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At least 19 recordsLinked to original sources
PubMed1978

Primary induction of vitellogenin mRNA in the rooster by 17beta-estradiol.

We have studied the kinetics of vitellogenin mRNA accumulation in rooster liver after a primary injection of 17beta-estradiol. The levels of vitellogenin mRNA have been determined both by hybridization of total cellular RNA to vitellogenin cDNA and by translation of vitellogenin mRNA in a wheat germ cell-free system. The results obtained by both methods of analysis are in good agreement and indicate that vitellogenin mRNA is present in the liver of normal roosters at a level of 0-5 molecules per liver cell and increases in amount during the 3 days following injection of estrogen, reaching a level of almost 6000 molecules per cell at the peak of the response. The level of vitellogenin mRNA declined exponentially during the next 14 days with a half-life of 29 hr, reaching a level of less than 10 molecules per cell at 17 days after injection of the hormone. The levels of vitellogenin mRNA after stimulation with estrogen have been correlated with the in vivo rate of synthesis of the vitellogenin polypeptide. The results indicate that the rate of vitellogenin synthesis is closely correlated with the level of vitellogenin mRNA. On the basis of these findings, we conclude that vitellogenin mRNA does not exist in the liver in an untranslated form after withdrawal from estrogen.

Animals↗
PubMed1979

Two processing steps in maturation of vitellogenin polypeptides in Drosophila melanogaster.

Synthesis of the three vitellogenin polypeptides (molecular weights of 44,000, 45,000, and 46,000) of Drosophila melanogaster has been analyzed in vivo and in a cell-free system. After labeling periods in vivo, the three vitellogenin polypeptides were made as the principal synthetic products of the female fat body. During a short (0.5 min) labeling period, they were identified as discrete species on two-dimensional gels. Two of the polypeptides have molecular weights of 45,000 and a third has a molecular weight of 44,000. After longer labeling periods (5-45 min) the three mature vitellogenins appeared. Both immunoprecipitation and peptide mapping confirmed that the species labeled at 0.5 min are immature forms of the vitellogenin polypeptides. In vitro translation of poly(A)-RNA from female fat body indicated another processing step in vitellogenin synthesis. Three polypeptides were obtained that were identified as precursors of the vitellogenins on the basis of immunoprecipitation and peptide mapping. Two of the translation products have a molecular weight of 46,000 and the third has a molecular weight of 45,000. Because the vitellogenins are secreted proteins, we interpret the higher molecular weight of the in vitro translation products as being due to signal peptides.

Adipose Tissue↗
PubMed1979

Enrichment and characterization of the DNA coding for vitellogenin in Xenopus laevis.

Purified vitellogenin mRNA of Xenopus laevis was incubated with mechanically sheared DNA in high concentrations of formamide and the resulting R-loops (i.e. RNA . DNA hybrid fragments) separated from the bulk DNA by caesium chloride buoyant density centrifugation. Hybridization with 125I-labeled vitellogenin mRNA revealed a 15--30-fold enrichment of the DNA coding for vitellogenin. Restriction analysis of the R-loop-enriched DNA demonstrated that all known endonuclease HindIII fragments coding for vitellogenin of unfractionated Xenopus DNA were also present in the enriched material, including the specific fragments for the oligo(A)-containing segment of the RNA. Comparison of these restriction data with the structure found in cloned vitellogenin cDNA, indicates the presence of at least one intervening sequence in the genomic DNA coding for vitellogenin.

Animals↗
PubMed1977

Comparative study of hen yolk phosvitin and plasma vitellogenin.

Vitellogenin, the only phosphoprotein detectable in the plasma of laying hens, is present at an approximate concentration of 1 mg/mL and can be isolated by chromatography on diethylaminoethylcellulose. Vitellogenin has a molecular weight of 235 000--240 000 and contains approximately 3% phosphorus by weight. Evidence that this protein is the precursor of phosvitins includes its ability to act as an acceptor for phosphate with a phosvitin specific kinase, the generation of a peptide similar to phosvitin by trypsinization, and the presence of distinctive peptides of multiple clustered phosphoserine upon partial acid hydrolysis. This partial sequence similarity between phosvitins and vitellogenin has not been previously reported. The phosphorus content and amino acid composition of vitellogenin are consistent with a model which contains two phosvitins and one lipovitellin. The total molecular weights of these proteins (28 000 + 34 000 + 170 000 = 232 000) are close to that of vitellogenin.

Amino Acids↗
PubMed1977

Regulation by estrogen of the vitellogenin gene.

The vitellogenin gene is inactive in the liver of male Xenopus laevis, unless exogenous estrogen is administered. We have previously shown that conventional doses of estradiol-17beta result in the appearance of new hepatic messenger RNAs, some of which are encoded for vitellogenin. We now report that much higher doses of the hormone (2 mg/frog per day for 4 days) are required to elicit maximal responses. The relative levels of membrane-bound polysomes and vitellogenin mRNA were determined as a function of time and dose of hormone. Translation of total polysomal RNA in a cell-free system derived from wheat germ was used to estimate the relative levels of vitellogenin messenger RNA. Faithful translation of this messenger RNA was indicated by two lines of evidence: labeled cell-free products were immunoprecipitated with antivitellogenin antibody, and the migration of the major labeled product in sodium dodecyl sulfate/acrylamide gels was identical to that of native vitellogenin. Our results establish conditions for maximal estrogen-induced responses in this system, and are compatible with the hypothesis that a major regulatory mechanism of steroid hormones in the control of protein synthesis is that of gene activation and regulation of messenger RNA levels.

Animals↗
PubMed1979

Plasma levels of vitellogenin in Chrysemys picta during the annual gonadal cycle: measurement by specific radioimmunoassay.

A RIA for turtle (Chrysemys picta) vitellogenin is described. After dimethylformamide precipitation of vitellogenin from the plasma of estrogen-treated female turtles, antibodies were developed in rabbits. The dimethylformamide precipitate was further purified by o-triethylaminoethyl cellulose column chromatography; the vitellogenin component eluted as a single peak. This material was used for iodination by a mild chloramine method. Antibodies to turtle vitellogenin did not cross-react with plasma from male turtles or vitellogenic females of other vertebrate groups, including lizards and snakes. Limited cross-reactivity exists among the chelonians, however. Using a 1:5000 dilution of antiserum, the limit of detection was 15 ng, and the midrange was 320 +/- 45 ng. For an antiserum dilution of 1:1000, these figures were 30 and 600 +/- 37 ng, respectively. Using this assay, the seasonal pattern of plasma vitellogenin in the turtle has been described, and preliminary studies on in vitro hepatic vitellogenesis have been performed.

Animals↗
PubMed1979

Vitellogenin in Xenopus laevis is encoded in a small family of genes.

Vitellogenin, the yolk protein precursor, is produced in X. laevis liver from a 6.3 kilobase (kb) mRNA. Sequences of this mRNA have been transcribed into cDNA and cloned in E. coli. Some properties of 21 of these cloned DNAs, ranging in size from 1 to 3.7 kb, have been reported by Wahli et al. (1978b). This paper reports restriction endonuclease mapping, cross hybridization, heteroduplex mapping in the electron microscope and heteroduplex melting experiments with these DNAs. We conclude that the cloned DNAs fall into two main groups of sequences which differ from each other in approximately 20% of their nucleotides. Each main group contains two subgroups which differ from each other by about 5% sequence divergence. By hybridizing cloned DNAs with restricted genomic DNA, we showed that sequences corresponding to all four sequence groups are present in a single animal. Furthermore, we have obtained tentative evidence for the presence of large intervening sequences in genomic vitellogenin DNA. Analysis of R loop molecules demonstrated that all four sequences are present in the vitellogenin mRNA population purified from individual animals. While some alternate explanations are not entirely excluded, we suggest that vitellogenin is encoded by a small family of related genes in Xenopus.

Animals↗
PubMed1978

Synthesis of vitellogenin, an attractive model for investigating hormone-induced gene activation.

The estrogen-induced synthesis of vitellogenin in the frog Xenopus and the chicken is an attractive system for investigating the molecular events leading to the activation of a specific gene. In this review article the events occurring at the level of the protein and mRNA in the cytoplasm are discussed. The available data show that the induction of vitellogenin synthesis is due to the accumulation of the corresponding vitellogenin mRNA in the cytoplasm. This suggests that transcriptional or posttranscriptional events in the nucleus are activated by the hormone. The few experiments investigating the processes in the nuclear compartment are reviewed.

Animals↗
PubMed1979

Characterisation of bacterial clones containing DNA sequences derived from Xenopus laevis vitellogenin mRNA.

A 1700 nucleotide DNA sequence derived from Xenopus vitellogenin mRNA has been cloned in the bacterial plasmid pBR322. The identity of the cloned sequence was verified in two ways. Firstly, the plasmid DNA was shown to hybridise to an RNA of the correct size (6,700 nucleotides). This was shown by in situ hybridisation to electrophoretically separated RNA and also by the formation of "R-loops" with purified vitellogenin mRNA. Then, using a novel procedure in which plasmid DNA covalently bound to diazotised paper is used to select complementary mRNA sequences, the cloned sequence was shown to hybridise to an mRNA which directed the synthesis of vitellogenin when translated in a reticulocyte lysate cell-free system.

Animals↗
PubMed1979

Distribution of estradiol receptor and vitellogenin gene in chick liver chromatin fractions.

The distribution of estradiol receptor and vitellogenin gene was studied in estradiol stimulated chick liver chromatin fractions prepared by limited DNAse II digestion and MgCl2 precipitation. The receptor was found in all fractions, undigested chromatin (P1), Mg2+ insoluble chromatin (P2) and Mg2+ soluble chromatin (S2). This last fraction was rich in acidic proteins, had a high protein:DNA ratio (7.0 w/w), contained 28% of rapidly labelled RNA, 20% of the receptor, 3-5% of chromatin DNA and showed a 2 fold enrichment of vitellogenin DNA sequences over unfractionated chromatin as well as P1 and P2 DNA. On isopycnic metrizamide gradients, all chromatin fractions showed a receptor peak banding at 1.23 g/cm3, the density of nucleoproteins. Hybridization experiments showed that the DNA banding at this density in fraction S2 was enriched 4 fold in vitellogenin DNA sequences over unfractionated chromatin as well as P1 and P2 DNA. These results suggest an association of hormone receptor complex with nucleoprotein structures of an apparently active chromatin fraction.

Animals↗
PubMed2026

Molecular characterization of vitellogenin and its receptor with CRISPR-based sgRNA validation in the legume pod borer, Maruca vitrata (Geyer) (Lepidoptera: Crambidae).

Maruca vitrata, the legume pod borer, causes yield losses of up to 80% in grain legumes. Increasing insecticide resistance and environmental concerns necessitate sustainable pest management alternatives. In the present study, the complete vitellogenin (Vg) coding sequence (CDS), a key reproductive gene involved in oogenesis and embryonic development, was cloned and molecularly characterised from M. vitrata. The assembled Vg CDS (∼5.3 kb) shared 99.04% sequence identity with the reported M. vitrata Vg sequence (MG799570.1). Phylogenetic analysis demonstrated close evolutionary association with related Lepidopteran species, while protein domain analysis identified three conserved domains, namely LPD_N, DUF1943, and VWD. Among these, the single exon-encoded LPD_N domain was selected as the target region for CRISPR/Cas9-mediated editing. Homology models of Vg and vitellogenin receptor (VgR) (Global Model Quality Estimation (GMQE): 0.58 and 0.51) showed a favourable interaction by protein-protein docking (score: -295.66). Three single-guide RNAs (sgRNAs) were designed, synthesised through in-vitro transcription, and evaluated using in vitro cleavage assays. sgRNA1 targeting the LPD_N domain and sgRNA2 targeting the signal peptide region exhibited efficient site-specific cleavage activity, whereas sgRNA3 failed to induce cleavage because of an unfavourable secondary structure that likely impaired Cas9-sgRNA complex formation. Overall, this study provides the first CRISPR-oriented functional characterisation and sgRNA validation of the M. vitrata Vg gene, together with structural characterisation of VgR and Vg-VgR interaction analysis, providing preliminary molecular resources for future CRISPR/Cas9 studies and supporting future embryo microinjection and heritable genome editing for sustainable management of M. vitrata.

CRISPR/Cas9↗
PubMed1979

Vitellogenin, lipid and carbohydrate metabolism during vitellogenesis and pregnancy, and after hormonal induction in the blenny Zoarces viviparus (L.).

1. Ovarian vitellogenic growth in Zoarces viviparus lasts about 2 months. Vitellogenesis is immediately followed by ovulation, fertilization and a pregnancy period of 4 months. Vitellogenin is observed in the blood during vitellogenesis, but declines during the first month of pregnancy. 2. The largest amount of liver lipid is found before vitellogenesis is initiated. During pregnancy the liver is depleted of lipid and glycogen, and total lipid and phospholipid is accumulating in the blood. 3. Estradiol treatment during pregnancy results in a dose-dependent increase in vitellogenin and lipids of the blood. 4. In late pregnancy, birth can be provoked with progesterone alone, or with combined progesterone and estradiol treatment.

Animals↗
PubMed1979

Physical and chemical characterization of vitellogenin from the hemolymph and eggs of the tobacco hornworm, Manduca sexta.

1. Vitellogenin has been purified from mature eggs and the hemolymph of adult females of Manduca sexta by a combination of gel permeation chromatography and sodium bromide density gradient centrifugation. 2. It has a molecular weight of 2.6 x 10(5) and is a glycolipoprotein containing approx 11% lipids and 3% carbohydrates. 3. The carbohydrate moiety is comprised entirely of mannose and N-acetyl glucosamine. 4. Two polypeptide chains are present with molecular weights of 1.8 x 10(5) and 5.0 x 10(4). 5. Partial proteolytic hydrolysis of vitellogenin resulted in the degradation of the large polypeptide but did not affect the small one, suggesting that the small polypeptide is located in the interior of the particle. 6. The proteolytic hydrolysis products of the large polypeptide differed from one another by approx 12.5 x 10(3) daltons.

Amino Acids↗
PubMed1979

Dose response kinetics of serum vitellogenin, liver DNA, RNA, protein and lipid after induction by estradiol-17 beta in male flounders (Platichthys flesus L.).

1. Male flounders receiving 100 micrograms estradiol each second day were fully induced to vitellogenin synthesis within 11 days, while fishes given 5 micrograms doses continued to accumulate vitellogenin in the serum at a progressive rate through 17 days. 2. Liver DNA per unit fish remained constant, while RNA per unit fish in flounders given 100 and 5 micrograms doses attained values 80 and 25% respectively, above the values found in control animals. 3. Liver RNA per unit DNA increased at maximal rate within 6 days in fishes receiving 100 micrograms doses. RNA synthesis continued at a progressive rate through 17 days in fishes given 5 micrograms doses of estradiol. 4. Liver protein per unit DNA elevated at a plateau 60% above control within 6 days with 100 micrograms doses. Doses of 5 micrograms had only little effect on liver protein. 5. Estradiol had a lipogenic effect on the liver. Cellular lipid rose 120 and 60% above control after treatment with 100 and 5 micrograms respectively. 6. Liver dry weight per unit DNA increased 60 and 55% above control with 100 and 5 micrograms doses respectively. Cellular hypertrophy in fishes receiving the smaller dose was primarily associated with an increase in lipid concentration, while protein and lipid contributed almost equally to cellular growth in fishes receiving the high dose.

Animals↗
PubMed1977

Coordination of ribosome content and polysome formation during estradiol stimulation of vitellogenin synthesis in immature male chick livers.

To elucidate the mechanisms by which protein synthesis is affected by estradiol, we characterized cockerel liver polysomal profiles during hormone induction and withdrawal. We describe a method for isolating intact polysomes which results in preparations that are stable even after storage in solution at 10 degrees for 16 hr. In addition, our procedure eliminates the necessity for starving animals prior to experiments. Recovery of radioactive polysomes indicated that yield is about 90% and that our polysomal preparations appear to represent polysome distribution in vivo. Using this approach we show that estradiol injection stimulates ribosome content 6-fold and that formation of polysomes is coincident with the induction of vitellogenin synthesis. We also demonstrate that the size and number of polysomes increase and decrease in a coordinated fashion with the rate of vitellogenin synthesis. The kinetics of ribosome synthesis and the fact that at least 80% of the newly synthesized ribosomes are directly recruited into polysomes indicate that ribosomes might be limiting the rate of protein synthesis during the stimulatory phase of the hormone cycle.

Animals↗
PubMed1978

Decrease in functional albumin mRNA during estrogen-induced vitellogenin biosynthesis in avian liver.

Translation of rooster liver RNA in a wheat germ extract is shown to yield albumin as one of the cell-free products. Quantitation of albumin mRNA by the translation assay indicates that functional albumin mRNA represents 10% of total liver mRNA activity in control roosters. After estrogen administration, this level decreases in a continuous fashion until functional albumin mRNA represents 5% of total mRNA activity at 12 days. This decrease in functional albumin mRNA was correlated with several parameters of vitellogenin induction. Functional vitellogenin mRNA increases to a maximum at 4 days after hormone treatment and returns to control levels by 12 days. A similar pattern is seen for the hormone-stimulated increase in total mRNA activity. The decrease in functional albumin mRNA, therefore, persists after the vitellogenic response of the liver has been completed. These results suggest that the decrease in hepatic albumin synthesis after hormone treatment is due to an estrogen-mediated decrease in the content of albumin mRNA.

Albumins↗
PubMed1977

[Determination of the molecular weight of vitellogenin and of lipovitellins of Orchestia gammarella, Crustacea, Amphipoda].

Vitellogenin and lipovitellins of Orchestia gammarella, tested by electrophoresis on gels of different acrylamide concentrations, following the procedure of Hedrick and Smith (1968), displays a migration pattern identical to that of proteins of respectively congruent to 4 x 10(5) (vitellogenin), congruent to 3,5 x 10(5) (lipovitellins I and I') and congruent to 5 x 10(5) (lipovitellin II) molecular weights.

Animals↗
PubMed2026

Simulation of CRISPR/Cas9-mediated gene editing for the Vitellogenin gene in Apis mellifera.

CRISPR/Cas9 genome editing provides a powerful framework for interrogating gene function in Apis mellifera. Yet, empirical application remains challenging due to biological constraints, including haplodiploid genetics, narrow embryonic injection window, and the social rearing requirements that complicate functional validation. These constraints necessitate in silico pre-screening to maximize editing success before resource-intensive wet-lab implementation. Within the omnigenic framework, which distinguishes core regulatory genes from peripheral loci buffered by network effects, vitellogenin (Vg) represents an optimal target which is ancestrally dedicated to yolk provisioning; it has been co-opted to orchestrate diverse non-reproductive functions including longevity, stress resistance, immunity, and social behavior. We developed a computational pipeline to design a list of 57 and 56 candidate guide RNAs (gRNA) for targeted Vg knockout, evaluating candidate sites in both functional exons 2 and 3 based on structural accessibility and frameshift efficiency. Comparative analysis revealed complementary strengths in two top-best candidates from initial target pool of predicted gRNAs. The gRNA targeting exon 2 exhibits weaker secondary structure (ΔG = -0.25 kcal/mol versus -2.10 kcal/mol for exon 3), aligning with empirical evidence that sites with ΔG > -1.0 kcal/mol achieve 2-5 × higher Cas9 binding efficiency. This site yielded moderate frameshift frequency (77.8%; 61.9 percentile). Conversely, the predicted editing outcome for the gRNA targeting exon 3, despite stronger structural constraints, demonstrated superior functional disruption metrics demonstrating very high frameshift frequency (88.3%; 95.2 percentile), high in silico editing precision, minimal microhomology-mediated repair bias, and reproducible outcomes wherein nearly all predicted indels disrupt the coding sequence. Protein structure and domain analyses further predict that frameshift edits will generate a truncated protein missing all downstream functional domains. We recommend parallel empirical validation of both exon 2 and exon 3 targets to resolve the trade-off between structural accessibility (favoring higher editing rates) and frameshift efficacy (favoring complete loss-of-function). This dual-target strategy accommodates uncertainty in in vivo performance while maximizing the probability of generating informative phenotypes. Our in silico framework enables rational CRISPR design in non-model organisms by computationally balancing biophysical accessibility with functional impact, accelerating functional genomics in species where empirical optimization faces substantial biological constraints.

Animals↗