2015 journal article
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 B-BIOCHEMISTRY & MOLECULAR BIOLOGY, 194, 71–86.
author keywords: Maturation; Molecular; Moronidae; Oocyte; Ovary; Teleost; Vitellogenin; Yolk
MeSH headings : Animals; Aquaculture; Bass / blood; Bass / physiology; Egg Proteins / blood; Egg Proteins / chemistry; Egg Proteins / genetics; Egg Proteins / metabolism; Estradiol / pharmacology; Estrogens / pharmacology; Female; Gene Expression Regulation / drug effects; Liver / drug effects; Liver / metabolism; Male; Mediterranean Sea; Ovary / drug effects; Ovary / metabolism; Peptide Fragments / blood; Peptide Fragments / chemistry; Peptide Fragments / genetics; Peptide Fragments / metabolism; Phylogeny; Protein Isoforms / blood; Protein Isoforms / chemistry; Protein Isoforms / genetics; Protein Isoforms / metabolism; Protein Processing, Post-Translational / drug effects; Protein Sorting Signals / drug effects; Proteolysis / drug effects; Recombinant Proteins / chemistry; Recombinant Proteins / metabolism; Terminology as Topic; Vitellogenesis / drug effects; Vitellogenins / blood; Vitellogenins / chemistry; Vitellogenins / genetics; Vitellogenins / metabolism
TL;DR:
Findings indicate that the moronid multiple Vtg systems do not substantially vary with reproductive environment and all three forms of sea bass Lv undergo limited partial degradation during oocyte maturation.
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UN Sustainable Development Goal Categories
14. Life Below Water
(Web of Science; OpenAlex)
Source: Web Of Science
Added: August 6, 2018
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 normalized 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 gray 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 Moronidae, the striped bass (Morone saxatilis) and white perch (Morone 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 do not substantially vary with reproductive environment.