Estrogen induction of VLDLy assembly in egg-laying hens. (1/521)

The yolk of a 60-g chicken egg contains 6 g of triacylglycerols transported to the oocyte from the liver of the laying hen in apolipoprotein (apo) B-containing particles. With the onset of egg production, estrogen shifts hepatocytic lipoprotein production from generic VLDL to VLDLy (yolk targeted). These VLDLy are triacylglycerol-rich particles; they are reduced in size by one half, are resistant to lipoprotein lipase and are taken up intact by oocyte receptors. The VLDLy pathway for apoB provides sufficient energy for the caloric requirements of chick development. VLDLy size reduction occurs in spite of surplus liver triacylglycerols and is necessary for VLDL particles to pass through the granulosa basal lamina and reach the receptors located on the oocyte surface. New ultrastructural data show that some proximal tubule cells of bird kidney secrete generic VLDL, perhaps providing energy and other VLDL-associated nutrients to tissues bypassed by VLDLy. Birds are an apoB100-only species, providing a natural in vivo model with which to investigate mechanisms of apoB100 VLDL assembly. Preliminary studies of liver lipoprotein assembly intermediates isolated from the biosynthetic membranes (endoplasmic reticulum) of the laying hen are consistent with the presence of both putative first- and second-step precursor particles of VLDLy. These findings suggest that the two-step mechanism of apoB core lipidation is an ancient development in apoB biology, handed down to mammals from oviparous ancestors.  (+info)

Vitrification of mouse germinal vesicle oocytes: effect of treatment temperature and egg yolk on chromatin and spindle normality and cumulus integrity. (2/521)

The success rates for cryopreservation of immature oocytes from several species including human remain low, in contrast to major improvements with mature oocytes. In this study, a new approach has been developed using a short exposure ultra-rapid freezing protocol, examining the effect of temperature and egg yolk (two factors which may be expected to influence membrane flexibility) on the cryostability of immature mouse oocytes and cumulus complexes. These two factors were tested in various patterns for their cryoprotective effect using ethylene glycol as the principal cryoprotectant. The results showed that 37 degrees C pre- and post-freeze exposure significantly improved both survival and normal spindle configuration after in-vitro maturation. Egg yolk was found to produce further beneficial effects on both the oocyte and cumulus cell integrity, with the best effects being obtained at 37 degrees C with inclusion of egg yolk both before and after the freezing. This protocol produced > 80% normal survival post-thaw with intact and attached cumulus complex, 84% maturation rate and 45% normal metaphase configuration. In summary, a unique combination of high survival and meiotic normality together with good preservation of the attached cumulus cell mass has been achieved using a simple new vitrification procedure.  (+info)

Select 3-hydroxy-3-methylglutaryl-coenzyme A reductase inhibitors vary in their ability to reduce egg yolk cholesterol levels in laying hens through alteration of hepatic cholesterol biosynthesis and plasma VLDL composition. (3/521)

The inability to markedly attenuate cholesterol levels in chicken eggs has led to speculation that cholesterol is essential for yolk formation and that egg production would cease when yolk cholesterol deposition was inadequate for embryonic survival. However, this critical level hypothesis remains unproven. Here, we determine the relative responsiveness of laying hens to three select inhibitors of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGR), the rate-limiting enzyme of cholesterol biosynthesis. A control diet, either alone or supplemented with one of two dietary levels (0.03 or 0.06%) of atorvastatin, lovastatin, or simvastatin, was fed to White Leghorn hens for 5 wk. Liver cholesterol concentrations (mg/g tissue) were decreased (P 0.05), and 22% (P 0.05), and -3% (P > 0.05)], was much less affected. We concluded that cholesterol per se may not be an obligatory component for yolk formation in chickens and, as such, may be amenable to further pharmacological manipulation  (+info)

Genetic analysis of vitellogenesis in Drosophila melanogaster: the identification of a temperature-sensitive mutation affecting one of the yolk proteins. (4/521)

A number of female sterile mutations on the first and third chromosomes of Drosophila melanogaster have been screened for defects in the yolk proteins using polyacrylamide gel electrophoresis. Two new mutants were identified. 6m45 accumulates all three yolk proteins (YP1, YP2 and YP3) in the haemolymph but they are all absent from the ovaries suggesting it is a yolk-protein-uptake mutant. In contrast, 1163 is a temperature-sensitive mutation with a large reduction in the quantity of YP1 in the haemolymph and ovaries at 29 degrees C. Both mutants are autonomous in ovary transplant experiments.  (+info)

Plasma iron transport during egg laying and after oestrogen administration in the domestic fowl (Gallus domesticus). (5/521)

The concentrations of 59Fe and of radioiodinated transferrin and albumin were measured in the blood, liver, spleen, bone marrow and ova at different times after the injection of transferrin-bound 59Fe and the labelled proteins into non-laying, laying and oestrogen treated chickens. In the egg-laying and oestrogen-treated birds the 59Fe of the plasma was rapidly transferred from transferrin to another component with the properties of th phosphoprotein, phosvitin. Radioactive iron, and labelled transferrin and albumin to a lesser extent, entered the ova only while they were in the ovary. Relatively more labelled transferrin than albumin was found in all the tissues studied except in the ova, in which the two labelled proteins were present in the same relative concentration as in the plasma. It is concluded that, during egg laying and after oestrogen treatment, plasma iron bound to transferrin is taken up by the liver, incorporated into phosvitin and is then secreted into the plasma leading to elevation of the plasma iron concentration and transfer of iron to the ova.  (+info)

Lutein and zeaxanthin concentrations in plasma after dietary supplementation with egg yolk. (6/521)

BACKGROUND: The food matrix in which carotenoids are found affects their bioavailability. Lutein and zeaxanthin are abundant in egg yolks and accumulate in the macular region of the retina, where they may affect visual function. OBJECTIVE: We sought to determine whether plasma lutein and zeaxanthin concentrations are elevated after dietary supplementation with egg yolk. DESIGN: Eleven moderately hypercholesterolemic men and women consumed 2 separate baseline diets, which contained 29-33% of energy as total fat, with 20% of energy as either beef tallow or corn oil. These diets were supplemented with cooked chicken egg yolks (1.3 egg yolks/d for an intake of 10.4 MJ). Each subject consumed all 4 diets. Each diet was consumed for 4.5 wk, with a washout period of >/=2 wk between diet phases. At the end of each diet phase, fasting morning plasma samples were collected and stored for carotenoid analysis by HPLC. Commercial chicken egg yolks were analyzed for carotenoids and cholesterol. RESULTS: Egg yolk supplementation of the beef tallow diet increased plasma lutein by 28% (P < 0.05) and zeaxanthin by 142% (P < 0.001); supplementation of the corn oil diet increased plasma lutein by 50% (P < 0.05) and zeaxanthin by 114% (P < 0.001). Changes in plasma lycopene and beta-carotene were variable, with no consistent trend. Egg yolk supplementation increased plasma LDL-cholesterol concentrations by 8-11% (P < 0.05). CONCLUSIONS: Egg yolk is a highly bioavailable source of lutein and zeaxanthin. The benefit of introducing these carotenoids into the diet with egg yolk is counterbalanced by potential LDL-cholesterol elevation from the added dietary cholesterol.  (+info)

The carbohydrates of the isoforms of three avian riboflavin-binding proteins. (7/521)

The carbohydrate chains of nine isoforms of chicken egg-white riboflavin-binding protein (RfBP) and six isoforms each of quail egg-white and yolk RfBP have been structurally characterized. The two N-glycosylation sites, Asn36 and Asn147, of the most abundant isoform of each of the three proteins were analyzed in further detail leading to the identification of different glycosylation patterns. In both chicken and quail egg-white RfBP the carbohydrates attached to position 36 had a lower degree of branching and, in the case of the quail protein, this site was only partially glycosylated. A very heterogeneous mixture of complex structures was characteristic of the other glycosylation site. Analysis of the two sites in quail yolk RfBP confirmed this result which agrees with what has been established for hen yolk RfBP. The presence in the three proteins of a highly heterogeneous mixture of differently branched glycans suggests that the differences in isoelectric points, which is a peculiarity of the different isoforms, are probably indeed due to differences in carbohydrate structure.  (+info)

Growth of Salmonella typhimurium and Salmonella enteritidis in egg yolks from highly immunized hens. (8/521)

This experiment was conducted to ascertain whether the growth of Salmonella Enteritidis (SE) or Salmonella Typhimurium (ST) would be suppressed in the presence of antibodies contained in egg yolks. Specific pathogen-free chickens (102 days of age) were subcutaneously immunized with oil-adjuvanted bacterin of SE or ST, twice within a four-week interval. During 160 to 170 days of age, eggs were collected, the yolks were removed and mixed with an equal volume of physiological buffered saline, inoculated with ten colony forming units (CFU) of SE or ST, and incubated at 37 degrees C or 20 degrees C for 23 hr. The growth of organisms in each yolk solution was examined. The egg yolk derived from non-immunized hens was examined in the same manner as the controls. There was no difference in the growth titer between the antibody-positive yolk and the negative yolk. The result suggests that the antibodies in the yolk do not influence the growth of each organism, even if the hens are highly immunized.  (+info)