PUBLICATION
Characterization of the zebrafish (Danio rerio) mineralocorticoid receptor
- Authors
- Pippal, J.B., Cheung, C.M., Yao, Y.Z., Brennan, F.E., and Fuller, P.J.
- ID
- ZDB-PUB-101018-10
- Date
- 2011
- Source
- Molecular and Cellular Endocrinology 332(1-2): 58-66 (Journal)
- Registered Authors
- Keywords
- Ligand-binding, Deoxycorticosterone, Aldosterone, Receptor
- MeSH Terms
-
- Nimodipine/metabolism
- Nimodipine/pharmacology
- Spironolactone/metabolism
- Spironolactone/pharmacology
- Sequence Alignment
- Antihypertensive Agents/metabolism
- Antihypertensive Agents/pharmacology
- Desoxycorticosterone/metabolism
- Desoxycorticosterone/pharmacology
- Molecular Sequence Data
- Cell Line
- Sequence Analysis, DNA
- Aldosterone/metabolism
- Aldosterone/pharmacology
- Mineralocorticoid Receptor Antagonists/metabolism
- Mineralocorticoid Receptor Antagonists/pharmacology
- Zebrafish/anatomy & histology
- Zebrafish/genetics
- Zebrafish/metabolism*
- Amino Acid Sequence
- Animals
- Humans
- Hydrocortisone/metabolism
- Hydrocortisone/pharmacology
- Receptors, Mineralocorticoid/agonists
- Receptors, Mineralocorticoid/genetics
- Receptors, Mineralocorticoid/metabolism*
- Transcriptional Activation/drug effects
- PubMed
- 20932876 Full text @ Mol. Cell. Endocrinol.
Citation
Pippal, J.B., Cheung, C.M., Yao, Y.Z., Brennan, F.E., and Fuller, P.J. (2011) Characterization of the zebrafish (Danio rerio) mineralocorticoid receptor. Molecular and Cellular Endocrinology. 332(1-2):58-66.
Abstract
Comparison between evolutionarily distant receptors can provide critical insights into both structure and function. Sequence comparison between the mineralocorticoid receptors (MR) of the zebrafish (zMR) and human (hMR) reveal a high degree of sequence conservation in the major functional domains. We isolated a zMR cDNA to contrast the transcriptional response to a range of ligands and to establish whether a teleost MR exhibits the amino/carboxyl-terminal interaction (N/C-interaction) previously reported for the hMR. Aldosterone, deoxycorticosterone (DOC) and cortisol induced zMR transcriptional activity with similar efficacy to that observed with the hMR. The hMR antagonist, spironolactone, acted as an agonist with the zMR. The zMR exhibited an N/C-interaction in response to aldosterone but, in contrast to the hMR, cortisol and DOC predominantly stimulated the interaction in the zMR. Conservation of the N/C-interaction between evolutionarily distant MR provides evidence of functional significance.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping