Estrogen-inducible yolk precursors: Characterization of the multiple vitellogenin system in European sea bass (Dicentrachus labrax)
| Autor: | Yilmaz, Ozlem, Prat, Francisco, Ibáñez, Antonio José, Amano, Haruna, Sullivan, Craig V. |
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| Přispěvatelé: | Laboratoire de Physiologie et Génomique des Poissons (LPGP), Institut National de la Recherche Agronomique (INRA)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Institute of Marine Sciences of Andalusia, Universitat de València (UV), Kitasato University, Carolina AquaGyn, European Society of Endocrinology (ESE). GBR. |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: | |
| Zdroj: | 27. Conference of European Comparative Endocrinologists 27. Conference of European Comparative Endocrinologists, Aug 2014, Rennes, France. 2014, CECE 2014 CECE 2014. 2014; 27. Conference of European Comparative Endocrinologists, Rennes, FRA, 2014-08-25-2014-08-29, 153-153 Digital.CSIC. Repositorio Institucional del CSIC instname |
| Popis: | Trabajo presentado en la 27th Conference of European Comparative Endocrinologists (CECE 2014), celebrada en Rennes (Francia) del 25 al 29 de agosto de 2014. This study explored multiplicity of the estrogen-inducible yolk precursor protein, vitellogenin (Vtg), in the European sea bass (Sbs), a major aquaculture species and leading model in fish endocrinology. Three full-length Sbs vtg cDNAs were assembled from partial cDNAs that were cloned and sequenced from total RNA isolated from estradiol-induced male livers. Homology analyses of the deduced polypeptides via BLAST and ClustalW alignments with available Vtg sequences for teleosts from a broad array of taxa identified them as as Sbs VtgAa, VtgAb and VtgC. Analyses of conservation by Vtg-type of the key structural residues, cysteine (C), proline (P) and glycine (G) using Evotrace and their localization in the 3-D polypeptide structures modelled using Cn3D with a lamprey lipovitellin (Lv) template indicated that the N-sheet of the Lv domain of SbsVtgC, which bears the binding surface for the 'classical' Vtg receptor (Vtgr), has undergone massive alteration of its structure relative to the A-type Sbs Vtgs that may explain the limited Vtgr-binding reported for this form of Vtg. The presence and relative concentrations of each form of Sbs Vtg or product YP in postvitellogenic female liver, plasma and ovary were measured by nanoLC-MS/MS as ProteoIQ-normalized spectral counts. VtgAb tryptic peptide spectra were two- to several-fold more abundant than for the other Vtgs, and VtgC spectra were very limited except in ovary where they were a third of VtgAb spectral counts. Western blotting performed using antisera raised against purified grey mullet (Mugil cephalus) Lvs revealed limited degradation of all three forms of Lv during oocyte maturation, unlike the case in other marine pelagic spawners where only the LvAa undergoes almost complete proteolysis to free amino acids (FAA), which are important osmotic effectors of oocyte hydration and egg buoyancy. The nearly identical Vtgs and patterns of YP degradation during oocyte maturation in sea bass and Moronidae spawning demersal or pelagic eggs in freshwater indicate that Vtg system structure and function cannot be inferred solely from reproductive life history. |
| Databáze: | OpenAIRE |
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