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Craig V Sullivan - One of the best experts on this subject based on the ideXlab platform.
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vitellogenesis and Yolk Proteins fish
2016Co-Authors: Craig V Sullivan, Ozlem YilmazAbstract:Vitellogenin is the dominant contributor to vertebrate egg Yolk. All fishes produce vitellogenins as crucial embryonic nutrients. During oogenesis, oocytes grow by orders of magnitude while vitellogenin delivers to their ooplasm most of the materials needed to build and sustain a new life. The past 20 years have seen major advances in our understanding of the multiplicity, evolution, structure and functions of fish vitellogenins and their receptors, especially from a molecular perspective and with a view toward utilization of the knowledge for the betterment of finfish aquaculture, fisheries management and biomedical research. The present article covers these fascinating developments.
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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.
Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology, 2016Co-Authors: Ozlem Yilmaz, Haruna Amano, Francisco Prat, A. Jose Ibáñez, Sadi Köksoy, Craig V SullivanAbstract: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.
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Ovarian Yolk formation in fishes: Molecular mechanisms underlying formation of lipid droplets and vitellogenin-derived Yolk Proteins
General and Comparative Endocrinology, 2015Co-Authors: Naoshi Hiramatsu, Craig V Sullivan, Takahiro Matsubara, Benjamin J. Reading, Takashi Todo, Justin Schilling, Yong-woon Ryu, Hiroko Mizuta, Wenshu Luo, Osamu NishimiyaAbstract:Fish egg Yolk is largely derived from vitellogenins, which are synthesized in the liver, taken up from the maternal circulation by growing oocytes via receptor-mediated endocytosis and enzymatically processed into Yolk Proteins that are stored in the ooplasm. Lipid droplets are another major component of fish egg Yolk, and these are mainly composed of neutral lipids that may originate from maternal plasma lipoProteins. This review aims to briefly summarize our current understanding of the molecular mechanisms underlying Yolk formation in fishes. A hypothetical model of oocyte growth is proposed based on recent advances in our knowledge of fish Yolk formation.
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proportional accumulation of Yolk Proteins derived from multiple vitellogenins is precisely regulated during vitellogenesis in striped bass morone saxatilis
Journal of Experimental Zoology, 2014Co-Authors: Valerie N. Williams, Naoshi Hiramatsu, Benjamin J. Reading, Haruna Amano, Justin Schilling, Scott A Salger, Taufika Islam Williams, Kevin Gross, Craig V SullivanAbstract:We quantified three vitellogenins (VtgAa, VtgAb, VtgC) or their derived Yolk Proteins (YPs) in the liver, plasma, and ovary during pre-vitellogenic (PreVG), mid-vitellogenic (MVG), and late- vitellogenic (LVG) oocyte growth and during post-vitellogenesis (PostVG) in the striped bass (Morone saxatilis) using label-free quantitative mass spectrometry (MS). Western blotting of the samples using antisera raised against gray mullet (Mugil cephalus) lipovitellins derived from VtgAa, VtgAb, and VtgC confirmed the MS results. Semi-quantitative reverse transcription polymerase chainreaction(RT-PCR)revealedliverastheprimarysiteofexpressionforallthreeVtgs,withextra- hepatictranscription weaklydetectedinovary,foregut,adiposetissue,andbrain.Quantitativereal- time RT-PCR confirmed vtgAb to be primarily expressed in liver and VtgAb Proteins were predominant in liver and plasma from MVG to PostVG. However, the primary period of deposition into oocytes of VtgAb occurred up until MVG, whereas VtgAa was primarily deposited from MVG to LVG. The VtgC was gradually taken up by oocytes throughout vitellogenesis and was detected at trace levels in plasma. The ratio of Yolk Proteins derived from VtgAa, VtgAb, VtgC (YPAa/YPAb/YPC) in PostVG ovary is 1.4:1.4:1, which differs from ratios previously reported for other fish species in that YPC comprises a greater proportion of the egg Yolk. Our results indicate that proportional accumulation of multiple Vtgs in the Yolk may depend both on the precise rates of their hepatic secretion and specific uptake by oocytes. Furthermore, composition of the Vtg-derived Yolk may vary among Acanthomorph fishes, perhaps reflecting their different early life histories and reproductive strategies. J. Exp. Zool. 9999A: 1-15, 2014. © 2014 Wiley Periodicals, Inc.
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Multiple vitellogenins and product Yolk Proteins in striped bass, Morone saxatilis: molecular characterization and processing during oocyte growth and maturation
Fish physiology and biochemistry, 2013Co-Authors: Valerie N. Williams, Akihiko Hara, Naoshi Hiramatsu, Benjamin J. Reading, Haruna Amano, Norman J. Glassbrook, Craig V SullivanAbstract:The multiple vitellogenin (Vtg) system of striped bass, a perciform species spawning nearly neutrally buoyant eggs in freshwater, was investigated. Vitellogenin cDNA cloning, Western blotting of Yolk Proteins (YPs) using Vtg and YP type-specific antisera, and tandem mass spectrometry (MS/MS) of the YPs revealed the complex mechanisms of Yolk formation and maturation in this species. It was discovered that striped bass possesses a tripartite Vtg system (VtgAa, VtgAb, and VtgC) in which all three forms of Vtg make a substantial contribution to the Yolk. The production of Vtg-derived YPs is generally similar to that described for other perciforms. However, novel amino-terminal labeling of oocyte YPs prior to MS/MS identified multiple alternative sites for cleavage of these Proteins from their parent Vtg, revealing a YP mixture far more complex than reported previously. This approach also revealed that the major YP product of each form of striped bass Vtg, lipovitellin heavy chain (LvH), undergoes limited degradation to smaller polypeptides during oocyte maturation, unlike the case in marine fishes spawning buoyant eggs in which LvHAa undergoes extensive proteolysis to osmotically active free amino acids. These differences likely reflect the lesser need for hydration of pelagic eggs spawned in freshwater. The detailed characterization of Vtgs and their proteolytic fate(s) during oocyte growth and maturation establishes striped bass as a freshwater model for investigating teleost multiple Vtg systems.
Naoshi Hiramatsu - One of the best experts on this subject based on the ideXlab platform.
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Ovarian Yolk formation in fishes: Molecular mechanisms underlying formation of lipid droplets and vitellogenin-derived Yolk Proteins
General and Comparative Endocrinology, 2015Co-Authors: Naoshi Hiramatsu, Craig V Sullivan, Takahiro Matsubara, Benjamin J. Reading, Takashi Todo, Justin Schilling, Yong-woon Ryu, Hiroko Mizuta, Wenshu Luo, Osamu NishimiyaAbstract:Fish egg Yolk is largely derived from vitellogenins, which are synthesized in the liver, taken up from the maternal circulation by growing oocytes via receptor-mediated endocytosis and enzymatically processed into Yolk Proteins that are stored in the ooplasm. Lipid droplets are another major component of fish egg Yolk, and these are mainly composed of neutral lipids that may originate from maternal plasma lipoProteins. This review aims to briefly summarize our current understanding of the molecular mechanisms underlying Yolk formation in fishes. A hypothetical model of oocyte growth is proposed based on recent advances in our knowledge of fish Yolk formation.
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proportional accumulation of Yolk Proteins derived from multiple vitellogenins is precisely regulated during vitellogenesis in striped bass morone saxatilis
Journal of Experimental Zoology, 2014Co-Authors: Valerie N. Williams, Naoshi Hiramatsu, Benjamin J. Reading, Haruna Amano, Justin Schilling, Scott A Salger, Taufika Islam Williams, Kevin Gross, Craig V SullivanAbstract:We quantified three vitellogenins (VtgAa, VtgAb, VtgC) or their derived Yolk Proteins (YPs) in the liver, plasma, and ovary during pre-vitellogenic (PreVG), mid-vitellogenic (MVG), and late- vitellogenic (LVG) oocyte growth and during post-vitellogenesis (PostVG) in the striped bass (Morone saxatilis) using label-free quantitative mass spectrometry (MS). Western blotting of the samples using antisera raised against gray mullet (Mugil cephalus) lipovitellins derived from VtgAa, VtgAb, and VtgC confirmed the MS results. Semi-quantitative reverse transcription polymerase chainreaction(RT-PCR)revealedliverastheprimarysiteofexpressionforallthreeVtgs,withextra- hepatictranscription weaklydetectedinovary,foregut,adiposetissue,andbrain.Quantitativereal- time RT-PCR confirmed vtgAb to be primarily expressed in liver and VtgAb Proteins were predominant in liver and plasma from MVG to PostVG. However, the primary period of deposition into oocytes of VtgAb occurred up until MVG, whereas VtgAa was primarily deposited from MVG to LVG. The VtgC was gradually taken up by oocytes throughout vitellogenesis and was detected at trace levels in plasma. The ratio of Yolk Proteins derived from VtgAa, VtgAb, VtgC (YPAa/YPAb/YPC) in PostVG ovary is 1.4:1.4:1, which differs from ratios previously reported for other fish species in that YPC comprises a greater proportion of the egg Yolk. Our results indicate that proportional accumulation of multiple Vtgs in the Yolk may depend both on the precise rates of their hepatic secretion and specific uptake by oocytes. Furthermore, composition of the Vtg-derived Yolk may vary among Acanthomorph fishes, perhaps reflecting their different early life histories and reproductive strategies. J. Exp. Zool. 9999A: 1-15, 2014. © 2014 Wiley Periodicals, Inc.
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Multiple vitellogenins and product Yolk Proteins in striped bass, Morone saxatilis: molecular characterization and processing during oocyte growth and maturation
Fish physiology and biochemistry, 2013Co-Authors: Valerie N. Williams, Akihiko Hara, Naoshi Hiramatsu, Benjamin J. Reading, Haruna Amano, Norman J. Glassbrook, Craig V SullivanAbstract:The multiple vitellogenin (Vtg) system of striped bass, a perciform species spawning nearly neutrally buoyant eggs in freshwater, was investigated. Vitellogenin cDNA cloning, Western blotting of Yolk Proteins (YPs) using Vtg and YP type-specific antisera, and tandem mass spectrometry (MS/MS) of the YPs revealed the complex mechanisms of Yolk formation and maturation in this species. It was discovered that striped bass possesses a tripartite Vtg system (VtgAa, VtgAb, and VtgC) in which all three forms of Vtg make a substantial contribution to the Yolk. The production of Vtg-derived YPs is generally similar to that described for other perciforms. However, novel amino-terminal labeling of oocyte YPs prior to MS/MS identified multiple alternative sites for cleavage of these Proteins from their parent Vtg, revealing a YP mixture far more complex than reported previously. This approach also revealed that the major YP product of each form of striped bass Vtg, lipovitellin heavy chain (LvH), undergoes limited degradation to smaller polypeptides during oocyte maturation, unlike the case in marine fishes spawning buoyant eggs in which LvHAa undergoes extensive proteolysis to osmotically active free amino acids. These differences likely reflect the lesser need for hydration of pelagic eggs spawned in freshwater. The detailed characterization of Vtgs and their proteolytic fate(s) during oocyte growth and maturation establishes striped bass as a freshwater model for investigating teleost multiple Vtg systems.
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characterization of vitellogenin and its derived Yolk Proteins in cloudy catshark scyliorhinus torazame
Fish Physiology and Biochemistry, 2012Co-Authors: Kodai Yamane, Naoshi Hiramatsu, Takahiro Matsubara, Haruna Amano, Tomoki Yagai, Osamu Nishimiya, Rieko Sugawara, Toshiaki Fujita, Takashi Todo, Akihiko HaraAbstract:Elasmobranchs (sharks and rays) exhibit unique reproductive characteristics and, in contrast to the situation in teleosts, very little is known about the identity, structure and physical characteristics of their egg Yolk Proteins. The aims of this study were to (1) detect and purify the vitellogenin (Vtg; egg Yolk precursor) and Yolk Proteins (YPs) of the cloudy catshark (Scyliorhinus torazame), (2) examine the relationships between Vtg and YPs and (3) characterize and classify the deduced primary structure of the Vtg transcript (vtg). The apparent molecular weights of purified Vtg and putative Vtg-related YPs (lipovitellin: Lv, phosvitin: Pv) were determined by gel filtration and were ~560, >669 and ~58 kDa, respectively. Following SDS-PAGE, these purified products (i.e., Vtg, Lv and Pv) appeared as bands of ~210, ~110 and ~22 kDa, respectively. On Western blots, antisera against purified Vtg, Lv and Pv recognized the ~210 kDa Vtg band. Catshark Pv, in contrast to teleost Pvs, had a very low serine content. The catshark Vtg cDNA sequence (vtg) appeared to contain an open-reading frame consisting of domains encoding Lv, Pv and β′-component (β′-c). A phylogenetic analysis, with a consideration of genome duplication events, placed catshark vtg into the ‘vtgAB type.’ It is concluded that at least a single major type of Vtg protein, which is transcribed and translated from catshark vtgAB gene, is the precursor of three egg Yolk Proteins (Lv, Pv and β′-c) in catshark.
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Conserved and Variant Molecular and Functional Features of Multiple Egg Yolk Precursor Proteins (Vitellogenins) in White Perch (Morone americana) and other Teleosts
Marine Biotechnology, 2008Co-Authors: Benjamin J. Reading, Akihiko Hara, Naoshi Hiramatsu, Sayumi Sawaguchi, Takahiro Matsubara, Mark O. LivelyAbstract:Three complete cDNAs encoding different forms of vitellogenin (Vtg) were isolated from a white perch ( Morone americana ) liver cDNA library and characterized with respect to immunobiochemical and functional features of the three Vtgs and their product Yolk Proteins (YPs) in this species and in the congeneric striped bass ( Morone saxatilis ). The two longest cDNAs encoded Vtgs with a complete suite of Yolk protein domains that, based on comparisons with vtg sequences from other species, were categorized as VtgAa and VtgAb using the current nomenclature for multiple teleost Vtgs. The shorter cDNA encoded a Vtg that lacked a phosvitin domain, had a shortened C-terminus, and was categorized as VtgC. Mapping of peptide sequences from the purified Vtgs and their derived YPs to Vtg sequences deduced from the cDNAs definitively identified the white perch VtgAa, VtgAb, and VtgC Proteins. Detailed comparisons of the primary structures of each Vtg with partial or complete sequences of Morone Yolk Proteins or of Vtgs from other fishes revealed conserved and variant structural elements of teleost Vtgs with functional significance, including, as examples, signal peptide cleavage sites, dimerization sites, cathepsin D protease recognition sites, and receptor-binding domains. These comparisons also yielded an interim revision of the classification scheme for multiple teleost Vtgs.
Akihiko Hara - One of the best experts on this subject based on the ideXlab platform.
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Multiple vitellogenins and product Yolk Proteins in striped bass, Morone saxatilis: molecular characterization and processing during oocyte growth and maturation
Fish physiology and biochemistry, 2013Co-Authors: Valerie N. Williams, Akihiko Hara, Naoshi Hiramatsu, Benjamin J. Reading, Haruna Amano, Norman J. Glassbrook, Craig V SullivanAbstract:The multiple vitellogenin (Vtg) system of striped bass, a perciform species spawning nearly neutrally buoyant eggs in freshwater, was investigated. Vitellogenin cDNA cloning, Western blotting of Yolk Proteins (YPs) using Vtg and YP type-specific antisera, and tandem mass spectrometry (MS/MS) of the YPs revealed the complex mechanisms of Yolk formation and maturation in this species. It was discovered that striped bass possesses a tripartite Vtg system (VtgAa, VtgAb, and VtgC) in which all three forms of Vtg make a substantial contribution to the Yolk. The production of Vtg-derived YPs is generally similar to that described for other perciforms. However, novel amino-terminal labeling of oocyte YPs prior to MS/MS identified multiple alternative sites for cleavage of these Proteins from their parent Vtg, revealing a YP mixture far more complex than reported previously. This approach also revealed that the major YP product of each form of striped bass Vtg, lipovitellin heavy chain (LvH), undergoes limited degradation to smaller polypeptides during oocyte maturation, unlike the case in marine fishes spawning buoyant eggs in which LvHAa undergoes extensive proteolysis to osmotically active free amino acids. These differences likely reflect the lesser need for hydration of pelagic eggs spawned in freshwater. The detailed characterization of Vtgs and their proteolytic fate(s) during oocyte growth and maturation establishes striped bass as a freshwater model for investigating teleost multiple Vtg systems.
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characterization of vitellogenin and its derived Yolk Proteins in cloudy catshark scyliorhinus torazame
Fish Physiology and Biochemistry, 2012Co-Authors: Kodai Yamane, Naoshi Hiramatsu, Takahiro Matsubara, Haruna Amano, Tomoki Yagai, Osamu Nishimiya, Rieko Sugawara, Toshiaki Fujita, Takashi Todo, Akihiko HaraAbstract:Elasmobranchs (sharks and rays) exhibit unique reproductive characteristics and, in contrast to the situation in teleosts, very little is known about the identity, structure and physical characteristics of their egg Yolk Proteins. The aims of this study were to (1) detect and purify the vitellogenin (Vtg; egg Yolk precursor) and Yolk Proteins (YPs) of the cloudy catshark (Scyliorhinus torazame), (2) examine the relationships between Vtg and YPs and (3) characterize and classify the deduced primary structure of the Vtg transcript (vtg). The apparent molecular weights of purified Vtg and putative Vtg-related YPs (lipovitellin: Lv, phosvitin: Pv) were determined by gel filtration and were ~560, >669 and ~58 kDa, respectively. Following SDS-PAGE, these purified products (i.e., Vtg, Lv and Pv) appeared as bands of ~210, ~110 and ~22 kDa, respectively. On Western blots, antisera against purified Vtg, Lv and Pv recognized the ~210 kDa Vtg band. Catshark Pv, in contrast to teleost Pvs, had a very low serine content. The catshark Vtg cDNA sequence (vtg) appeared to contain an open-reading frame consisting of domains encoding Lv, Pv and β′-component (β′-c). A phylogenetic analysis, with a consideration of genome duplication events, placed catshark vtg into the ‘vtgAB type.’ It is concluded that at least a single major type of Vtg protein, which is transcribed and translated from catshark vtgAB gene, is the precursor of three egg Yolk Proteins (Lv, Pv and β′-c) in catshark.
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Conserved and Variant Molecular and Functional Features of Multiple Egg Yolk Precursor Proteins (Vitellogenins) in White Perch (Morone americana) and other Teleosts
Marine Biotechnology, 2008Co-Authors: Benjamin J. Reading, Akihiko Hara, Naoshi Hiramatsu, Sayumi Sawaguchi, Takahiro Matsubara, Mark O. LivelyAbstract:Three complete cDNAs encoding different forms of vitellogenin (Vtg) were isolated from a white perch ( Morone americana ) liver cDNA library and characterized with respect to immunobiochemical and functional features of the three Vtgs and their product Yolk Proteins (YPs) in this species and in the congeneric striped bass ( Morone saxatilis ). The two longest cDNAs encoded Vtgs with a complete suite of Yolk protein domains that, based on comparisons with vtg sequences from other species, were categorized as VtgAa and VtgAb using the current nomenclature for multiple teleost Vtgs. The shorter cDNA encoded a Vtg that lacked a phosvitin domain, had a shortened C-terminus, and was categorized as VtgC. Mapping of peptide sequences from the purified Vtgs and their derived YPs to Vtg sequences deduced from the cDNAs definitively identified the white perch VtgAa, VtgAb, and VtgC Proteins. Detailed comparisons of the primary structures of each Vtg with partial or complete sequences of Morone Yolk Proteins or of Vtgs from other fishes revealed conserved and variant structural elements of teleost Vtgs with functional significance, including, as examples, signal peptide cleavage sites, dimerization sites, cathepsin D protease recognition sites, and receptor-binding domains. These comparisons also yielded an interim revision of the classification scheme for multiple teleost Vtgs.
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multiple vitellogenin derived Yolk Proteins in gray mullet mugil cephalus disparate proteolytic patterns associated with ovarian follicle maturation
Molecular Reproduction and Development, 2008Co-Authors: Haruna Amano, Naoshi Hiramatsu, Craig V Sullivan, Takahiro Matsubara, Toshiaki Fujita, Hirohiko Kagawa, Akihiko HaraAbstract:Disparate proteolytic patterns of Yolk Proteins, derived from three types of vitellogenin (VgA, VgB, and VgC), were observed in gray mullet. Immuno-biochemical analyses of extracts obtained from vitellogenic ovaries (VO) and ovulated eggs (OE) confirmed that a large proportion of VgA-derived lipovitellin (LvA) was degraded into free amino acids (FAAs) during ovarian follicle maturation. The maturation-associated alteration of VgB-derived Lv (LvB) involved only limited proteolysis; the heavy and light LvB chains were dissociated into at least three and one polypeptide fragments, respectively. The native mass of VgC-derived Lv (LvC) exhibited little difference between VO and OE, although it was apparent that the LvC was 'nicked' during maturation, resulting in the appearance of several bands in OE. Similar analyses confirmed that VgA-derived beta'-component (beta'-cA) and VgB-derived beta'-c (beta'-cB) decreased during maturation in both quantity and native mass, while phosvitin derived from either VgA (PvA) or VgB (PvB) appeared to be degraded into FAAs. The pattern of maturation-associated proteolysis of mullet Yolk Proteins is similar to that reported for other marine teleosts spawning pelagic eggs. However, the depository ratio of the three distinct types of Lv in the mullet VO appeared to be different from that estimated for another marine pelagophil, the barfin flounder. These results support a recent paradigm regarding the significance of Vg multiplicity upon successive physiological events in this group of fishes including the hydration of maturing oocytes, the acquisition of proper egg buoyancy, and the generation of requisite nutrient stocks for each stage of embryogenesis and larval development.
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carp cyprinus carpio vitellogenin characterization of Yolk Proteins development of immunoassays and use as biomarker of exposure to environmental estrogens
Environmental sciences : an international journal of environmental physiology and toxicology, 2007Co-Authors: Akihiko Hara, Haruhisa Fukada, Toshiaki Fujita, Kaori Hirano, Munetaka Shimizu, Fuminari Ito, Hideshige Takada, Masaru Nakamura, Taisen IguchiAbstract:The precursor protein of egg Yolk, vitellogenin (Vg), is cleaved into three major components (lipovitellin, phosvitin and beta'-component) at the time of incorporation by growing oocytes. We purified three Yolk Proteins (YP1, YP2 and YP3) from ovaries of the common carp (Cyprinus carpio) by a combined method of ammonium sulfate precipitation and column chromatography. Biochemical analyses of the purified Proteins of this species suggest that YP1, YP2 and YP3 are lipovitellin, beta'-component and phosvitin, respectively. A specific antiserum against purified carp YP1 (lipovitellin) was used to develop a single radial immunodiffusion (SRID) technique and an enzyme-linked immunosorbent assay (ELISA) for carp Vg. By SRID and ELISA, we measured the circulating carp Vg level to be in the ranges of 12.5-400 microg/ml and 2.0-1000 ng/ml, respectively, which cover a wide range of Vg levels. From 1997-1998, male and female carp were captured at points of effluent discharge from a sewage treatment plant connected to the Tama River, where estrogenic compounds were later detected, and the presence of Vg in their circulation was examined. Vg was detected in both male and female carp at the mg/ml level, suggesting that estrogens such as estrone and estradiol were sufficiently high to induce Vg in male carp inhabiting this area. The result of this study supports the use of carp Vg as a biomarker of fish exposure to environmental estrogens.
Haruna Amano - One of the best experts on this subject based on the ideXlab platform.
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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.
Comparative Biochemistry and Physiology - Part B: Biochemistry and Molecular Biology, 2016Co-Authors: Ozlem Yilmaz, Haruna Amano, Francisco Prat, A. Jose Ibáñez, Sadi Köksoy, Craig V SullivanAbstract: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.
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proportional accumulation of Yolk Proteins derived from multiple vitellogenins is precisely regulated during vitellogenesis in striped bass morone saxatilis
Journal of Experimental Zoology, 2014Co-Authors: Valerie N. Williams, Naoshi Hiramatsu, Benjamin J. Reading, Haruna Amano, Justin Schilling, Scott A Salger, Taufika Islam Williams, Kevin Gross, Craig V SullivanAbstract:We quantified three vitellogenins (VtgAa, VtgAb, VtgC) or their derived Yolk Proteins (YPs) in the liver, plasma, and ovary during pre-vitellogenic (PreVG), mid-vitellogenic (MVG), and late- vitellogenic (LVG) oocyte growth and during post-vitellogenesis (PostVG) in the striped bass (Morone saxatilis) using label-free quantitative mass spectrometry (MS). Western blotting of the samples using antisera raised against gray mullet (Mugil cephalus) lipovitellins derived from VtgAa, VtgAb, and VtgC confirmed the MS results. Semi-quantitative reverse transcription polymerase chainreaction(RT-PCR)revealedliverastheprimarysiteofexpressionforallthreeVtgs,withextra- hepatictranscription weaklydetectedinovary,foregut,adiposetissue,andbrain.Quantitativereal- time RT-PCR confirmed vtgAb to be primarily expressed in liver and VtgAb Proteins were predominant in liver and plasma from MVG to PostVG. However, the primary period of deposition into oocytes of VtgAb occurred up until MVG, whereas VtgAa was primarily deposited from MVG to LVG. The VtgC was gradually taken up by oocytes throughout vitellogenesis and was detected at trace levels in plasma. The ratio of Yolk Proteins derived from VtgAa, VtgAb, VtgC (YPAa/YPAb/YPC) in PostVG ovary is 1.4:1.4:1, which differs from ratios previously reported for other fish species in that YPC comprises a greater proportion of the egg Yolk. Our results indicate that proportional accumulation of multiple Vtgs in the Yolk may depend both on the precise rates of their hepatic secretion and specific uptake by oocytes. Furthermore, composition of the Vtg-derived Yolk may vary among Acanthomorph fishes, perhaps reflecting their different early life histories and reproductive strategies. J. Exp. Zool. 9999A: 1-15, 2014. © 2014 Wiley Periodicals, Inc.
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Multiple vitellogenins and product Yolk Proteins in striped bass, Morone saxatilis: molecular characterization and processing during oocyte growth and maturation
Fish physiology and biochemistry, 2013Co-Authors: Valerie N. Williams, Akihiko Hara, Naoshi Hiramatsu, Benjamin J. Reading, Haruna Amano, Norman J. Glassbrook, Craig V SullivanAbstract:The multiple vitellogenin (Vtg) system of striped bass, a perciform species spawning nearly neutrally buoyant eggs in freshwater, was investigated. Vitellogenin cDNA cloning, Western blotting of Yolk Proteins (YPs) using Vtg and YP type-specific antisera, and tandem mass spectrometry (MS/MS) of the YPs revealed the complex mechanisms of Yolk formation and maturation in this species. It was discovered that striped bass possesses a tripartite Vtg system (VtgAa, VtgAb, and VtgC) in which all three forms of Vtg make a substantial contribution to the Yolk. The production of Vtg-derived YPs is generally similar to that described for other perciforms. However, novel amino-terminal labeling of oocyte YPs prior to MS/MS identified multiple alternative sites for cleavage of these Proteins from their parent Vtg, revealing a YP mixture far more complex than reported previously. This approach also revealed that the major YP product of each form of striped bass Vtg, lipovitellin heavy chain (LvH), undergoes limited degradation to smaller polypeptides during oocyte maturation, unlike the case in marine fishes spawning buoyant eggs in which LvHAa undergoes extensive proteolysis to osmotically active free amino acids. These differences likely reflect the lesser need for hydration of pelagic eggs spawned in freshwater. The detailed characterization of Vtgs and their proteolytic fate(s) during oocyte growth and maturation establishes striped bass as a freshwater model for investigating teleost multiple Vtg systems.
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characterization of vitellogenin and its derived Yolk Proteins in cloudy catshark scyliorhinus torazame
Fish Physiology and Biochemistry, 2012Co-Authors: Kodai Yamane, Naoshi Hiramatsu, Takahiro Matsubara, Haruna Amano, Tomoki Yagai, Osamu Nishimiya, Rieko Sugawara, Toshiaki Fujita, Takashi Todo, Akihiko HaraAbstract:Elasmobranchs (sharks and rays) exhibit unique reproductive characteristics and, in contrast to the situation in teleosts, very little is known about the identity, structure and physical characteristics of their egg Yolk Proteins. The aims of this study were to (1) detect and purify the vitellogenin (Vtg; egg Yolk precursor) and Yolk Proteins (YPs) of the cloudy catshark (Scyliorhinus torazame), (2) examine the relationships between Vtg and YPs and (3) characterize and classify the deduced primary structure of the Vtg transcript (vtg). The apparent molecular weights of purified Vtg and putative Vtg-related YPs (lipovitellin: Lv, phosvitin: Pv) were determined by gel filtration and were ~560, >669 and ~58 kDa, respectively. Following SDS-PAGE, these purified products (i.e., Vtg, Lv and Pv) appeared as bands of ~210, ~110 and ~22 kDa, respectively. On Western blots, antisera against purified Vtg, Lv and Pv recognized the ~210 kDa Vtg band. Catshark Pv, in contrast to teleost Pvs, had a very low serine content. The catshark Vtg cDNA sequence (vtg) appeared to contain an open-reading frame consisting of domains encoding Lv, Pv and β′-component (β′-c). A phylogenetic analysis, with a consideration of genome duplication events, placed catshark vtg into the ‘vtgAB type.’ It is concluded that at least a single major type of Vtg protein, which is transcribed and translated from catshark vtgAB gene, is the precursor of three egg Yolk Proteins (Lv, Pv and β′-c) in catshark.
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multiple vitellogenin derived Yolk Proteins in gray mullet mugil cephalus disparate proteolytic patterns associated with ovarian follicle maturation
Molecular Reproduction and Development, 2008Co-Authors: Haruna Amano, Naoshi Hiramatsu, Craig V Sullivan, Takahiro Matsubara, Toshiaki Fujita, Hirohiko Kagawa, Akihiko HaraAbstract:Disparate proteolytic patterns of Yolk Proteins, derived from three types of vitellogenin (VgA, VgB, and VgC), were observed in gray mullet. Immuno-biochemical analyses of extracts obtained from vitellogenic ovaries (VO) and ovulated eggs (OE) confirmed that a large proportion of VgA-derived lipovitellin (LvA) was degraded into free amino acids (FAAs) during ovarian follicle maturation. The maturation-associated alteration of VgB-derived Lv (LvB) involved only limited proteolysis; the heavy and light LvB chains were dissociated into at least three and one polypeptide fragments, respectively. The native mass of VgC-derived Lv (LvC) exhibited little difference between VO and OE, although it was apparent that the LvC was 'nicked' during maturation, resulting in the appearance of several bands in OE. Similar analyses confirmed that VgA-derived beta'-component (beta'-cA) and VgB-derived beta'-c (beta'-cB) decreased during maturation in both quantity and native mass, while phosvitin derived from either VgA (PvA) or VgB (PvB) appeared to be degraded into FAAs. The pattern of maturation-associated proteolysis of mullet Yolk Proteins is similar to that reported for other marine teleosts spawning pelagic eggs. However, the depository ratio of the three distinct types of Lv in the mullet VO appeared to be different from that estimated for another marine pelagophil, the barfin flounder. These results support a recent paradigm regarding the significance of Vg multiplicity upon successive physiological events in this group of fishes including the hydration of maturing oocytes, the acquisition of proper egg buoyancy, and the generation of requisite nutrient stocks for each stage of embryogenesis and larval development.
Benjamin J. Reading - One of the best experts on this subject based on the ideXlab platform.
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Ovarian Yolk formation in fishes: Molecular mechanisms underlying formation of lipid droplets and vitellogenin-derived Yolk Proteins
General and Comparative Endocrinology, 2015Co-Authors: Naoshi Hiramatsu, Craig V Sullivan, Takahiro Matsubara, Benjamin J. Reading, Takashi Todo, Justin Schilling, Yong-woon Ryu, Hiroko Mizuta, Wenshu Luo, Osamu NishimiyaAbstract:Fish egg Yolk is largely derived from vitellogenins, which are synthesized in the liver, taken up from the maternal circulation by growing oocytes via receptor-mediated endocytosis and enzymatically processed into Yolk Proteins that are stored in the ooplasm. Lipid droplets are another major component of fish egg Yolk, and these are mainly composed of neutral lipids that may originate from maternal plasma lipoProteins. This review aims to briefly summarize our current understanding of the molecular mechanisms underlying Yolk formation in fishes. A hypothetical model of oocyte growth is proposed based on recent advances in our knowledge of fish Yolk formation.
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proportional accumulation of Yolk Proteins derived from multiple vitellogenins is precisely regulated during vitellogenesis in striped bass morone saxatilis
Journal of Experimental Zoology, 2014Co-Authors: Valerie N. Williams, Naoshi Hiramatsu, Benjamin J. Reading, Haruna Amano, Justin Schilling, Scott A Salger, Taufika Islam Williams, Kevin Gross, Craig V SullivanAbstract:We quantified three vitellogenins (VtgAa, VtgAb, VtgC) or their derived Yolk Proteins (YPs) in the liver, plasma, and ovary during pre-vitellogenic (PreVG), mid-vitellogenic (MVG), and late- vitellogenic (LVG) oocyte growth and during post-vitellogenesis (PostVG) in the striped bass (Morone saxatilis) using label-free quantitative mass spectrometry (MS). Western blotting of the samples using antisera raised against gray mullet (Mugil cephalus) lipovitellins derived from VtgAa, VtgAb, and VtgC confirmed the MS results. Semi-quantitative reverse transcription polymerase chainreaction(RT-PCR)revealedliverastheprimarysiteofexpressionforallthreeVtgs,withextra- hepatictranscription weaklydetectedinovary,foregut,adiposetissue,andbrain.Quantitativereal- time RT-PCR confirmed vtgAb to be primarily expressed in liver and VtgAb Proteins were predominant in liver and plasma from MVG to PostVG. However, the primary period of deposition into oocytes of VtgAb occurred up until MVG, whereas VtgAa was primarily deposited from MVG to LVG. The VtgC was gradually taken up by oocytes throughout vitellogenesis and was detected at trace levels in plasma. The ratio of Yolk Proteins derived from VtgAa, VtgAb, VtgC (YPAa/YPAb/YPC) in PostVG ovary is 1.4:1.4:1, which differs from ratios previously reported for other fish species in that YPC comprises a greater proportion of the egg Yolk. Our results indicate that proportional accumulation of multiple Vtgs in the Yolk may depend both on the precise rates of their hepatic secretion and specific uptake by oocytes. Furthermore, composition of the Vtg-derived Yolk may vary among Acanthomorph fishes, perhaps reflecting their different early life histories and reproductive strategies. J. Exp. Zool. 9999A: 1-15, 2014. © 2014 Wiley Periodicals, Inc.
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Multiple vitellogenins and product Yolk Proteins in striped bass, Morone saxatilis: molecular characterization and processing during oocyte growth and maturation
Fish physiology and biochemistry, 2013Co-Authors: Valerie N. Williams, Akihiko Hara, Naoshi Hiramatsu, Benjamin J. Reading, Haruna Amano, Norman J. Glassbrook, Craig V SullivanAbstract:The multiple vitellogenin (Vtg) system of striped bass, a perciform species spawning nearly neutrally buoyant eggs in freshwater, was investigated. Vitellogenin cDNA cloning, Western blotting of Yolk Proteins (YPs) using Vtg and YP type-specific antisera, and tandem mass spectrometry (MS/MS) of the YPs revealed the complex mechanisms of Yolk formation and maturation in this species. It was discovered that striped bass possesses a tripartite Vtg system (VtgAa, VtgAb, and VtgC) in which all three forms of Vtg make a substantial contribution to the Yolk. The production of Vtg-derived YPs is generally similar to that described for other perciforms. However, novel amino-terminal labeling of oocyte YPs prior to MS/MS identified multiple alternative sites for cleavage of these Proteins from their parent Vtg, revealing a YP mixture far more complex than reported previously. This approach also revealed that the major YP product of each form of striped bass Vtg, lipovitellin heavy chain (LvH), undergoes limited degradation to smaller polypeptides during oocyte maturation, unlike the case in marine fishes spawning buoyant eggs in which LvHAa undergoes extensive proteolysis to osmotically active free amino acids. These differences likely reflect the lesser need for hydration of pelagic eggs spawned in freshwater. The detailed characterization of Vtgs and their proteolytic fate(s) during oocyte growth and maturation establishes striped bass as a freshwater model for investigating teleost multiple Vtg systems.
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Conserved and Variant Molecular and Functional Features of Multiple Egg Yolk Precursor Proteins (Vitellogenins) in White Perch (Morone americana) and other Teleosts
Marine Biotechnology, 2008Co-Authors: Benjamin J. Reading, Akihiko Hara, Naoshi Hiramatsu, Sayumi Sawaguchi, Takahiro Matsubara, Mark O. LivelyAbstract:Three complete cDNAs encoding different forms of vitellogenin (Vtg) were isolated from a white perch ( Morone americana ) liver cDNA library and characterized with respect to immunobiochemical and functional features of the three Vtgs and their product Yolk Proteins (YPs) in this species and in the congeneric striped bass ( Morone saxatilis ). The two longest cDNAs encoded Vtgs with a complete suite of Yolk protein domains that, based on comparisons with vtg sequences from other species, were categorized as VtgAa and VtgAb using the current nomenclature for multiple teleost Vtgs. The shorter cDNA encoded a Vtg that lacked a phosvitin domain, had a shortened C-terminus, and was categorized as VtgC. Mapping of peptide sequences from the purified Vtgs and their derived YPs to Vtg sequences deduced from the cDNAs definitively identified the white perch VtgAa, VtgAb, and VtgC Proteins. Detailed comparisons of the primary structures of each Vtg with partial or complete sequences of Morone Yolk Proteins or of Vtgs from other fishes revealed conserved and variant structural elements of teleost Vtgs with functional significance, including, as examples, signal peptide cleavage sites, dimerization sites, cathepsin D protease recognition sites, and receptor-binding domains. These comparisons also yielded an interim revision of the classification scheme for multiple teleost Vtgs.
