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Molecular cloning and characterization of the corticoid receptors from the American alligator

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Title: Molecular cloning and characterization of the corticoid receptors from the American alligator
Authors: Oka, Kaori Browse this author
Kohno, Satomi Browse this author
Urushitani, Hiroshi Browse this author
Guillette, Louis J., Jr. Browse this author
Ohta, Yasuhiko Browse this author
Iguchi, Taisen Browse this author
Katsu, Yoshinao Browse this author →KAKEN DB
Keywords: Alligator
Glucocorticoid receptor
Mineralocorticoid receptor
Issue Date: 30-Jan-2013
Publisher: Elsevier Ireland
Journal Title: Molecular and Cellular Endocrinology
Volume: 365
Issue: 2
Start Page: 153
End Page: 161
Publisher DOI: 10.1016/j.mce.2012.10.014
PMID: 23127802
Abstract: Steroid hormones are essential for health in vertebrates. Corticosteroids, for example, have a regulatory role in many physiological functions, such as osmoregulation, respiration, immune responses, stress responses, reproduction, growth, and metabolism. Although extensively studied in mammals and some non-mammalian species, the molecular mechanisms of corticosteroid hormone (glucocorticoids and mineralocorticoids) action are poorly understood in reptiles. Here, we have evaluated hormone receptor-ligand interactions in the American alligator (Alligator mississippiensis), following the isolation of cDNAs encoding a glucocorticoid receptor (GR) and a mineralocorticoid receptor (MR). The full-length alligator GR (aGR) and aMR cDNAs were obtained using 5' and 3' rapid amplification cDNA ends (RACE). The deduced amino acid sequences exhibited high identity to the chicken orthologs (aGR: 83%; aMR: 90%). Using transient transfection assays of mammalian cells, both aGR and aMR proteins displayed corticosteroid-dependent activation of transcription from keto-steroid hormone responsive, murine mammary tumor virus promoters. We further compared the ligand-specifity of human, chicken, Xenopus, and zebrafish GR and MR. We found that the alligator and chicken GR/MR have very similar amino acid sequences, and this translates to very similar ligand specificity. This is the first report of the full-coding regions of a reptilian GR and MR, and the examination of their transactivation by steroid hormones.
Type: article (author version)
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 勝 義直

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