The preparation and characterization of vitellogenin messenger RNA from rainbow trout (<i>Salmo gairdneri</i>)

Valotaire, Yves; Tenniswood, Martin; Guellec, Catherine Le; Tata, Jamshed R.

doi:10.1042/bj2170073

Cited by 27 publications

(7 citation statements)

References 31 publications

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“…This result corroborates the recent report of Kishida et al (1992), who used DEAE-agarose to purify an s-VTG with an apparent 170 kDa primary subunit from blood plasma of E 2 -induced striped bass. This value is very similar to estimates of the molecular weight (170-200 kDa) of the rainbow trout VTG monomer (Chen 1983;Valotaire et al 1984), and similar to VTG subunit molecular weights (85-200 kDa) reported for several other fishes (tabulated by Mommsen and Walsh 1988;Silversand and Haux 1989;Bradley and Grizzle 1989;Ding et al 1989).…”

Section: Sampling Monthsupporting

confidence: 73%

Purification, characterization and immunoassay of striped bass (Morone saxatilis) vitellogenin

Tao

Hara

Hodson

et al. 1993

Fish Physiol Biochem

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The egg yolk precursor, vitellogenin (VTG), was purified from blood plasma of striped bass by chromatography on hydroxylapatite or DEAE-agarose. The fish were first implanted with estradiol-17β (E2), which induced vitellogenesis. A rabbit antiserum (a-FSPP) raised against plasma from mature female striped bass, and then adsorbed with mature male plasma, was used to detect female-specific plasma protein (FSPP) in the chromatography fractions. Striped bass VTG (s-VTG) was collected from the peak fraction that was induced by E2, reacted with a-FSPP, and contained all detectable phosphoprotein. It appeared as a single band (Mr ≂ 170,000) in SDS-PAGE or Western blots using a-FSPP, and as a pair of closely-spaced phospholipoprotein bands in native gradient-PAGE, suggesting that there is more than one circulating form of s-VTG. The relationship of s-VTG to the yolk proteins was verified using a-FSPP. The antiserum reacted with the main peak from gel filtration of saline ovary extracts, and it specifically immunostained the two main bands in Western blots of the extracts and the yolk granules of mature oocytes. The amino acid composition of s-VTG was similar to that of VTG from other fish and Xenopus. A radial immunodiffusion assay for s-VTG was developed using a-FSPP and purified s-VTG as standard. The s-VTG was not detected in blood plasma of males, immature females, or regressed adult females, but plasma s-VTG levels were highly correlated with plasma E2 and testosterone levels, and oocyte growth, in maturing females. The results indicate that the maturational status of female striped bass can be identified by s-VTG immunoassay.

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Section: Sampling Monthsupporting

confidence: 73%

Purification, characterization and immunoassay of striped bass (Morone saxatilis) vitellogenin

Tao

Hara

Hodson

et al. 1993

Fish Physiol Biochem

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“…These pot halves acted as spawning substrata, without which the fish would not spawn. Fish were exposed to treatments for a total of 42 d. Spawning substrata were removed for 7 d (days [22][23][24][25][26][27][28][29] to allow the fish to rest and then returned for the final 2 weeks of the exposure. The aquaria were randomly assigned to receive treatment concentrations of NP or control solutions delivered by a proportional-flow diluter.…”

Section: Exposuresmentioning

confidence: 99%

“…In cyprinid fishes such as the roach (Rutilus rutilus L.), which spawns once in a reproductive season, and in bleak (Alburnus albrunus L.) and white bream (Blicca bjoerkna L.), which have multiple spawnings per season, plasma Vtg concentrations were weakly yet positively correlated with plasma E 2 concentrations [26]. Induction of Vtg has been suggested to be a sensitive, E 2 -specific biomarker [8,[27][28][29] for the exposure of oviparous animals, such as the fathead minnow, to estrogen agonists [30], and it has been used to monitor for exposure of fish to endogenous estrogens, exogenous estrogens, and xenoestrogens [3,12,31]. However, in those experiments, a relatively great increase in plasma E 2 concentration resulted in a rather modest increase in plasma Vtg concentration.…”

Section: Relationship Between Plasma E 2 and Vtgmentioning

confidence: 99%

Effects of 4-Nonylphenol on Fecundity and Biomarkers of Estrogenicity in Fathead Minnows (Pimephales Promelas)

Giesy¹,

Pierens²,

Snyder³

et al. 2000

Environ Toxicol Chem

112

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Adult fathead minnows (Pimophales promelas) were exposed to waterborne concentrations of 4-nonylphenol (NP) ranging from 0.05 to 3.4 g NP/L for 42 d. Results were similar, but slightly different, for two experiments conducted during July and August, near the beginning of the breeding season, and a second experiment conducted during September and October, at the end of the breeding season, during which the adults were maintained continuously in breeding condition. Inverted U-type doseresponse relationships were observed for egg production and for concentrations of vitellogenin (Vtg) and 17␤-estradiol (E 2 ) in blood plasma. Concentrations of plasma Vtg were significantly different between males and females, with plasma concentrations in females ranging from 20 to 110 g Vtg/ml. Both experiments had no statistically significant, dose-dependent effect of NP on plasma Vtg in males but significant effects of NP on Vtg concentrations in females. In the first experiment, Vtg concentration generally increased with NP concentration, whereas the second experiment showed a negative correlation. Plasma E 2 concentrations in both males and females were significantly affected by NP. The concentration of total estrogen equivalents in the plasma increased 900% because of exposure to NP. Most of this increase resulted from increased plasma E 2 concentrations, with only a 4% increase resulting from the estrogen agonist activity of NP. The effects of NP on adult fathead minnows seem not to result from a directacting estrogen agonist mechanism but rather from changes in the endogenous concentrations of E 2 through an indirect activation mechanism of action.

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“…44 By denaturing conditions of SDS-PAGE, the monomeric form of Salmo gairdneri Vtg was found to range from 170 kDa 45 to 200 kDa. 46 Ding et al 47 reported two forms of Vtg of monomeric sizes, 130 and 180 kDa in the evolutionarily more advanced teleost fish, O. aureus. Vtg variation studied in 11 species of Perciformes, encompassing the families Cichlidae, Serranidae, Lutjanidae, Centropomidae, and Eleotrididae confirmed that in this order of fish the main features of Vtg protein diversity are interfamily variability in size and subunit number.…”

Section: Vitellogenin Proteins -Interspecific Diversity In Molecular mentioning

confidence: 98%

Vitellogenesis and Vitellogenin Uptake into Oocytes

Ding¹

2005

Hormones and Their Receptors in Fish Reproduction

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The yolk proteins found in the oocyte of oviparous animals are synthesized by the liver as a large lipophosphoglycoprotein precursor, vitellogenin (Vtg), which represents a vital, sole source of nutrient for the developing larvae. Vitellogenesis underlies early development of oviparous animals. The Vtg gene is extremely sensitive to estrogen and other steroid hormones. Thus, vitellogenesis is a useful model for studying hormonal regulation of eukaryotic gene expression. The Oreochromis aureus vitellogenin, OaVtg gene spans 9 kb and contains 34 exons. Although the OaVtg promoter has a nonconsensus TATA, this promoter is capable of driving basal transcription. Two imperfect estrogen response elements, ERE p (proximal) and ERE d (distal), located in the promoter at Ϫ532 and Ϫ1352 elicit a significant increase in estrogen-dependent reporter gene activity. Competition gel mobility shift assays have demonstrated that ERE p and a novel ERE exon2 (located within exon 2) exhibit specific binding of estrogen receptor. Thus, nonconsensus OaVtg EREs contribute to the estrogen-dependent regulation of the OaVtg gene in vivo. During estrogen-induced vitellogenesis, the massive rate of transcription and translation of Vtg followed by its secretion into the blood makes this a major circulating protein that is taken up by membrane-bound vitellogenin receptors (VtgR) found on oocytes. The VtgR, which belongs to the low density lipoprotein receptor family, interacts with the N-terminal region of Vtg Hormones and Their Receptors in Fish Reproduction Downloaded from www.worldscientific.com by UNIVERSITY OF BIRMINGHAM LIBRARY -INFORMATION SERVICES on 03/20/15. For personal use only. Vitellogenesis and Vitellogenin Receptor 255via electrostatic attraction. Once in the oocytes, Vtg is cleaved into yolk proteins (lipovitellin and phosvitin), which are stored as nutrients for the developing embryo.

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The preparation and characterization of vitellogenin messenger RNA from rainbow trout (Salmo gairdneri)

Cited by 27 publications

References 31 publications

Purification, characterization and immunoassay of striped bass (Morone saxatilis) vitellogenin

Purification, characterization and immunoassay of striped bass (Morone saxatilis) vitellogenin

Effects of 4-Nonylphenol on Fecundity and Biomarkers of Estrogenicity in Fathead Minnows (Pimephales Promelas)

Vitellogenesis and Vitellogenin Uptake into Oocytes

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