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Journal of Pediatric Surgery Apr 1984The authors describe a case of intestinal obstruction due to a mesodiverticular band, in which both vitelline artery and vein remnants were affirmed to be present...
The authors describe a case of intestinal obstruction due to a mesodiverticular band, in which both vitelline artery and vein remnants were affirmed to be present histologically. Reviewing case reports in literature, it was revealed that the vein found in the band was the right vitelline vein remnant and that this was an important fact which proved the hypothesis that the superior mesenteric vein derives from the right vitelline vein.
Topics: Arteries; Child, Preschool; Female; Humans; Intestinal Obstruction; Male; Meckel Diverticulum; Veins; Vitelline Membrane
PubMed: 6539377
DOI: 10.1016/s0022-3468(84)80453-4 -
Cryobiology Sep 2000Prior studies on cryopreserving embryos of several non-drosophilid flies established that two Drosophila melanogaster embryo cryopreservation protocols were not directly...
Prior studies on cryopreserving embryos of several non-drosophilid flies established that two Drosophila melanogaster embryo cryopreservation protocols were not directly suitable for use with these species. This paper describes our work on developing a protocol for cryopreservation of embryos of the housefly, Musca domestica. Significant progress was made when permeabilization of the vitelline membrane was optimized, a vitrification solution containing ethylene glycol, polyethylene glycol, and trehalose was formulated, and when cooling and recovery of the cryopreservation protocol included a step which passed the embryos through liquid nitrogen vapor. More than 70% of housefly embryos withstand treatments of dechorionation, permeabilization, loading with cryoprotectant, and dehydration in vitrification solution, but the cooling, warming, and poststorage rearing steps still cause a considerable reduction in survival. About 53% of the vitrified M. domestica embryos hatched into larvae. Relative to the percentage of the control adult emergence, about 13% of the embryos stored in liquid nitrogen developed into fertile adults. Hatching of the F(1) progeny of adults having been cryopreserved as embryos was similar to control levels.
Topics: 2-Propanol; Animals; Chromatography, High Pressure Liquid; Cryopreservation; Cryoprotective Agents; Culture Media; Desiccation; Embryo, Nonmammalian; Ethylene Glycol; Female; Fertility; Heptanes; Hexanes; Houseflies; Lipids; Male; Nitrogen; Permeability; Polyethylene Glycols; Solutions; Temperature; Trehalose; Vitelline Membrane
PubMed: 11034794
DOI: 10.1006/cryo.2000.2278 -
Journal of Embryology and Experimental... Dec 1959
Topics: Animals; Chickens; Congenital Abnormalities; Embryo, Mammalian; Embryo, Nonmammalian; Vitelline Membrane
PubMed: 14446742
DOI: No ID Found -
Developmental Biology Aug 1982
Topics: Animals; Antigens; Drosophila melanogaster; Female; Membrane Proteins; Time Factors; Vitelline Membrane
PubMed: 6811349
DOI: 10.1016/0012-1606(82)90177-4 -
Development, Growth & Differentiation Feb 1997The vitelline envelope (VE) is an extremely thin, acellular, proteinaceous coat that surrounds the extracellular surface of sea urchin eggs. Despite previous studies on... (Comparative Study)
Comparative Study
The vitelline envelope (VE) is an extremely thin, acellular, proteinaceous coat that surrounds the extracellular surface of sea urchin eggs. Despite previous studies on VE composition, structure and function, our understanding to the envelope is still incomplete at the molecular level. We have isolated VE components from intact, unfertilized Strongylocentrotus purpuratus eggs by reduction with alkaline dithiothreitol-see water solutions and have characterized the macromolecules by SDS-PAGE. There were eight major glycoprotein bands, including two high molecular weight components at 265 and 300 kDa, and several minor components. We have revealed, by lectin blot analysis, that most components contain mannose, while a subset of glycoproteins contain fucose and N-acetylglucosamine; galactose and sialic acid were also detected. The components in the VE preparations were compared with cell surface complex preparations by immunoblot analysis, using antisera against a VE preparation, a 305 kDa electrophoretically purified VE glycoprotein and an extracellular portion of the sea urchin egg recombinant 350 kDa sperm receptor. Serum against the recombinant sperm receptor reacted with a component of approximately 350 kDa on blots, but did not react with the 300 kDa component found in VE preparations. Therefore, we suggest these two glycoproteins are not the same.
Topics: Animals; Carbohydrates; Female; Immunochemistry; Male; Membrane Glycoproteins; Molecular Structure; Molecular Weight; Receptors, Cell Surface; Sea Urchins; Solubility; Sperm-Ovum Interactions; Vitelline Membrane
PubMed: 9079036
DOI: 10.1046/j.1440-169x.1997.00008.x -
The Journal of Endocrinology Nov 1992The major vitelline envelope proteins were detected in the plasma of female rainbow trout maturing under natural conditions by using the Western blot technique. Females...
The major vitelline envelope proteins were detected in the plasma of female rainbow trout maturing under natural conditions by using the Western blot technique. Females were sampled every month from July until ovulation in January. The amount of vitelline envelope proteins in plasma increased markedly as the gonads increased in size from 0.4 to about 15% of the total body weight. The plasma level of oestradiol-17 beta largely followed the alterations in the amount of vitelline envelope proteins, indicating the endocrine control of vitelline envelope protein synthesis. In addition, plasma vitellogenin changed in a manner that resembled the changes in the amount of plasma vitelline envelope proteins. The appearance and growth of the vitelline envelope during oocyte development was demonstrated using immunohistochemical methods. The vitelline envelopes from oocytes at different stages of development were immunoreactive with the antibodies directed against the major vitelline envelope proteins. No immunoreactivity could be observed in the ooplasm or in the surrounding follicular cells, which indicated that the major vitelline envelope proteins were of extraovarian origin. The present study further supports the hypothesis that the major protein constituents of the vitelline envelope in teleosts are under the endocrine control of oestradiol-17 beta and that the site of synthesis is outside the ovary.
Topics: Animals; Blotting, Western; Egg Proteins; Female; Immunohistochemistry; Oocytes; Trout; Vitelline Membrane
PubMed: 1474337
DOI: 10.1677/joe.0.1350303 -
Scientific Reports Jan 2019In the ascidian Ciona robusta (formerly C. intestinalis type A), the mechanism underlying sperm penetration through the egg investment remains unknown. We previously...
In the ascidian Ciona robusta (formerly C. intestinalis type A), the mechanism underlying sperm penetration through the egg investment remains unknown. We previously reported that proteins containing both an astacin metalloprotease domain and thrombospondin type 1 repeats are abundant in the sperm surface protein-enriched fraction of C. robusta. Here we investigated the involvement of those proteins in fertilisation. We refined the sequences of astacin metalloproteases, confirmed that five of them are present in the sperm, and labelled them as tunicate astacin and thrombospondin type 1 repeat-containing (Tast) proteins. Fertilisation of C. robusta eggs was potently inhibited by a metalloprotease inhibitor GM6001. The eggs cleaved normally when they were vitelline coat-free or the inhibitor was added after insemination. Furthermore, vitelline coat proteins were degraded after incubation with intact sperm. These results suggest that sperm metalloproteases are indispensable for fertilisation, probably owing to direct or indirect mediation of vitelline-coat digestion during sperm penetration. TALEN-mediated knockout of Tast genes and the presence of GM6001 impaired larval development at the metamorphic stage, suggesting that Tast gene products play a key role in late development.
Topics: Animals; Ciona intestinalis; Egg Proteins; Female; Male; Metalloproteases; Sperm-Ovum Interactions; Spermatozoa; Vitelline Membrane
PubMed: 30700775
DOI: 10.1038/s41598-018-37721-1 -
Molecular Ecology Dec 2003Sex allocation studies seek to ascertain whether mothers manipulate offspring sex ratio prior to ovulation. To do so, DNA for molecular sexing should be collected as... (Comparative Study)
Comparative Study
Sex allocation studies seek to ascertain whether mothers manipulate offspring sex ratio prior to ovulation. To do so, DNA for molecular sexing should be collected as soon after conception as possible, but instead neonates are usually sampled. Here, we aim to identify and quantify some of the problems associated with using molecular techniques to identify the sex of newly laid avian eggs. From both fertilized and unfertilized chicken (Gallus gallus) eggs, we sampled (1) the blastoderm/disc, (2) vitelline membrane and (3) a mixture of (1) and (2). Thus, we replicated scenarios under which contaminated samples are taken and/or unfertilized eggs are not identified as such and are sampled. We found that two commonly used molecular sexing tests, based on the CHD-1 genes, differed in sensitivity, but this did not always predict their ability to sex egg samples. The vitelline membrane was a considerable source of maternal and probably paternal contamination. Fertile eggs were regularly assigned the wrong sex when vitelline membrane contaminated the blastoderm sample. The membrane of unfertilized eggs was always female, i.e. maternal DNA had been amplified. DNA was amplified from 47 to 63% of unfertilized blastodiscs, even though it was highly unlikely that DNA from a single haploid cell could be amplified reliably using these polymerase chain reaction (PCR) techniques. Surprisingly, the blastodiscs were identified as both males and females. We suggest that in these cases only maternal DNA was amplified, and that 'false' males, Z not ZZ, were detected. This was due to the reduced ability of both sets of primers to anneal to the W chromosome compared to the Z chromosome at low DNA concentrations. Overall, our data suggested that estimates of primary sex ratios based on newly laid eggs will be appreciably inaccurate.
Topics: Animals; Blastoderm; Chickens; Electrophoresis, Polyacrylamide Gel; Ovum; Polymerase Chain Reaction; Sensitivity and Specificity; Sex Determination Processes; Sex Ratio; Vitelline Membrane
PubMed: 14629359
DOI: 10.1046/j.1365-294x.2003.02007.x -
Journal of Cellular Biochemistry 1986An amphibian egg recovered from the body cavity is enclosed by a coelomic egg envelope. Upon transport down the oviduct, the envelope is converted to the vitelline...
An amphibian egg recovered from the body cavity is enclosed by a coelomic egg envelope. Upon transport down the oviduct, the envelope is converted to the vitelline envelope. The coelomic and vitelline envelopes are distinct in terms of sperm penetrability, ultrastructural morphology, and radioiodination profiles. In this study, the macromolecular compositions of these two envelopes were determined. Isolated envelopes were compared by one- and two-dimensional gel electrophoresis, peptide mapping, and radiolabeling. A protein with a molecular weight of 57,000 (57K) was present in the vitelline envelope but was absent in the coelomic envelope. A glycoprotein with a molecular weight of 43K in the coelomic envelope was converted to a component with a molecular weight of 41K in the vitelline envelope. The 43K-molecular weight component of the coelomic envelopes could be radioiodinated by lactoperoxidase but no labeling of the 41K-molecular weight component occurred in the vitelline envelope. Peptide mapping using limited proteolysis established that the 43K-molecular weight component of the coelomic envelope was a precursor to the 41K-molecular weight component of the vitelline envelope. These molecular alterations may underlie the ultrastructural and physiological changes occurring in these envelopes.
Topics: Animals; Electrophoresis, Polyacrylamide Gel; Female; Glycoproteins; Membrane Proteins; Molecular Weight; Oviducts; Ovum; Peptide Fragments; Vitelline Membrane; Xenopus laevis
PubMed: 3711153
DOI: 10.1002/jcb.240300407 -
Journal of Cell Science Aug 2001A study was made of the localization and assembly of the VM32E protein, a putative vitelline membrane component of the Drosophila eggshell. The results highlight some...
A study was made of the localization and assembly of the VM32E protein, a putative vitelline membrane component of the Drosophila eggshell. The results highlight some unique features of this protein compared with the other proteins of the same gene family. At the time of its synthesis (stage 10), the VM32E protein is not detectable in polar follicle cells. However, it is able to move in the extracellular space around the oocyte and, by stage 11 is uniformly distributed in the vitelline membrane. During the terminal stages of oogenesis the VM32E protein is partially released from the vitelline membrane and becomes localized in the endochorion layer also. By analyzing transgenic flies carrying variously truncated VM32E proteins, we could identify the protein domains required for the proper assembly of the VM32E protein in the eggshell. The highly conserved vitelline membrane domain is implicated in the early interactions with other components and is required for cross-linking VM32E protein in the vitelline membrane. The terminal carboxylic domain is necessary for localization to the endochorion layer. Protein with the C-end domain deleted is localized solely to the vitelline membrane and cross-linked only in laid eggs, as occurs for the other vitelline membrane proteins.
Topics: Amino Acid Sequence; Animals; Animals, Genetically Modified; Blotting, Western; Drosophila melanogaster; Egg Proteins; Epitopes; Female; Microscopy, Immunoelectron; Molecular Sequence Data; Mutation; Oogenesis; Protein Structure, Tertiary; Vitelline Membrane
PubMed: 11683415
DOI: 10.1242/jcs.114.15.2819