Vitellogenin isolation, purification and antigenic cross-reactivity in three teleost species

Watts, M.; Pankhurst, Neville William; Pryce, Andrea C.; Sun, Binyang

doi:10.1016/s1096-4959(02)00288-9

Cited by 37 publications

(35 citation statements)

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“…Although, some subunits of Vtgs are highly conserved and share a common general structure among fish (Finn, 2007), its complexity due to posttranslational modifications and translocation processes, often results, in poor antigenic cross-reactivity, even between closely related species (Watts et al, 2003;An et al, 2007). This makes a necessary more in-depth study of Vtg for every species of fish.…”

Section: __________________mentioning

confidence: 99%

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Proteomic characterization of vitellogenins from three species of South American fresh water fish

Urdaneta

Camafeita

Poleo

et al. 2018

lajar

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ABSTRACT. Vitellogenins (Vtg) are glycolipophosphoproteins synthesized by oviparous vertebrates as yolk proteins precursors. These proteins have been studied for their role in reproduction and in endocrine disruption. In this work, we report the first proteomic study towards the characterization of Vtg from Pseudoplatystoma fasciatum, Piaractus brachypomus and Colossoma macropomum. Male specimens of each of the three fish species were estradiol-induced (experimental) and non-induced (control). The initial Vtg characterization was made by 2D protein gel electrophoresis of both groups The identification of the high molecular weight spots, presumed to be Vtgs, was assessed by MALDI-TOF mass spectrometry analysis. A post-translational modification study was performed by differential staining of 2D gels in order to visualize phosphoproteins and glycoproteins. Plasma samples from the three species, induced with estrogen, showed three high molecular weight spots with variable isoelectric points. Post-translational modifications showed that Vtgs from P. brachypomus and C. macropomum presented a phosphorylated and glycosylated subunit, while the same subunit in P. fasciatum was only glycosylated. This characterization will help in the development of reliable immunoassays, which could be used for studies of endocrine disruption or for the improvement of artificial spawning, by uncovering the time of fish maturation or sex determination.

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confidence: 99%

“…In the present study, the protocol described by Watts et al (2003) for Vtg induction was used with modifications. The inductions were done during the regular spawning season for these fish, which in Venezuela goes from May to August.…”

Section: Hormonal Treatmentmentioning

confidence: 99%

Proteomic characterization of vitellogenins from three species of South American fresh water fish

Urdaneta

Camafeita

Poleo

et al. 2018

lajar

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“…Proteomics technologies based on 2D-PAGE, western blots of proteins separated on 2D-PAGE (Hiramatsu et al, 2002) and phosphopeptide analysis are very useful for establishing the vitellogenin map (Watts et al, 2003). Vtg processing has been studied in a number of species: insects such as cockroach (Tufail and Takeda, 2002) and cicada (Lee et al, 2000), marine shrimp (Avarre et al, 2003), teleost species, such as, masu salmon, greenback flounder, Atlantic salmon, rainbow trout, zebrafish, medaka, red sea bream and white perch (Matsubara et al, 1999;Hiramatsu et al, 2002;Watts et al, 2003;Wood and Van der Kraak, 2003;Tong et al, 2004;Sawaguchi et al, 2006), and in chicken (Luo et al, 1997).…”

Section: -D Map Of the Vitellogenin-derived Proteins In Oocytesmentioning

confidence: 99%

“…Vtg processing has been studied in a number of species: insects such as cockroach (Tufail and Takeda, 2002) and cicada (Lee et al, 2000), marine shrimp (Avarre et al, 2003), teleost species, such as, masu salmon, greenback flounder, Atlantic salmon, rainbow trout, zebrafish, medaka, red sea bream and white perch (Matsubara et al, 1999;Hiramatsu et al, 2002;Watts et al, 2003;Wood and Van der Kraak, 2003;Tong et al, 2004;Sawaguchi et al, 2006), and in chicken (Luo et al, 1997). Proteomics methods were used to characterize rainbow trout Vtg protein in its intact form, and then analyzed its derived tryptic and cyanogen bromide peptides by MALDI-TOF-MS and ESI quadrupole (Q)-TOF (Banoub et al, 2004).…”

Section: -D Map Of the Vitellogenin-derived Proteins In Oocytesmentioning

confidence: 99%

Proteomics analysis of the developing fish oocyte

2007

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“…[9][10][11] Enzyme-linked immunosorbent assay (ELISA) and radioimmunoassay (RIA) are the most commonly used approaches. 12,13 These antibody-based methods have considerable advantages of sensitivity and selectivity, however, at the same time they suffer from problems related to antibody specificity when facing multiple fish species. An antibody made against Vtg from one species is limited in its application as a probe for another, 14 and the preparation of an antibody usually needs several months.…”

mentioning

confidence: 99%

Rapid Determination of Vitellogenin in Fish Plasma by Anion Exchange High Performance Liquid Chromatography Using Postcolumn Fluorescence Derivatization with o-Phthalaldehyde

Yuan

2006

ANAL. SCI.

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Vitellogenin (Vtg) is a serum lipophosphoglycoprotein that serves as the major precursor to the egg-yolk protein of oviparous vertebrates. It is synthesized in the liver, under the receptor-mediated regulation of 17β-estradiol (E2). 1 Teleost Vtg appears to circulate in the plasma as a dimer with an apparent molecular mass ranging from approximately 300 to 600 kDa. 2 Two distinct forms of Vtg have been identified in tilapias, 3 Japanese common goby, 4 barfin flounder 5 and haddock. 6 Normally, Vtg can only be detected in sexually active female fish. However, when male and juvenile fish are exposed to estrogen or estrogen mimic chemicals, 7,8 Vtg production can be induced. Therefore, the presence of Vtg in the blood of male and juvenile fish has been used as an indicator of the influence of xenobiotic estrogens. 7 In order to be effectively utilized as a biomarker, Vtg in the plasma has to be accurately measured.A number of methods have been developed for Vtg fish plasma analysis. 9-11Enzyme-linked immunosorbent assay (ELISA) and radioimmunoassay (RIA) are the most commonly used approaches. 12,13These antibody-based methods have considerable advantages of sensitivity and selectivity, however, at the same time they suffer from problems related to antibody specificity when facing multiple fish species. An antibody made against Vtg from one species is limited in its application as a probe for another, 14 and the preparation of an antibody usually needs several months. Although cross-reaction was also found in some species, it is not possible to make an accurate quantification of low levels of Vtg in other species because of the affinity difference.1 Moreover, Vtg is very susceptible to proteolytic degradation. During the long process incubation period required in immunoassay methods, 9 the degradation of Vtg is inevitable, thus changing the overall reactivity of the antibody towards Vtg, even with the presence of antiproteolytic agents. For these reasons, to develop a new rapid and accurate determination method for Vtg is necessary and important.High performance liquid chromatography (HPLC) has been widely applied in the determination of proteins. [15][16][17] Vtg is a type of high molecular weight protein and can be precipitated by organic solvents. Even with large porous and short chain reverse phase columns, such as C4, it is difficult to separate Vtg from other proteins. On the other hand, ion exchange chromatography is widely used to purify Vtg. An anion exchange POROS HQ column has been adopted to analyze Vtg combined with UV detection at the wavelength of 280 nm, 16 and the detection limit of Vtg was reported as 2 μg per assay. Recently a two-step chromatographic method, combining anion exchange membrane purification with high performance size exclusion chromatography, was reported for the quantitative determination of Vtg in loach and sea catfish at the wavelength of 210 nm, with the detection limit of 20 μg ml -1 Vtg. 15 Although many peptides and proteins can absorb UV light and emit fluorescence due to th...

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Vitellogenin isolation, purification and antigenic cross-reactivity in three teleost species

Cited by 37 publications

References 24 publications

Proteomic characterization of vitellogenins from three species of South American fresh water fish

Proteomic characterization of vitellogenins from three species of South American fresh water fish

Proteomics analysis of the developing fish oocyte

Rapid Determination of Vitellogenin in Fish Plasma by Anion Exchange High Performance Liquid Chromatography Using Postcolumn Fluorescence Derivatization with o-Phthalaldehyde

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