other domains show low homology ( |
| doi_str_mv | 10.1074/jbc.274.36.25205 |
| format | Article |
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This contrasts with other members of the nuclear receptor superfamily where multiple forms have been reported (e.g. estrogen receptor α/β, thyroid hormone receptor α/β, etc.). We have previously identified 11-ketotestosterone (a potent androgen in teleosts) as the spermatogenesis-inducing hormone of the Japanese eel and have cloned its receptor (eAR1) cDNA from eel testis. Here we report on the cloning of a cDNA encoding a second type of AR (eAR2) from the eel testis and the functional characterization of the encoded protein. This cDNA contains a complete open reading frame encoding 797 amino acid residues. The amino acid sequence of eAR2 shows high homology with other ARs, including eAR1, in the DNA-binding (98–88%) and ligand-binding (59–85%) domains, whereas the other domains show low homology (<35%). In transient transfection assays of mammalian cells, the eAR2 protein displayed androgen-dependent activation of transcription from the androgen-responsive murine mammary tumor virus promoter. Tissue distribution of its mRNA was different from that of eAR1. We conclude that eAR2 is a novel AR in the eel, which we suggest should be named eel ARβ to distinguish it from eAR1 (eARα).</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.274.36.25205</identifier><identifier>PMID: 10464240</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Anguilla ; Anguilla japonica ; Animals ; AR beta protein ; Base Sequence ; Brackish ; Cloning, Molecular ; DNA, Complementary - genetics ; DNA, Complementary - isolation & purification ; eAR2 protein ; Freshwater ; Male ; Marine ; Molecular Sequence Data ; Organ Specificity ; Receptors, Androgen - genetics ; RNA, Messenger - genetics ; Sequence Homology</subject><ispartof>The Journal of biological chemistry, 1999-09, Vol.274 (36), p.25205-25209</ispartof><rights>1999 © 1999 ASBMB. 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This contrasts with other members of the nuclear receptor superfamily where multiple forms have been reported (e.g. estrogen receptor α/β, thyroid hormone receptor α/β, etc.). We have previously identified 11-ketotestosterone (a potent androgen in teleosts) as the spermatogenesis-inducing hormone of the Japanese eel and have cloned its receptor (eAR1) cDNA from eel testis. Here we report on the cloning of a cDNA encoding a second type of AR (eAR2) from the eel testis and the functional characterization of the encoded protein. This cDNA contains a complete open reading frame encoding 797 amino acid residues. The amino acid sequence of eAR2 shows high homology with other ARs, including eAR1, in the DNA-binding (98–88%) and ligand-binding (59–85%) domains, whereas the other domains show low homology (<35%). In transient transfection assays of mammalian cells, the eAR2 protein displayed androgen-dependent activation of transcription from the androgen-responsive murine mammary tumor virus promoter. Tissue distribution of its mRNA was different from that of eAR1. 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In transient transfection assays of mammalian cells, the eAR2 protein displayed androgen-dependent activation of transcription from the androgen-responsive murine mammary tumor virus promoter. Tissue distribution of its mRNA was different from that of eAR1. We conclude that eAR2 is a novel AR in the eel, which we suggest should be named eel ARβ to distinguish it from eAR1 (eARα).</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10464240</pmid><doi>10.1074/jbc.274.36.25205</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Anguilla Anguilla japonica Animals AR beta protein Base Sequence Brackish Cloning, Molecular DNA, Complementary - genetics DNA, Complementary - isolation & purification eAR2 protein Freshwater Male Marine Molecular Sequence Data Organ Specificity Receptors, Androgen - genetics RNA, Messenger - genetics Sequence Homology |
| title | cDNA Cloning of a Novel Androgen Receptor Subtype |
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