Zoeken
Zoeken kan via de modus 'eenvoudig zoeken' (één veld) of uitgebreid via 'geavanceerd zoeken' (meerdere velden). Zo kan je bv. zoeken op een combinatie van een auteursnaam (auteur), een jaartal (jaar) en een documenttype.
Boekenmand
Nuttige resultaten kan je aanvinken en toevoegen aan een mandje. De inhoud hiervan kan je exporteren of afdrukken (naar bv. PDF).
RSS
Op de hoogte blijven van nieuw toegevoegde publicaties binnen uw interessegebied? Dit kan door een RSS-feed (?) te maken van jouw zoekopdracht.
nieuwe zoekopdracht
| one publication added to basket [205941] |
The heterodimeric ecdysteroid receptor complex in the brown shrimp Crangon crangon: EcR and RXR isoform characteristics and sensitivity towards the marine pollutant tributyltin
Verhaegen, Y.; Parmentier, K.; Swevers, L.; Renders, E.; Rougé, P.; De Coen, W.; Cooreman, K.; Smagghe, G. (2011). The heterodimeric ecdysteroid receptor complex in the brown shrimp Crangon crangon: EcR and RXR isoform characteristics and sensitivity towards the marine pollutant tributyltin. Gen. Comp. Endocrinol. 172(1): 158-169. https://dx.doi.org/10.1016/j.ygcen.2011.02.019
In: General and Comparative Endocrinology. Elsevier: New York,. ISSN 0016-6480; e-ISSN 1095-6840
|  |
| Trefwoorden |
Cells > Receptors
Ecdysteroids
Tributyltin
Vitamins > Fat soluble vitamins > Carotenoids > Retinoids
Crangon crangon (Linnaeus, 1758) [WoRMS]; Crustacea [WoRMS]
Marien/Kust |
| Author keywords |
Crangon crangon; Shrimp; Crustacea; Tributyltin; TBT;Retinoid-X-receptor; RXR; Ecdysteroid receptor; EcR |
| Auteurs | | Top |
- Verhaegen, Y.
- Parmentier, K.
- Swevers, L.
- Renders, E.
|
- Rougé, P.
- De Coen, W.
- Cooreman, K.
- Smagghe, G.
|
|
| Abstract |
Decapod crustaceans are characterized by multiple ecdysteroid receptor (EcR) and retinoid-X-receptor (RXR) isoforms, which likely exhibit variant dimerization and transactivation interactions. In the brown shrimp C. crangon we cloned C-terminally truncated CrcEcR and CrcRXR isoforms and isoforms exhibiting deletions within the hinge region. For the former, in silico modeling of the CrcEcR indicated that, where the conserved helices H10 and H11 of the ligand-binding domain (LBD) are missing, an alternative C-terminal a-helix repairs the ligand-binding pocket (LBP). The truncated CrcRXR isoforms lack a major part of the LBD (H4–H12), thereby compromising ligand binding and dimerization. Through an in vitro ecdysteroid responsive reporter assay, we showed that these natural receptor variations do not impair receptor functioning but probably alter the receptor dimerization preferences. By the same in vitro assay, using full-length CrcEcR and CrcRXR, the effect of tributyltin (TBT) on ecdysteroid-induced transactivation was evaluated. The transactivation by 10 nM PonA was reduced with 64% by 20 nM TBT. In silico modeling confirmed that TBT fits in the full-length CrcRXR–LBD. Furthermore, semi-quantitative PCR indicated altered expression of CrcEcR and CrcRXR isoforms after in vivo acute exposure to TBT, especially in the ovaries. |
IMIS is ontwikkeld en wordt gehost door het VLIZ.
