Vitellogenin synthesis in the avian liver. Vitellogenin is the precursor of the egg yolk phosphoproteins

Deeley, Roger G.; Mullinix, D P; Wetekam, Waldemar; Kronenberg, H.; Meyers, M.; Eldridge, Juanita; Goldberger, Robert F.

doi:10.1016/s0021-9258(19)40693-5

Cited by 214 publications

(21 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…VTG was purified from laying-hen plasma as described by Deeley et al [12] with some modifications. Briefly, about 10 ml of blood was drawn from the wing vein and collected in ice-cold tubes containing the following reagents (final concentrations): 16 mM-sodium citrate/ 1 mM-PMSF/2 ,AM-leupeptin/aprotinin (2.5 ,ug/ml).…”

Section: Purification Of Vtgmentioning

confidence: 99%

“…All buffers used in the purification of VTG by DEAEcellulose column chromatography contained 2 mm-CaCl2 and 1 mM-PMSF. After elution from the ion-exchange column [12], the fractions containing VTG were pooled and dialysed at 4 °C against buffer containing 150 mM-NaCl/0.2 mM-EDTA/1 mM-PMSF, pH 7.4. After dialysis, leupeptin (final concn.…”

Section: Purification Of Vtgmentioning

confidence: 99%

“…VTG was isolated from plasma of laying hens using the method described by Deeley et al [12] with some minor modifications that improved the stability of the purified protein (described in the Materials and methods section). In particular, the presence of 2 mM-CaCl2 and the protease inhibitors, leupeptin and aprotinin, in all isolation buffers resulted in preparations in which breakdown products of VTG were consistently absent upon storage at 4 °C for 5-7 days after isolation.…”

Section: Purification and Radiolabelling Of Chicken Vtgmentioning

confidence: 99%

“…Specific cell surface receptors have been implicated in mediating their uptake by the mechanism of receptormediated endocytosis [5][6][7][8][9][10][11]. VTG, a collective term for a group of homodimeric proteins of 240 kDa subunits, is of particular interest in that after its selective uptake by the oocytes, it is proteolytically cleaved into the yolk proteins termed lipovitellins and phosvitins [12]. These cleavage products of VTG are stored during oogenesis and constitute a depot of amino acids, lipid, inorganic phosphate, and possibly calcium, during embryogenesis.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Solubilization and characterization of the chicken oocyte vitellogenin receptor

Stifani

George

Schneider

1988

Biochemical Journal

107

View full text Add to dashboard Cite

This paper describes the biochemical characterization of the chicken oocyte plasma-membrane receptor for one of the major lipid-carrying yolk proteins, vitellogenin (VTG). The receptor was extracted from oocyte membranes with the non-ionic detergent octyl-beta-D-glucoside and visualized by ligand blotting, with 125I-VTG as a protein with an apparent Mr of 96000, under non-reducing conditions. It exhibited high affinity for native chicken VTG (Kd 2 X 10(-7) M) but was unable to bind VTG with reductively methylated lysine residues or phosvitin (the phosphoserine-rich intracellular cleavage product of VTG). Polyclonal antibodies to the 96 kDa protein inhibited VTG binding to the receptor and were able to precipitate functional VTG-receptor activity from oocyte-membrane detergent extracts with a concomitant removal of the 96 kDa protein. Antibodies directed against the mammalian receptor for low-density lipoprotein showed cross-reactivity with the chicken oocyte VTG receptor, raising the possibility that lipoprotein receptors in birds are structurally related to those in mammalian species.

show abstract

Section: Purification Of Vtgmentioning

confidence: 99%

Section: Purification Of Vtgmentioning

confidence: 99%

Section: Purification and Radiolabelling Of Chicken Vtgmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Solubilization and characterization of the chicken oocyte vitellogenin receptor

Stifani

George

Schneider

1988

Biochemical Journal

107

View full text Add to dashboard Cite

show abstract

“…The major differences detected in GC from the four largest prerecruitment follicles versus the most recently recruited follicle are related to yolk transport. These proteins are produced in the liver under the stimulation of estrogen and are then transported in the plasma to the ovary (Deeley et al, 1975). Also, identified are two novel, potentially important upstream regulators, MIR-21 and OSM, that require further investigation as potentially important pathways related to GC survival and differentiation.…”

Section: Discussionmentioning

confidence: 99%

Proteome profiling of chicken ovarian follicles immediately before and after cyclic recruitment

Ghanem

Johnson

2021

Molecular Reproduction Devel

View full text Add to dashboard Cite

A shotgun proteomics study using isobaric tags for relative and absolute quantification labeling was conducted to characterize proteins in chicken ovarian follicles immediately before and after cyclic recruitment. Granulosa cell (GC) layers from the most recently recruited follicle (GC9) and from each of the four largest prerecruitment follicles (GC1-4) plus theca tissue (TH) from the most recently recruited (TH9) and largest prerecruitment (TH1) follicles were compared. Of 1535 proteins identified, none were determined to be differentially expressed between TH9 and TH1. A pairwise comparison between GC9 and GC1, GC2, GC3, or GC4 resulted in one, five, five, and six differentially expressed proteins, respectively, including yolk and cholesterol transport proteins (vitellogenin 1-3 and apolipoprotein B). In addition, transforming growth factor-beta 1 and microRNA-21 pathways were predicted to be activated at recruitment. We also report, for the first time, the expression of the neuropeptide, RELAXIN-3 (RLN3), in GC. Quantitative polymerase chain reaction determined RLN3 expression to be highest in GC9 and GC1, but its receptors, RXFP1 and RXFP3, were highest in TH and ovarian stroma, respectively. Overall, cyclic recruitment is associated with changes in protein expression predominantly within follicle GC, and a potential role for RLN3 in follicle recruitment and the initiation of GC differentiation warrants further investigation.

show abstract

Biosynthesis, purification, and characterization of Aedes aegypti vitellin and vitellogenin

Borovsky

Whitney

1987

Arch Insect Biochem Physiol

View full text Add to dashboard Cite

Vitellin, the major egg yolk protein, and vitellogenin, the hemolymph precursor of egg yolk protein, have been purified to apparent homogeneity from the mosquito Aedes aegypti. The purification procedure included chromatography on ion exchange, hydrophobic, and gel filtration columns. Vitellin and vitellogenin have a similar molecular weight (Mr 300,000) on gel filtration columns. However, the molecular weights of vitellin and vitellogenin, as determined from SDS electrophoresis, were 393,000 and 337,000, respectively. Vitellin in sodium dodecyl sulfate released six subunits of molecular weight 116,000, 83,000, 75,000, 54,000, 36,000, and 29,000, whereas vitellogenin released only three subunits (155,000, 120,000, and 62,000). The average molecular weights of vitellin and vitellogenin after gel filtration and SDS electrophoresis were 346,000 and 318,000, respectively. Vitellin has a high content of aspartic acid and glutamic acid, and a low content of histidine, methionine, cysteine, and tryptophan. Vitellin also contains 0.9% mol of glucosamine and no galactosamine. The isoelectric points of vitellin and vitellogenin are at pH 6.4 and 6.3, respectively. Aedes aegypti fat bodies incubated for short intervals in tissue culture medium in the presence of [3H]valine showed incorporation by radio‐immunoprecipitation and SDS electrophoresis into three primary vitellogenin polypeptides of molecular weights (± SEM) 156,000 ± 4,000, 114,000 ± 5,000, and 62,000 ± 400 inside the fat body and 162,000 ± 3,000, 118,200 ± 2,000, and 63,000 ± 300 in the medium. These results suggest that the molecular weight of vitellogenin synthesized inside the fat body (Mr 332,000) remains unchanged when secreted into the hemolymph (Mr 343,000). The three vitellogenin subunits are processed by the ovary into six subunits which are then deposited in the yolk granules as vitellin.

show abstract

Vitellogenin synthesis in the avian liver. Vitellogenin is the precursor of the egg yolk phosphoproteins

Cited by 214 publications

References 40 publications

Solubilization and characterization of the chicken oocyte vitellogenin receptor

Solubilization and characterization of the chicken oocyte vitellogenin receptor

Proteome profiling of chicken ovarian follicles immediately before and after cyclic recruitment

Biosynthesis, purification, and characterization of Aedes aegypti vitellin and vitellogenin

Contact Info

Product

Resources

About