{"refrec":{"BRefID":205941,"RR":"<b>Verhaegen, Y.; Parmentier, K.; Swevers, L.; Renders, E.; Rougé, P.; De Coen, W.; Cooreman, K.; Smagghe, G.</b> (2011). The heterodimeric ecdysteroid receptor complex in the brown shrimp <i>Crangon crangon</i>: EcR and RXR isoform characteristics and sensitivity towards the marine pollutant tributyltin. <i>Gen. Comp. Endocrinol. 172(1)</i>: 158-169. <a href=\"https://dx.doi.org/10.1016/j.ygcen.2011.02.019\" target=\"_blank\">https://dx.doi.org/10.1016/j.ygcen.2011.02.019</a>","BEntID":198053,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Gen. Comp. Endocrinol. 172(1)</i>: 158-169. <a href=\"https://dx.doi.org/10.1016/j.ygcen.2011.02.019\" target=\"_blank\">https://dx.doi.org/10.1016/j.ygcen.2011.02.019</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Verhaegen, Y.; Parmentier, K.; Swevers, L.; Renders, E.; Rougé, P.; De Coen, W.; Cooreman, K.; Smagghe, G.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Verhaegen, Y. <i>et al.</i>","Englishabstract":"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 <i>C. crangon</i> we cloned <i>C</i>-terminally truncated CrcEcR and CrcRXR isoforms and isoforms exhibiting deletions within the hinge region. For the former, <i>in silico</i> modeling of the CrcEcR indicated that, where the conserved helices H10 and H11 of the ligand-binding domain (LBD) are missing, an alternative <i>C</i>-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 <i>in vitro</i> 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 <i>in vitro</i> 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. <i>In silico</i> modeling confirmed that TBT fits in the full-length CrcRXR–LBD. Furthermore, semi-quantitative PCR indicated altered expression of CrcEcR and CrcRXR isoforms after <i>in vivo</i> acute exposure to TBT, especially in the ovaries.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"The heterodimeric ecdysteroid receptor complex in the brown shrimp <i>Crangon crangon</i>: EcR and RXR isoform characteristics and sensitivity towards the marine pollutant tributyltin","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:33:17.368041","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Crangon crangon; Shrimp; Crustacea; Tributyltin; TBT;Retinoid-X-receptor; RXR; Ecdysteroid receptor; EcR","OtherDescriptors":null,"Notes":null,"AnaPub":2011,"MonPub":null,"DateUpdate":"2019-06-25","DateCreate":"2011-06-17","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000290842200022","VABBcode":null,"OpenAcc":0,"DOI":"10.1016/j.ygcen.2011.02.019"},"refs":null,"anarec":{"AnaID":205941,"PubliDate":2011,"Pagination":"158-169","XtraPublOfAnaID":null,"ISBN":null,"Volume":"172","Issue":"1","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":42729,"SerRR":"General and Comparative Endocrinology. 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