Dicentrarchus Labrax): Molecular Characterization, Quantification in Plasma, Liver and Ovary, and Maturational Proteolysis
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Multiple vitellogenins and product yolk proteins in European sea bass (Dicentrarchus labrax): Molecular characterization, quantification in plasma, liver and ovary, and maturational proteolysis. Ozlem Yilmaz, Francisco Prat, A. Jose Ibáñez, Sadi Köksoy, Haruna Amano, Craig V. Sullivan To cite this version: Ozlem Yilmaz, Francisco Prat, A. Jose Ibáñez, Sadi Köksoy, Haruna Amano, et al.. Multiple vitel- logenins and product yolk proteins in European sea bass (Dicentrarchus labrax): Molecular char- acterization, quantification in plasma, liver and ovary, and maturational proteolysis.. Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology, Elsevier, 2016, 194-195, pp.71-86. 10.1016/j.cbpb.2015.11.010. hal-01303975 HAL Id: hal-01303975 https://hal.archives-ouvertes.fr/hal-01303975 Submitted on 27 May 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. ÔØ ÅÒÙ×Ö ÔØ Multiple vitellogenins and product yolk proteins in European sea bass (Dicentrarchus labrax): Molecular characterization, quantification in plasma, liver and ovary, and maturational proteolysis Ozlem Yilmaz, Francisco Prat, A. Jose Ib´a˜nez, Sadi K¨oksoy, Haruna Amano, Craig V. Sullivan PII: S1096-4959(15)00210-9 DOI: doi: 10.1016/j.cbpb.2015.11.010 Reference: CBB 9960 To appear in: Comparative Biochemistry and Physiology, Part B Received date: 7 May 2015 Revised date: 3 November 2015 Accepted date: 26 November 2015 Version preprint Version postprint Please cite this article as: Yilmaz, Ozlem, Prat, Francisco, Ib´a˜nez, A. Jose, K¨oksoy, Sadi, Amano, Haruna, Sullivan, Craig V., Multiple vitellogenins and product yolk proteins in European sea bass (Dicentrarchus labrax): Molecular characterization, quantification in plasma, liver and ovary, and maturational proteolysis, Comparative Biochemistry and Physiology, Part B (2015), doi: 10.1016/j.cbpb.2015.11.010 This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. Comment citer ce document : Yilmaz, O., Prat, F., Ibáñez, A. J., Köksoy, S., Amano, H., Sullivan, C. V. (2016). Multiple vitellogenins and product yolk proteins in European sea bass (Dicentrarchus labrax): Molecular characterization, quantification in plasma, liver and ovary, and maturational proteolysis. ComparativeComparative Biochemistry Biochemistry and Physiology and Physiology. B-Biochemistry Part B, Biochemistry & Molecular and Biology. Molecular DOI Biology,: 10.1016/j.cbpb.2015.11.010 194-195, 71-86. DOI : 10.1016/j.cbpb.2015.11.010 ACCEPTED MANUSCRIPT Multiple vitellogenins and product yolk proteins in European sea bass (Dicentrarchus labrax): Molecular characterization, quantification in plasma, liver and ovary, and maturational proteolysis. OZLEM YILMAZa*, FRANCISCO PRATb, A. JOSE IBÁÑEZc**, SADI KÖKSOYd, HARUNA e f*** AMANO , AND CRAIG V. SULLIVAN aAkdeniz University, Fisheries Faculty, Antalya, 07070, TURKEY bInstituto de Ciencias Marinas de Andalucía, Consejo Superior de Investigaciones Científicas, Avda. República Saharaui 2, 11510 Puerto Real, Cádiz, SPAIN cInstituto de Acuicultura de Torre de la Sal, Consejo Superior de Investigaciones Científicas, Torre de la Sal, s/n 12595, Ribera de Cabanes, Castellòn, SPAIN d Central Research and Immunology Laboratories, Akdeniz University, Faculty of Medicine, Antalya, 07070, TURKEY e School of Marine Biosciences, Kitasato University, 1-15-1 Kitasato, Minami, Sagamihara, Version preprint Version postprint Kanagawa 252-0373, JAPAN f Department of Biology, College of Agriculture and Life Sciences, North Carolina State University, Raleigh, NC 27695-7617, USA. * Present address: ACCEPTEDInstitut National de la Recherche MANUSCRIPT Agronomique, INRA-SCRIBE, IFR 140, Campus de Beaulieu, 35000 Rennes Cedex, FRANCE ** Present address: Electron and Confocal Microscopy Service, University of Valência – SCIE, Dr Moliner, 50-Research building, Lab-1.63, 46100 Burjassot-Urjassot, Valência, SPAIN *** Corresponding author and present address: Carolina AquaGyn, P.O. Box 12914, Raleigh, NC 27605, USA. Tel./Fax; 919-302-7888. Email: [email protected] Comment citer ce document : 1 Yilmaz, O., Prat, F., Ibáñez, A. J., Köksoy, S., Amano, H., Sullivan, C. V. (2016). Multiple vitellogenins and product yolk proteins in European sea bass (Dicentrarchus labrax): Molecular characterization, quantification in plasma, liver and ovary, and maturational proteolysis. ComparativeComparative Biochemistry Biochemistry and Physiology and Physiology. B-Biochemistry Part B, Biochemistry & Molecular and Biology. Molecular DOI Biology,: 10.1016/j.cbpb.2015.11.010 194-195, 71-86. DOI : 10.1016/j.cbpb.2015.11.010 ACCEPTED MANUSCRIPT ABSTRACT Three complete vitellogenin (Vtg) polypeptides of European sea bass (Dicentrarchus labrax), an acanthomorph teleost spawning pelagic eggs in seawater, were deduced from cDNA and identified as VtgAa, VtgAb and VtgC based on current Vtg nomenclature and phylogeny. Label free quantitative mass spectrometry verified the presence of the three sea bass Vtgs or their product yolk proteins (YPs) in liver, plasma and ovary of postvitellogenic females. As evidenced by normlized spectral counts, VtgAb-derived protein was 2- to 5-fold more abundant, depending on sample type, than for VtgAa, while VtgC-derived protein was less abundant, albeit only 3-fold lower than for VtgAb in the ovary. Western blotting with Vtg type-specific antisera raised against corresponding grey mullet (Mugil cephalus) lipovitellins (Lvs) detected all three types of sea bass Vtg in the blood plasma of gravid females and/or estrogenized males and showed that all three forms of sea bass Lv undergo limited partial degradation during oocyte maturation. The comparatively high levels of VtgC-derived YPs in fully-grown oocytes and the maturational proteolysis of all three types of Lv differ from what has been reported for other teleosts spawning pelagic eggs in seawater but are similar to recent findings for two species of North American Version preprint Version postprint Moronidae, the striped bass (Morone saxatilis) and white perch (M. americana), which spawn pelagic and demersal eggs, respectively in fresh water. Together with the high Vtg sequence homologies and virtually identical structural features of each type of Vtg between species, these findings indicate that the moronid multiple Vtg systems doACCEPTED not substantially vary with MANUSCRIPT reproductive environment. Keywords: Maturation, Molecular, Moronidae, Oocyte, Ovary, Teleost, Vitellogenin, Yolk Abbreviations: cathepsin (CAT), complementry DNA (cDNA), ethylenediaminetetraacetic acid (EDTA), free amino acids (FAA), oocyte maturation (OM), ovulated (OV), postvitellogenic (PV), reverse transcription - polymerase chain reaction (RT-PCR), sodiumdodecylsulfate polyacrylamide gel electrophoresis (SDS-PAGE), untranslated region (UTR), vitellogenin (Vtg), yolk protein (YP) Comment citer ce document : 2 Yilmaz, O., Prat, F., Ibáñez, A. J., Köksoy, S., Amano, H., Sullivan, C. V. (2016). Multiple vitellogenins and product yolk proteins in European sea bass (Dicentrarchus labrax): Molecular characterization, quantification in plasma, liver and ovary, and maturational proteolysis. ComparativeComparative Biochemistry Biochemistry and Physiology and Physiology. B-Biochemistry Part B, Biochemistry & Molecular and Biology. Molecular DOI Biology,: 10.1016/j.cbpb.2015.11.010 194-195, 71-86. DOI : 10.1016/j.cbpb.2015.11.010 ACCEPTED MANUSCRIPT 1. Introduction Vitellogenin (Vtg) is secreted by the liver, taken up by growing oocytes via receptor-mediated endocytosis, and cleaved into yolk proteins (YPs), which in teleosts include lipovitellin (Lv), phosvitin (Pv), ’component (’c), a C-terminal peptide (C-t), and various Lv-Pv complexes (reviews: Patiño and Sullivan 2002; Babin et al. 2007; Finn 2007ab; Reading and Sullivan 2011). The Lv, consisting of a heavy chain (LvH) and a light chain (LvL), is by far the largest YP and is heavily lipidated, delivering mainly phospholipids into growing oocytes (Romano et al. 2004; Johnson 2009). The diminutive Pv mainly consists of phosphorylated serine residues that are thought to stabilize nascent Vtg structure during lipid loading, enhance Vtg solubility, and enable Pv to bind calcium and other metabolically important cations for deposition into yolk (Finn 2007b). The β′c and C-t arise as cleavage products of a YP domain homologous to human von Willebrand factor type D (vWFD), which contains a highly conserved motif of repeated cysteine residues and has been postulated to stabilize the Vtg dimer, play a role in cellular recognition or receptor binding, and protect Vtg or its product YPs from premature proteolysis (Finn 2007b; Reading et al. 2009).