Marine Biodiversity and Ecosystem Functioning
EU Network of Excellence

 
Main Menu

· Home
· Contacts
· Data Systems
· Documents
· FAQ
· Links
· MarBEF Open Archive
· Network Description
· Outreach
· Photo Gallery
· Quality Assurance
· Register of Resources
· Research Projects
· Rules and Guidelines
· Training
· Wiki
· Worldconference

 

Register of Resources (RoR)

 People  |  Datasets  |  Literature  |  Institutes  |  Projects 

[ report an error in this record ]basket (0): add | show Print this page

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
Peer reviewed article  

Available in  Authors 

Keywords
    Cells > Receptors
    Ecdysteroids
    Tributyltin
    Vitamins > Fat soluble vitamins > Carotenoids > Retinoids
    Crangon crangon (Linnaeus, 1758) [WoRMS]; Crustacea [WoRMS]
    Marine/Coastal
Author keywords
    Crangon crangon; Shrimp; Crustacea; Tributyltin; TBT;Retinoid-X-receptor; RXR; Ecdysteroid receptor; EcR

Authors  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.

All data in the Integrated Marine Information System (IMIS) is subject to the VLIZ privacy policy Top | Authors 


If any information here appears to be incorrect, please contact us
Back to Register of Resources
 
Quick links

MarBEF WIKI

Erasmus Mundus Master of Science in Marine Biodiversity and Conservation (EMBC)
Outreach

Science
Responsive Mode Programme (RMP) - Marie Nordstrom, copyright Aspden Rebecca

WoRMS
part of WoRMS logo

ERMS 2.0
Epinephelus marginatus Picture: JG Harmelin

EurOBIS

Geographic System

Datasets

 


Web site hosted and maintained by Flanders Marine Institute (VLIZ) - Contact data-at-marbef.org