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Rankin, T. L., Z. B. Tong, P. E. Castle, E. Lee, R. Gore-Langton, L. M. Nelson und J. Dean. „Human ZP3 restores fertility in Zp3 null mice without affecting order-specific sperm binding“. Development 125, Nr. 13 (01.07.1998): 2415–24. http://dx.doi.org/10.1242/dev.125.13.2415.
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The mammalian zona pellucida surrounding ovulated eggs mediates sperm binding at fertilization, provides a postfertilization block to polyspermy, and facilitates passage of pre-implantation embryos down the oviduct. Although the three zona proteins (ZP1, ZP2, ZP3) are well conserved, mammalian fertilization is relatively specific and human sperm do not bind to the mouse zona pellucida. There are considerable in vitro data that ZP3 acts as a primary sperm adhesion molecule in mice and, by analogy, a similar role has been postulated for human ZP3. Genetically altered mice lacking ZP3 (Zp3(tm/tm)) do not form a zona pellucida and are infertile. To rescue this phenotype, transgenic mice expressing human ZP3 (67% identical to mouse ZP3) were produced and bred with Zp3(tm/tm) null mice. The resultant human ZP3 rescue females had chimeric zonae pellucidae composed of mouse ZP1, mouse ZP2 and human ZP3. Human ZP3 expressed in mouse oocytes had an apparent mass (64 kDa) indistinguishable from native human ZP3 and distinct from mouse ZP3 (83 kDa). Despite the presence of human ZP3, human sperm did not bind to the chimeric zona pellucida, and notwithstanding the absence of mouse ZP3, mouse sperm bound to ovulated eggs in vitro and fertility was restored in vivo. These data have implications regarding the molecular basis of mouse and human sperm binding to their respective zonae pellucidae.
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Cao, Zuowu, Chuncheng Nie, Yan Xie und Dongqin Cai. „The bioactivities of the central segment of Zp2 polypeptide“. Zygote 24, Nr. 5 (19.05.2016): 768–74. http://dx.doi.org/10.1017/s0967199416000095.
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SummaryIn order to understand the role of the protein zona pellucida 2 in fertilization, an antibody against a central segment of the zona pellucida 2 peptide, segment 190–505 (Z2eH), was prepared. The influence of the antibody on sperm–zona interaction was tested using the sperm–egg binding assay. The effect of the antibody on fertility was evaluated by passive immunization with anti-Z2eH antibody. Immunohistochemical assay showed that an antibody from rabbit reacted specifically with the natural zona pellucida on mouse ovarian sections. Immunofluorescence assay showed that the antibody bound specifically to the zonae pellucidae of the ovulated oocytes and 2-cell embryos after passive immunization. The antibody-treated oocytes bound capacitated sperm as control oocytes, passive immunization did not impede the action of sperm to fertilize the oocyte in vivo. These findings suggest that the central peptide of ZP2 (190–505) is immunogenic and contains zona pellucida-specific epitopes, however the central polypeptide might not be the crucial part from which to construct a functional domain to bind sperm.
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Lopez, L. C., E. M. Bayna, D. Litoff, N. L. Shaper, J. H. Shaper und B. D. Shur. „Receptor function of mouse sperm surface galactosyltransferase during fertilization.“ Journal of Cell Biology 101, Nr. 4 (01.10.1985): 1501–10. http://dx.doi.org/10.1083/jcb.101.4.1501.
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Past studies from this laboratory have suggested that mouse sperm binding to the egg zona pellucida is mediated by a sperm galactosyltransferase (GalTase), which recognizes and binds to terminal N-acetylglucosamine (GlcNAc) residues in the zona pellucida (Shur, B. D., and N. G. Hall, 1982, J. Cell Biol. 95:567-573; 95:574-579). We now present evidence that directly supports this mechanism for gamete binding. GalTase was purified to homogeneity by sequential affinity-chromatography on GlcNAc-agarose and alpha-lactalbumin-agarose columns. The purified enzyme produced a dose-dependent inhibition of sperm binding to the zona pellucida, relative to controls. To inhibit sperm/zona binding, GalTase had to retain its native conformation, since neither heat-inactivated nor Mn++-deficient GalTase inhibited sperm binding. GalTase inhibition of sperm/zona binding was not due to steric blocking of an adjacent sperm receptor on the zona, since GalTase could be released from the zona pellucida by forced galactosylation with UDPGal, and the resulting galactosylated zona was still incapable of binding sperm. In control experiments, when UDPGal was replaced with the inappropriate sugar nucleotide, UDPglucose, sperm binding to the zona pellucida remained normal after the adsorbed GalTase was washed away. The addition of UDPGal produced a dose-dependent inhibition of sperm/zona binding, and also dissociated preformed sperm/zona adhesions by catalyzing the release of the sperm GalTase from its GlcNAc substrate in the zona pellucida. Under identical conditions, UDP-glucose had no effect on sperm binding to the zona pellucida. The ability of UDPGal to dissociate sperm/zona adhesions was both time- and temperature-dependent. UDPGal produced nearly total inhibition of sperm/zona binding when the zonae pellucidae were first galactosylated to reduce the number of GalTase binding sites. Finally, monospecific anti-GalTase IgG and its Fab fragments produced a dose-dependent inhibition of sperm/zona binding and concomitantly blocked sperm GalTase catalytic activity. Preimmune IgG or anti-mouse brain IgG, which also binds to the sperm surface, had no effect. The sperm GalTase was localized by indirect immunofluorescence to a discrete plasma membrane domain on the dorsal surface of the anterior head overlying the intact acrosome. These results, along with earlier studies, show clearly that sperm GalTase serves as a principal gamete receptor during fertilization.
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Baibakov, Boris, Nathan A. Boggs, Belinda Yauger, Galina Baibakov und Jurrien Dean. „Human sperm bind to the N-terminal domain of ZP2 in humanized zonae pellucidae in transgenic mice“. Journal of Cell Biology 197, Nr. 7 (25.06.2012): 897–905. http://dx.doi.org/10.1083/jcb.201203062.
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Fertilization requires taxon-specific gamete recognition, and human sperm do not bind to zonae pellucidae (ZP1–3) surrounding mouse eggs. Using transgenesis to replace endogenous mouse proteins with human homologues, gain-of-function sperm-binding assays were established to evaluate human gamete recognition. Human sperm bound only to zonae pellucidae containing human ZP2, either alone or coexpressed with other human zona proteins. Binding to the humanized matrix was a dominant effect that resulted in human sperm penetration of the zona pellucida and accumulation in the perivitelline space, where they were unable to fuse with mouse eggs. Using recombinant peptides, the site of gamete recognition was located to a defined domain in the N terminus of ZP2. These results provide experimental evidence for the role of ZP2 in mediating sperm binding to the zona pellucida and support a model in which human sperm–egg recognition is dependent on an N-terminal domain of ZP2, which is degraded after fertilization to provide a definitive block to polyspermy.
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Brown, C. R., und W. K. T. Cheng. „Changes in composition of the porcine zona pellucida during development of the oocyte to the 2- to 4-cell embryo“. Development 92, Nr. 1 (01.03.1986): 183–91. http://dx.doi.org/10.1242/dev.92.1.183.
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Our objective was to identify any changes that occur in the composition of the porcine zona pellucida during development of the 2- to 4-cell embryo from the oocyte. Oocytes, unfertilized eggs and single and 2- to 4-cell embryos have been recovered surgically and their zonae pellucidae 125I-labelled and analysed individually by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The zonae from ovulated eggs possessed two major glycoproteins Mr 250000 and 90000 which were absent from follicular oocytes but present in the fluid from the oestrus, but not luteal, oviduct. The glycoproteins remained on the zona pellucida of 2- to 4-cell embryos whose analysis showed the presence of additional polypeptides of Mr 150000, 57000, 50000 and 25000. It is concluded (i) that shortly after ovulation, and in spite of the presence around the egg of cumulus oophorus and corona radiata cells, significant amounts of oviducal glycoproteins are able to bind firmly to the zona pellucida, and (ii) that after contact with spermatozoa there is evidence of a limited hydrolysis of the structure by the sperm protease acrosin.
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Moreno, R. D., M. S. Sepúlveda, A. de Ioannes und C. Barros. „The polysulphate binding domain of human proacrosin/acrosin is involved in both the enzyme activation and spermatozoa-zona pellucida interaction“. Zygote 6, Nr. 1 (Februar 1998): 75–83. http://dx.doi.org/10.1017/s0967199400005104.
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SummaryMammalian acrosin is a protease present as a zymogen in the acrosome of a non-reacted mammalian sperm, and in vitro is able to carry out limited hydrolysis of homologous and heterologous zonae pellucidae. On the other hand, sulphated polymers and zona pellcida glycoproteins bind to acrosin on a domain different from the active site, named the polysulphate binding domain (PSBD). Thus it is believed that acrosome-reacted spermatozoa bind to glycan chains of the zona pellucida through PSBD participating as secondary binding receptor. The aim of the present work was to study the role of PSBD during both human gamete interaction and acrosin activation. In this work we present evidence that the anti-human acrosin monoclonal antibody C5F10 is directed to an epitope located on or near the PSBD on human proacrosin/acrosin. Moreover, we show that this antibody is able to inhibit both proacrosin activation induced by fucoidan and the sperm binding to the zona pellucida. Our results suggest that the same PSBD is involved in both sperm secondary binding, during zona pellucida penetration, and proacrosin activation.
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Mertens, E., U. Besenfelder, M. Gilles, M. Hölker, F. Rings, V. Havlicek, K. Schellander und A. Herrler. „190 INFLUENCE OF IN VITRO CULTURE OF BOVINE EMBRYOS ON THE STRUCTURE OF THE ZONA PELLUCIDA“. Reproduction, Fertility and Development 19, Nr. 1 (2007): 211. http://dx.doi.org/10.1071/rdv19n1ab190.
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The zona pellucida is an extracellular structure at the direct interface between the maternal and embryonic sides, through which all signals of the embryo–maternal dialogue as well as nutritional factors have to pass. Up to now there has been no investigation as to whether in vitro culture influences the structure of the zona pellucida compared to that of in vivo embryos. Therefore, in vitro (oocyte, zygote, 2-, 4-, 8-, 16-cell, morula, and Day 7 blastocyst, using the protocol published by Nganvongpanit et al. 2006 Reproduction 131, 861–874) and in vivo (zygote, 4-cell, morula, and blastocyst) embryos were prepared for microscopical investigation. In total, 191 in vitro and 99 in vivo embryos of quality 1 and 2 from at least 2 replicates were used. Araldit-embedded embryos were semi-thin-sectioned and stained with hematoxilin. A morphometrical evaluation was performed to determine the percentage of the more reticular outer part compared to the total thickness of the zona. Furthermore, the total thickness of the zona pellucida was compared between in vitro and in vivo embryos. In parallel, embryos were analyzed by scanning electron microscopy. Up to the 16-cell stage, the zona of in vivo and in vitro embryos is similar, but in vivo morulae and blastocysts show significantly thicker zonae than the in vitro stages. The reticular part of the zona is thicker in in vivo embryos than in in vitro embryos (30.2 � 2.1% vs. 12.4 � 1.8%, respectively). Investigating the pores of the zona pellucida, in vivo morulae/blastocysts show smaller-sized pores than in those derived in vitro. Most of the in vivo morulae/blastocysts are totally covered by secreted granules, and therefore the pores could not be investigated. Furthermore, 30-50% of the in vitro embryos show partly degenerated outer layers of the zona pellucida. This investigation demonstrates that in vitro and in vivo zonae pellucidae are significantly different, reflecting a negative influence of the IVM and IVC.
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Wassarman, Paul M. „Zona Pellucida Glycoproteins“. Annual Review of Biochemistry 57, Nr. 1 (Juni 1988): 415–42. http://dx.doi.org/10.1146/annurev.bi.57.070188.002215.
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Wassarman, Paul M. „Zona Pellucida Glycoproteins“. Journal of Biological Chemistry 283, Nr. 36 (06.06.2008): 24285–89. http://dx.doi.org/10.1074/jbc.r800027200.
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Avella, Matteo A., Boris Baibakov und Jurrien Dean. „A single domain of the ZP2 zona pellucida protein mediates gamete recognition in mice and humans“. Journal of Cell Biology 205, Nr. 6 (16.06.2014): 801–9. http://dx.doi.org/10.1083/jcb.201404025.
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The extracellular zona pellucida surrounds ovulated eggs and mediates gamete recognition that is essential for mammalian fertilization. Zonae matrices contain three (mouse) or four (human) glycoproteins (ZP1–4), but which protein binds sperm remains controversial. A defining characteristic of an essential zona ligand is sterility after genetic ablation. We have established transgenic mice expressing human ZP4 that form zonae pellucidae in the absence of mouse or human ZP2. Neither mouse nor human sperm bound to these ovulated eggs, and these female mice were sterile after in vivo insemination or natural mating. The same phenotype was observed with truncated ZP2 that lacks a restricted domain within ZP251–149. Chimeric human/mouse ZP2 isoforms expressed in transgenic mice and recombinant peptide bead assays confirmed that this region accounts for the taxon specificity observed in human–mouse gamete recognition. These observations in transgenic mice document that the ZP251–149 sperm-binding domain is necessary for human and mouse gamete recognition and penetration through the zona pellucida.
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The ability of the zona pellucida to mediate the species specific recognition of spermatozoa is due to a glycoprotein constituent of this structure, known as ZP3. In view of its important role in the initiation of fertilization, ZP3 has been identified as a suitable candidate for the development of a contraceptive vaccine. In order to generate recombinant marmoset ZP3 for immunization purposes a full length 1.3 kb insert encoding for marmoset ZP3 was cloned downstream of the malE gene to generate a fusion protein containing marZP3 and a maltose binding domain. This protein was found to be generated in a soluble form in aqueous solutions and the antigenic integrity of this molecule was demonstrated by it capacity to be recognized by a monoclonal antibody raised against human ZP3. This full length fusion protein has been purified by anion exchange chromatography and used to generate polyclonal antibodies. In addition to these in vitro studies on the generation of a recombinant marZP3 for active immunization purposes, in vivo studies have also been performed on the induction of active immunity against porcine ZP3. These studies have demonstrated that an important side effect of induction of immunity against a heterologous ZP3 antigen involves the depletion of the primordial follicle pool. Moreover this pathology could be transferred to non-immunized recipients by the passive transfer of antibody. These data raise the important question as to whether a similar pathology would be induced if homologous zona antigens were used for the induction of immunity. As a result of the work descriebd in this thesis, this question can now be addressed in the marmoset monkey using recombinant marZP3 as antigen.
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Chapman, Jamie. „The marsupial zona pellucida : its structure and glycoconjugate content“. Title page, abstract and contents only, 2003. http://web4.library.adelaide.edu.au/theses/09PH/09phc4661.pdf.
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Bibliography: leaves 262-298. This thesis investigated the structure and glycoconjugate composition of the zona pellucida (ZP) surrounding marsupial oocytes and the changes that occur during ovarian development, following ovulation, and following cortical granule exocytosis. The glycoconjugates of the oviduct epithelial lining of the brushtail possum around the time of ovulation were also examined to determine if there was any contribution of the oviductal secretions to the post-ovulatory ZP.
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Gaboriau, David Claude Andre. „Binding of boar sperm proacrosin to the zona pellucida“. Thesis, University of Cambridge, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.613079.
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Chung, Man-kin, und 鍾文健. „Biological characterization of cumulus glycodelin on humanspermatozoa-zona pellucida interaction“. Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2009. http://hub.hku.hk/bib/B42182633.
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Lacey, Helen Ann. „Production and characterisation of recombinant human zona pellucida glycoprotein 2“. Thesis, University of Sheffield, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.322910.
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Witzendorff, Dorothee von. „Das Glykom und Proteom der porcinen Zona pellucida ein massenspektrometrischer Ansatz /“. [S.l.] : [s.n.], 2006. http://deposit.ddb.de/cgi-bin/dokserv?idn=981929931.
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Pfisterer, Susanne Charlotte Martha. „Herstellung, Charakterisierung und Einsatz von anti-Zona pellucida Protein 3 Peptidantiseren“. [S.l.] : [s.n.], 1999. http://deposit.ddb.de/cgi-bin/dokserv?idn=958759006.
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Chung, Man-kin. „Biological characterization of cumulus glycodelin on human spermatozoa-zona pellucida interaction“. Click to view the E-thesis via HKUTO, 2009. http://sunzi.lib.hku.hk/hkuto/record/B42182633.
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Ringleb, Jennifer. „Identifikation antigener Determinanten des ZPB2-Proteins der Hauskatze und Charakterisierung ihrer kontrazeptiven und immunogenen Eigenschaften“. Phd thesis, [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=974115282.
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Törmälä, R. M. (Reeta-Maria). „Human zona pellucida abnormalities:a genetic approach to the understanding of fertilization failure“. Doctoral thesis, Oulun yliopisto, 2016. http://urn.fi/urn:isbn:9789526212982.
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Abstract Despite the development of assisted reproduction technologies and significant advances in reproductive biology and medicine over the years the cause of infertility remains unexplained in 10–20% of cases. The cause of infertility in these cases may be connected to problems in fertilization or implantation and genetic factors may play a part in this. The zona pellucida (ZP) is an extracellular matrix surrounding the oocyte and early-stage embryos. It is important for folliculogenesis, fertilization and implantation. In humans, it is composed of four known ZP glycoproteins that all show varying degrees of structural and functional roles in reproduction. The aim of the present study was to examine the role of zona pellucida genes in cases of total fertilization failure and zona anomalies, and to study their expression in human fetal and adult ovaries. A total of 34 sequence variations were detected in genes expressing the four human ZP proteins (ZP1–ZP4) among women with fertilization failure and those with varying degrees of zona anomalies in their oocytes. Most of the variations were known single nucleotide polymorphisms, while three were novel findings. Women with fertilization failure had a higher mean number of sequence variations in ZP1 and ZP3 when compared with controls. Some of the most frequent zona anomalies may be at least partly explained by sequence variations in ZP1–ZP4 genes. In fetal life, the expression of ZP3 protein and mRNA could already be detected as early as at the 11th week of gestation and it peaked at the 20th week, the time of primordial follicle formation. This suggests that components needed for zona matrix are already present well before the formation of the zona pellucida and may have a role in the development of primordial follicles. Expression of the transcription factor FIGLA (factor in the germline alpha) was increased at around the 20th week of gestation, supporting previous findings of its critical role in the initiation of folliculogenesis and primordial follicle formation. The present study adds to our knowledge on the currently still incomplete picture of formation of the ZP and fertilization in humans. Understanding the genetic background of infertile patients may help us to develop new tools not only to evaluate but also to improve their fertilization potential, and to choose the optimal treatment to achieve pregnancy Tiivistelmä Diagnostiikan kehityksestä huolimatta hedelmättömyyden syy jää edelleen epäselväksi 10–20 %:ssa tapauksista. Niissä hedelmättömyyden taustalla voivat olla munasolun hedelmöittymiseen ja kohtuun kiinnittymiseen liittyvät ongelmat, jotka voivat osittain johtua geneettisistä syistä. Alkiokuori on munasolua ja varhaista alkiota ympäröivä rakenne, joka osallistuu munarakkulan kehittymiseen, munasolun hedelmöittymiseen ja alkion tarttumiseen kohdun limakalvolle. Ihmisellä alkiokuori muodostuu neljästä tunnetusta alkiokuoriproteiinista (ZP1–ZP4). Tutkimuksessa selvitettiin alkiokuoriproteiineja koodittavien geenien vaikutusta hedelmällisyyteen potilailla, joilla koeputkihedelmöitys ei ollut tuottanut yhtään hedelmöittynyttä munasolua (engl. total fertilization failure, TFF) tai joiden munasoluissa havaittiin alkiokuoren rakennemuutoksia (engl. zona anomalies, ZA). Lisäksi selvitettiin alkiokuoriproteiinien ja niiden lähetti-RNA:n esiintymistä sikiöiden ja aikuisten munasarjoissa. TFF- ja ZA-potilaiden alkiokuoriproteiineja koodittavista geeneistä löytyi yhteensä 34 nukleotidimuutosta. Muutoksista kolme oli uusia löydöksiä, mutta suurin osa oli ennalta tunnettuja yhden nukleotidin polymorfioita eli geneettisiä monimuotoisuuskohtia. TFF-potilailla havaittiin ZP1- ja ZP3-geeneissä keskimäärin enemmän polymorfioita kuin verrokeilla. Myös osa yleisimmistä alkiokuoren rakennemuutoksista voidaan mahdollisesti selittää ZP1–ZP4-geeneistä löytyneillä polymorfioilla. Sikiöllä ZP3:n ilmentyminen oli havaittavissa jo 11. raskausviikolla, mutta voimakkainta se oli primordiaalivaiheen munarakkuloiden muodostumisen aikaan 20. raskausviikolla. Tämä voi viitata siihen, että ZP3 saattaa osallistua primordiaalivaiheen munarakkulan kehittymiseen ennen varsinaisen alkiokuoren muodostumista. ZP-geenien säätelytekijän FIGLA:n esiintyminen lisääntyi 20. raskausviikolla, mikä tukee aikaisempia havaintoja FIGLA:n merkityksestä munarakkulan kehittymisen aktivaatiossa ja primordiaalivaiheen munarakkuloiden muodostumisessa. Tämä tutkimus tuo lisätietoa alkiokuoren merkityksestä munasolun hedelmöittymisessä ja syventää tietämystämme alkiokuoren muodostumisesta ihmisellä. Hedelmättömyyden taustalla olevien geneettisten tekijöiden tunteminen voi parantaa lapsettomuuspotilaiden hedelmällisyyden arviointia ja auttaa löytämään heille parhaiten sopivan hoidon
Litscher, Eveline S., und Paul M. Wassarman. A Guide to Zona Pellucida Domain Proteins. Hoboken, NJ: John Wiley & Sons, Inc, 2015. http://dx.doi.org/10.1002/9781119044765.
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International Symposium on Prospects of Zona Pellucida Glycoproteins for Immunocontraception (1995 New Delhi, India). Zona pellucida glycoproteins and immunocontraception: Proceedings of the International Symposium on Prospects of Zona Pellucida Glycoproteins for Immunocontraception, New Delhi, India, 2-5 December 1995. Cambridge: Journal of Reproduction and Fertility, 1996.
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Zhang, Bing Rong. Evaluation of frozen-thawed semen from Swedish red and white AI bulls: With special reference to the relation between zona pellucida binding, in vitro fertilization and in vivo fertility. Uppsala: Sveriges Lantbruksuniversitet, 1998.
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Singer, Francis J. Treatment of wild horse mares with the immunocontraceptive porcine zonae pellucida vaccine: Effects on populations and behavior. [Place of publication not identified]: [U.S. Department of the Interior, Bureau of Land Management], 2005.
Hinsch, E., W. Hägele, W. B. Schill und K. D. Hinsch. „The Zona Pellucida “Receptors”“. In Advances in Experimental Medicine and Biology, 313–28. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5913-9_54.
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Modig, Carina, Liselotte Westerlund und Per-Erik Olsson. „Oocyte zona pellucida proteins“. In The Fish Oocyte, 113–39. Dordrecht: Springer Netherlands, 2007. http://dx.doi.org/10.1007/978-1-4020-6235-3_5.
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Dean, Jurrien. „Developmental Genetics of the Zona Pellucida“. In Ovarian Cell Interactions, 49–59. New York, NY: Springer New York, 1993. http://dx.doi.org/10.1007/978-1-4613-8336-9_4.
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Skinner, S. M., und B. S. Dunbar. „Species Variation in the Zona Pellucida“. In Immunological Approaches to Contraception and Promotion of Fertility, 251–68. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5140-5_29.
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Yonezawa, Naoto. „Posttranslational Modifications of Zona Pellucida Proteins“. In Advances in Experimental Medicine and Biology, 111–40. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0817-2_6.
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Overstreet, James W., und Catherine A. VandeVoort. „Sperm-Zona Pellucida Interaction in Macaques“. In In Vitro Fertilization and Embryo Transfer in Primates, 103–9. New York, NY: Springer New York, 1993. http://dx.doi.org/10.1007/978-1-4612-2716-8_6.
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Phillips, David M. „Structure and Function of the Zona Pellucida“. In Ultrastructure of the Ovary, 63–72. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-3944-5_4.
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Chamberlin, M. E., M. J. Ringuette, C. C. Philpott, S. M. Chamow und J. Dean. „Molecular Genetics of the Mouse Zona Pellucida“. In The Mammalian Egg Coat, 1–17. Berlin, Heidelberg: Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-74048-0_1.
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Sehgal, Shobha, und S. K. Gupta. „Disillusions and Hopes About Zona Pellucida Glycoproteins“. In Contraception Research for Today and the Nineties, 345–56. New York, NY: Springer New York, 1988. http://dx.doi.org/10.1007/978-1-4612-3746-4_32.
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Konferenzberichte zum Thema "Zona pellucida":
1
Descloux, Laurent, Sohi Rastegar, Guy P. Delacretaz, Artha J. Hollis und Klaus Rink. „Kinetics of zona pellucida thermodissolution in mouse zygotes“. In BiOS Europe '97, herausgegeben von Guy P. Delacretaz, Guilhem Godlewski, Roberto Pini, Rudolf W. Steiner und Lars O. Svaasand. SPIE, 1998. http://dx.doi.org/10.1117/12.297888.
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2
Murayama, Yoshinobu, Kenta Yoshida, Harutaka Takahashi, Jinji Mizuno, Kazuyuki Akaishi und Hiroaki Inui. „Softening of the mouse zona pellucida during oocyte maturation“. In 2013 35th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC). IEEE, 2013. http://dx.doi.org/10.1109/embc.2013.6611127.
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3
Yamanishi, Yoko, Takehito Mizunuma, Naoki Inomata, Shogo Kudo und Funihito Arai. „Soft scrubbing off of zona pellucida on disposable microfluidic chip“. In 2010 IEEE 23rd International Conference on Micro Electro Mechanical Systems (MEMS). IEEE, 2010. http://dx.doi.org/10.1109/memsys.2010.5442516.
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4
Oungoulian, Sevan R., Kelvin Chan, Jason Barritt, Casey A. McDonald, Alan B. Copperman, David Elad und Gerard A. Ateshian. „Influence of Zona Pellucida Area Expansion Stiffness on the Passive Response of Oocytes to Osmotic Loading“. In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53826.
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Annotation:
The zona pellucida (ZP) is a thick glycoprotein shell surrounding the mammalian egg cell (oocyte) that regulates spermatozoa access during fertilization and protects the zygote during early embryonic development [1]. Hardening of the zona pellucida over the cell fertilization cycle is a well-recognized phenomenon and has been investigated using contact methods to measure shear and bending elasticity from indentation and micropipette aspiration [2, 3]. However, the area elasticity of the ZP, which provides resistance to cell swelling under variable osmotic environments, has not yet been reported. A recently devised theoretical model [4] suggests that the ZP area expansion modulus may be determined through non-contact hypo-osmotic loading of the oocyte. If successful, this method may be suited for implementation by practicing fertility health professionals during routine manipulation.
5
Ediz, Kerem, und Nejat Olgac. „The Effect of Mercury in the Micro-Dynamics of Injection Pipettes“. In ASME 2003 International Mechanical Engineering Congress and Exposition. ASMEDC, 2003. http://dx.doi.org/10.1115/imece2003-55538.
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“Microinjection” is becoming increasingly important in molecular biology. These operations include the micromanipulation of cellular subjects, such as piercing procedure through the zona pellucida and the membrane in ICSI (intracytoplasmic sperm injection).
6
Karlsson, A., N. C. Overgaard und A. Heyden. „Automatic segmentation of zona pellucida in HMC images of human embryos“. In Proceedings of the 17th International Conference on Pattern Recognition, 2004. ICPR 2004. IEEE, 2004. http://dx.doi.org/10.1109/icpr.2004.1334580.
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7
Li, Yadi, Haibo Huang, Liguo Chen, Xiwei Gao, Jiaqi Huang, Xiangpeng Li und Zhan Yang. „An Automatic Measurement Method of Zona Pellucida Thickness Based on Coordinate Transformation“. In 2017 IEEE 7th Annual International Conference on CYBER Technology in Automation, Control, and Intelligent Systems (CYBER). IEEE, 2017. http://dx.doi.org/10.1109/cyber.2017.8446359.
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8
Hollis, Artha J., Sohi Rastegar, Guy P. Delacretaz, Laurent Descloux und Klaus Rink. „Characterization of the thermal field associated with laser microdrilling of zona pellucida“. In BiOS Europe '97, herausgegeben von Guy P. Delacretaz, Guilhem Godlewski, Roberto Pini, Rudolf W. Steiner und Lars O. Svaasand. SPIE, 1998. http://dx.doi.org/10.1117/12.297887.
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9
Fakan, Stanislav, Klaus Rink, Guy P. Delacretaz, Alfred Senn, Dorotha Nocera, Marc Germond und Rene-Paul Salathe. „1.48-um diode laser microdissection of the zona pellucida of mouse zygotes“. In Laser-Tissue Interaction V. SPIE, 1994. http://dx.doi.org/10.1117/12.182960.
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10
Rastegar, Sohi, Artha J. Hollis, Laurent Descloux, Klaus Rink, Guy P. Delacretaz, Alfred Senn, Dorotha Nocera und Marc Germond. „Analysis of localized drilling of zona pellucida by 1.48-μm diode laser“. In Photonics West '96, herausgegeben von Steven L. Jacques. SPIE, 1996. http://dx.doi.org/10.1117/12.239576.
