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Articles de revues sur le sujet « Zona pellucida »

Auteur : Grafiati

Publié le 4 juin 2021

Mis à jour le 25 juillet 2025

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1

Rankin, T. L., Z. B. Tong, P. E. Castle, et al. "Human ZP3 restores fertility in Zp3 null mice without affecting order-specific sperm binding." Development 125, no. 13 (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)

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2

Cao, Zuowu, Chuncheng Nie, Yan Xie, and Dongqin Cai. "The bioactivities of the central segment of Zp2 polypeptide." Zygote 24, no. 5 (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

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Lopez, L. C., E. M. Bayna, D. Litoff, N. L. Shaper, J. H. Shaper, and B. D. Shur. "Receptor function of mouse sperm surface galactosyltransferase during fertilization." Journal of Cell Biology 101, no. 4 (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

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Baibakov, Boris, Nathan A. Boggs, Belinda Yauger, Galina Baibakov, and Jurrien Dean. "Human sperm bind to the N-terminal domain of ZP2 in humanized zonae pellucidae in transgenic mice." Journal of Cell Biology 197, no. 7 (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, whe

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Brown, C. R., and 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, no. 1 (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 gly

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Moreno, R. D., M. S. Sepúlveda, A. de Ioannes, and C. Barros. "The polysulphate binding domain of human proacrosin/acrosin is involved in both the enzyme activation and spermatozoa-zona pellucida interaction." Zygote 6, no. 1 (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 PSB

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Mertens, E., U. Besenfelder, M. Gilles, et al. "190 INFLUENCE OF IN VITRO CULTURE OF BOVINE EMBRYOS ON THE STRUCTURE OF THE ZONA PELLUCIDA." Reproduction, Fertility and Development 19, no. 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)

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VANDEVOORT, CATHERINE A., GARY N. CHERR, and JAMES W. OVERSTREET. "Hyaluronic Acid Enhances the Zona Pellucida—Induced Acrosome Reaction of Macaque Sperm." Journal of Andrology 18, no. 1 (1997): 1–5. http://dx.doi.org/10.1002/j.1939-4640.1997.tb01869.x.

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ABSTRACT: Hyaluronic acid (HA) not only surrounds the zona pellucida as part of the cumulus matrix but also is present throughout the zona pellucida and the perivitelline space of many mammalian oocytes. However, most in vitro techniques to study sperm—oocyte interaction eliminate HA from the oocyte through enzymatic digestion and/or do not expose sperm to HA prior to zona pellucida binding. This study explores the effect of preincubation of sperm or oocytes with HA on sperm—zona pellucida binding and subsequent acrosome reaction of bound sperm. Cynomolgus macaque semen was washed, incubated,

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Avella, Matteo A., Boris Baibakov, and Jurrien Dean. "A single domain of the ZP2 zona pellucida protein mediates gamete recognition in mice and humans." Journal of Cell Biology 205, no. 6 (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

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Hoodbhoy, Tanya, and Jurrien Dean. "Insights into the molecular basis of sperm–egg recognition in mammals." Reproduction 127, no. 4 (2004): 417–22. http://dx.doi.org/10.1530/rep.1.00181.

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The zona pellucida surrounding the egg and pre-implantation embryo is required for in vivo fertility and early development. Explanatory models of sperm–egg recognition need to take into account the ability of sperm to bind to ovulated eggs, but not to two-cell embryos. For the last two decades, investigators have sought to identify an individual protein or carbohydrate side chain as the ‘sperm receptor’. However, recent genetic data in mice are more consistent with the three-dimensional structure of the zona pellucida, rather than a single protein (or carbohydrate), determining sperm binding.

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Wassarman, Paul M. "Zona Pellucida Glycoproteins." Annual Review of Biochemistry 57, no. 1 (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, no. 36 (2008): 24285–89. http://dx.doi.org/10.1074/jbc.r800027200.

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Gadella, B. M. "002. PIG SPERM EGG INTERACTION AND FORMATION OF A ZONA PELLUCIDA BINDING COMPLEX." Reproduction, Fertility and Development 22, no. 9 (2010): 2. http://dx.doi.org/10.1071/srb10abs002.

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In order to achieve fertilization sperm cells first need to successfully interact with the zona pellucida. Before reaching the zona pellucida the sperm cell undergoes extensive remodeling both in the male and female genital tract. These changes serve to mediate optimal recognition of the zona pellucida in the oviduct (primary zona pellucida binding). Optimal sperm-zona interactions are crucial for porcine oocyte fertilization: The zona pellucida- attached sperm cell is triggered to undergo the acrosome reaction and will also become hypermotile. Together these two responses allow the sperm cell

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14

Hasegawa, Akiko, Nozomi Kanazawa, Hideaki Sawai, Shinji Komori, and Koji Koyama. "Pig zona pellucida 2 (pZP2) protein does not participate in zona pellucida formation in transgenic mice." Reproduction 132, no. 3 (2006): 455–64. http://dx.doi.org/10.1530/rep.1.01016.

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The zona pellucida, an extracellular matrix surrounding mammalian oocytes, is composed of three or four glycoproteins. It is well known that the zona pellucida plays several critical roles during fertilization, but there is little knowledge about its formation. The purpose of this study is to examine whether a pig zona pellucida glycoprotein 2 (pZP2) would assemble with mouse zona pellucida. A transgene construct was prepared by placing a minigene encoding pZP2 downstream from the promoter of mouse ZP2. The result showed that the transgenic protein was synthesized in growing oocytes but not in

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15

Zhao, Ming, Lyn Gold, Heidi Dorward, et al. "Mutation of a Conserved Hydrophobic Patch PreventsIncorporation of ZP3 into the Zona Pellucida SurroundingMouseEggs." Molecular and Cellular Biology 23, no. 24 (2003): 8982–91. http://dx.doi.org/10.1128/mcb.23.24.8982-8991.2003.

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ABSTRACT Three glycoproteins (ZP1, ZP2, and ZP3) are synthesized in growing mouse oocytes and secreted to form an extracellular zona pellucida that mediates sperm binding and fertilization. Each has a signal peptide to direct it into a secretory pathway, a “zona” domain implicated in matrix polymerization and a transmembrane domain from which the ectodomain must be released. Using confocal microscopy and enhanced green fluorescent protein (EGFP), the intracellular trafficking of ZP3 was observed in growing mouse oocytes. Replacement of the zona domain with EGFP did not prevent secretion of ZP3

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LECLERC, PIERRE, and GREGORY S. KOPF. "Evidence for the Role of Heterotrimeric Guanine Nucleotide‐Binding Regulatory Proteins in the Regulation of the Mouse Sperm Adenylyl Cyclase by the Egg's Zona Pellucida." Journal of Andrology 20, no. 1 (1999): 126–34. http://dx.doi.org/10.1002/j.1939-4640.1999.tb02505.x.

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ABSTRACT: Sperm acrosomal exocytosis is the result of a complex set of signal transduction pathways activated physiologically by the egg's extracellular matrix, the zona pellucida. In the mouse, the zona pellucida has been demonstrated to induce an increase in sperm intracellular pH, Ca2+ and cyclic adenosine monophosphate (cAMP) concentrations as well as to activate proteins of the G, class (G; guanine nucleotide‐binding regulatory proteins). We recently reported that the mouse zona pellucida could activate the adenylyl cyclase of mouse sperm. It is not known, however, whether zona pellucida

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Saxena, D. K., I. Tanii, T. Oh-oka, K. Yoshinaga, and K. Toshimori. "Behaviour and role of an intra-acrosomal antigenic molecule, acrin 3, during mouse fertilisation in vitro." Zygote 8, no. 4 (2000): 329–38. http://dx.doi.org/10.1017/s096719940000112x.

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In this study we examined the behaviour and role of an intra-acrosomal antigenic molecule, acrin 3, during mouse fertilisation in vitro by assessing the effect of its pertinent monoclonal antibody mMC101. Experiments were designed to assess the effect of mMC101 on sperm–zona pellucida binding, the acrosome reaction, zona pellucida penetration, sperm–egg fusion, and fertilisation in vitro. mMC101 did not affect sperm motility or primary and secondary binding to the zona pellucida, but significantly inhibited fertilisation of zona-pellucida-intact oocytes in a dose-dependent manner. In the prese

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Kitchener, A. L., L. M. Edds, F. C. Molinia, and D. J. Kay. "Porcine zonae pellucidae immunisation of tammar wallabies (Macropus eugenii): fertility and immune responses." Reproduction, Fertility and Development 14, no. 4 (2002): 215. http://dx.doi.org/10.1071/rd01121.

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This study looked at the feasibility of targeting the zona pellucida for a contraceptive vaccine as a possible alternative method of control for overabundant macropods. Tammar wallabies, as a model for other macropods, were immunized with porcine zonae pellucidae (PZP) and were found to achieve significant concentrations of antibody to PZP in sera and reproductive tract fluids. Wallabies immunized with PZP exhibited lower ovarian weight with reduced numbers of antral follicles when compared with control animals. Wallabies were placed in a natural mating trial followed by an artificial insemina

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Thomson, M. S., D. A. Stringfellow, and L. H. Lauerman. "Adherence of Haemophilus somnus to bovine embryos after in vitro exposure." American Journal of Veterinary Research 49, no. 1 (1988): 63–66. https://doi.org/10.2460/ajvr.1988.49.01.63.

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SUMMARY Preimplantation bovine embryos were exposed in vitro to Haemophilus somnus to determine whether the bacteria would adhere to zona pellucida-intact embryos or would adhere to or infect zona pellucida-free embryos. The effect of H somnus on in vitro embryonic development also was investigated. After exposure to H somnus and before washing, some of the zona pellucida-intact embryos were held in antibiotic-containing medium. Haemophilus somnus was isolated from 10 of 42 zona pellucida-intact embryos and none of the zona pellucida-free embryos. Haemophilus somnus was not recovered from any

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Ishchuk, Mariia A., Evgeniia M. Komarova, Elena A. Lesik, et al. "DNA-fragmented sperm ability to bind to the zona pellucida." Journal of obstetrics and women's diseases 72, no. 6 (2023): 63–76. http://dx.doi.org/10.17816/jowd569417.

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BACKGROUND: A high percentage of the infertile couples are classified as having unexplained infertility. At the same time, male partners may have both normozoospermia and high level of sperm DNA fragmentation. The investigation of the selectivity of the oocyte zona pellucida for spermatozoa with fragmented DNA is an extremely promising direction. The novel data could improve sperm selection methods, which in turn will increase the efficiency of IVF cycles. AIM: The aim of this study was to assess the ability of spermatozoa with fragmented DNA to bind to the zona pellucida. MATERIAL

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Jovine, Luca, Costel C. Darie, Eveline S. Litscher, and Paul M. Wassarman. "ZONA PELLUCIDA DOMAIN PROTEINS." Annual Review of Biochemistry 74, no. 1 (2005): 83–114. http://dx.doi.org/10.1146/annurev.biochem.74.082803.133039.

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Nagy, A. "Removal of Zona Pellucida." Cold Spring Harbor Protocols 2006, no. 21 (2006): pdb.prot4421. http://dx.doi.org/10.1101/pdb.prot4421.

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Kinloch, R. A., S. Mortillo, and P. M. Wassarman. "Transgenic mouse eggs with functional hamster sperm receptors in their zona pellucida." Development 115, no. 4 (1992): 937–46. http://dx.doi.org/10.1242/dev.115.4.937.

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Sperm receptors are located in the mammalian egg extracellular coat, or zona pellucida. Mouse and hamster sperm receptor glycoproteins, mZP3 (83 × 10(3) M(r)) and hZP3 (56 × 10(3) M(r)), respectively, have very similar polypeptides (44 × 10(3) M(r); 81% identical) that are glycosylated to different extents. Purified mZP3 and hZP3 can bind to mouse sperm, prevent them from binding to eggs and induce them to undergo exocytosis, the acrosome reaction, in vitro. A DNA construct that placed the hZP3 gene under the control of mZP3 gene 5′-flanking sequence was used in this report to produce two mous

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Hoodbhoy, Tanya, Manuel Avilés, Boris Baibakov, et al. "ZP2 and ZP3 Traffic Independently within Oocytes prior to Assembly into the Extracellular Zona Pellucida." Molecular and Cellular Biology 26, no. 21 (2006): 7991–98. http://dx.doi.org/10.1128/mcb.00904-06.

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ABSTRACT The extracellular zona pellucida surrounds mammalian eggs and mediates taxon-specific sperm-egg recognition at fertilization. In mice, the zona pellucida is composed of three glycoproteins, but the presence of ZP2 and ZP3 is sufficient to form a biologically functional structure. Each zona pellucida glycoprotein is synthesized in growing oocytes and traffics through the endomembrane system to the cell surface, where it is released from a transmembrane domain and assembled into the insoluble zona pellucida matrix. ZP2 and ZP3 colocalize in the endoplasmic reticulum and in 1- to 5-μm po

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Rogers, K. D., B. A. Foster, E. J. Guiterrez, F. A. Diaz, and K. R. Bondioli. "41 Effects of Dimethyl Sulfoxide- or Glycerol-Based Vitrification Protocols on Zona Pellucida Hardening in Mature Bovine Oocytes." Reproduction, Fertility and Development 30, no. 1 (2018): 160. http://dx.doi.org/10.1071/rdv30n1ab41.

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Zona pellucida hardening is a natural process that occurs after oocyte fertilization to prevent polyspermic fertilization and to protect embryonic development. Pre-fertilization hardening of the zona pellucida, however, decreases fertilization rates. Cryoprotectants have also been shown to negatively affect fertilization rates, one possible mechanism of which being through zona hardening. This experiment was conducted to determine the effect of different cryoprotectants on hardening of the zona pellucida of mature bovine oocytes. Oocytes were collected by ovum pick-up (OPU) by transvaginal ult

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Zhao, Ming, Lyn Gold, Ann M. Ginsberg, Li-Fang Liang, and Jurrien Dean. "Conserved Furin Cleavage Site Not Essential for Secretion and Integration of ZP3 into the Extracellular Egg Coat of Transgenic Mice." Molecular and Cellular Biology 22, no. 9 (2002): 3111–20. http://dx.doi.org/10.1128/mcb.22.9.3111-3120.2002.

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ABSTRACT The extracellular zona pellucida surrounding mammalian eggs is formed by interactions of the ZP1, ZP2, and ZP3 glycoproteins. Female mice lacking ZP2 or ZP3 do not form a stable zona matrix and are sterile. The three zona proteins are synthesized in growing oocytes and secreted prior to incorporation into the zona pellucida. A well-conserved furin site upstream of a transmembrane domain near the carboxyl terminus of each has been implicated in the release of the zona ectodomains from oocytes. However, mutation of the furin site (RNRR → ANAA) does not affect the intracellular trafficki

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VANDEVOORT, CATHERINE A., THEODORE L. TOLLNER, and JAMES W. OVERSTREET. "Sperm‐Zona Pellucida Interaction in Cynomolgus and Rhesus Macaques." Journal of Andrology 13, no. 5 (1992): 428–32. http://dx.doi.org/10.1002/j.1939-4640.1992.tb03338.x.

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Abstract: These experiments were carried out to establish and validate an in vitro system for studying macaque sperm—zona pellucida interaction. Sperm of rhesus and cynomolgus macaques were capacitated in vitro and incubated with cryopreserved zonae pellucidae. Homologous gamete incubations were tested, as well as cross‐species combinations. Approximately 25% of macaque sperm bound to the zonae acrosome reacted within 1 minute of gamete coincubation, although the percentage of acrosome reactions in the sperm suspension was less than 1%. There was a small but consistent increase in the percent

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Ganeva, Rumiana, Dimitar Parvanov, Denitsa Velikova, Magdalena Vasileva, Kristina Nikolova, and Georgi Stamenov. "Sperm morphology and DNA fragmentation after zona pellucida selection." Reproduction and Fertility 2, no. 3 (2021): 221–30. http://dx.doi.org/10.1530/raf-21-0041.

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Sperm DNA fragmentation (SDF) and sperm morphological defects can negatively affect ART outcomes. Consequently, there is a need for additional semen processing technique that accounts for sperm DNA status and morphology prior to ICSI. The objective was to evaluate the efficacy of an additional zona pellucida adhesion-based sperm selection for obtaining sperm populations with a high percentage of normal morphology and DNA integrity as compared to native semen and routine swim-up preparation. Semen samples from 78 normozoospermic men were subjected to swim up and placed in petri dishes coated wi

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Kan, F. W., S. St-Jacques, and G. Bleau. "Immunoelectron microscopic localization of an oviductal antigen in hamster zona pellucida by use of a monoclonal antibody." Journal of Histochemistry & Cytochemistry 36, no. 11 (1988): 1441–47. http://dx.doi.org/10.1177/36.11.3171167.

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The zona pellucida is an extracellular matrix of glycoproteins which surrounds the mammalian oocyte and preimplantation embryo. We have recently developed monoclonal antibodies against oviductal zona pellucida of the golden hamster. We applied the post-embedding immunocytochemical method using a monoclonal antibody (IgGl,k) to determine the precise location of antigenic sites in the cumulus oophorus complex of the superovulated hamster. By applying the high-resolution protein A-gold technique, we demonstrated that the sites of immunoreactivity were exclusively in the zona pellucida encompassin

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Schnakenberg, Uwe, and Yuan Cao. "Elektrische Charakterisierung von Eizellen mit mikrofluidischen Systemen." BIOspektrum 30, no. 2 (2024): 186–88. http://dx.doi.org/10.1007/s12268-024-2134-9.

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AbstractIn in vitro fertilization, the status of the zona pellucida is of pivotal interest to determine the window of best fertilization. In this window, the zona pellucida becomes soft, so that a sperm can penetrate. Two lab-on-chip systems will be introduced which were developed to monitor the status of the zona pellucida of mouse oocytes with electrical impedance spectroscopy. The combination of microfluidic systems and impedance spectroscopy offer advantages of easy cell handling and observer-independent characterization.

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Urch, U. A., and H. Patel. "The interaction of boar sperm proacrosin with its natural substrate, the zona pellucida, and with polysulfated polysaccharides." Development 111, no. 4 (1991): 1165–72. http://dx.doi.org/10.1242/dev.111.4.1165.

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Boar sperm acrosin is an acrosomal protease with trypsin-like specificity, and it functions in fertilization by assisting sperm passage through the zona pellucida by limited hydrolysis of this extracellular matrix. In addition to a proteolytic active site domain, acrosin binds the zona pellucida at a separate binding domain that is lost during proacrosin autolysis. In this study, we quantitate the binding of proacrosin to the physiological substrate for acrosin, the zona pellucida, and to a non-substrate, the polysulfated polysaccharide fucoidan. Binding was analogous to sea urchin sperm bindi

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Stringfellow, D. A., L. H. Lauerman, and M. S. Thomson. "Trypsin treatment of bovine ova after in vitro exposure to vesicular stomatitis virus." American Journal of Veterinary Research 50, no. 6 (1989): 990–92. https://doi.org/10.2460/ajvr.1989.50.06.990.

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SUMMARY Preimplantation bovine ova were exposed in vitro to vesicular stomatitis virus, Indiana serotype, to document adherence of the virus to the zona pellucida. To determine the efficacy of this treatment, some of the ova were treated with trypsin after exposure to the virus. Vesicular stomatitis virus was isolated from 5 of 10 groups of zona pellucida-intact ova after 12 sequential washes without trypsin treatment. Vesicular stomatitis virus was also isolated from 4 of 11 groups of zona pellucida-intact ova after trypsin treatment.

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Dun, M. D., R. Aitken, and B. Nixon. "178. THE CHAPERONIN CONTAINING TCP-1 (CCT/TRiC) MULTISUBUNIT COMPLEX IS INVOLVED IN MEDIATING SPERM - OOCYTE INTERACTIONS." Reproduction, Fertility and Development 22, no. 9 (2010): 96. http://dx.doi.org/10.1071/srb10abs178.

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Mammalian spermatozoa only express their capacity for fertilization following capacitation, a process characterized by a suite of biophysical and biochemical changes that occurs as the cells ascend the female reproductive tract. A key event associated with the attainment of a capacitated state is a dramatic reorganization of the sperm surface architecture to render these cells competent to bind to the protective matrix of the oocyte, the zona pellucida. Our previous analysis of these remodeling events has provided compelling evidence that they include the assembly and/or presentation of multim

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Paterson, Margaret, Zoë A. Jennings, Marcel van Duin, and R. John Aitken. "Immunocontraception with Zona pellucida Proteins." Cells Tissues Organs 166, no. 2 (2000): 228–32. http://dx.doi.org/10.1159/000016735.

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Schmitz, Carlo, Seyedeh Zeynab Sadr, Hagen Körschgen, et al. "The E-modulus of the oocyte is a non-destructive measure of zona pellucida hardening." Reproduction 162, no. 4 (2021): 259–66. http://dx.doi.org/10.1530/rep-21-0122.

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After fertilization, the oocyte-specific metalloproteinase ovastacin is released and cleaves the zona pellucida protein 2 (ZP2), making the zona pellucida impermeable to sperm. Before fertilization, the zona remains permeable because previously released ovastacin is inhibited by fetuin-B. Consequently, in the absence of fetuin-B, ZP2 cleavage occurs prematurely and leads to infertility of female fetuin-B deficient mice. In contrast, fetuin-B/ovastacin double-deficient oocytes show a permanently permeable zona with intact ZP2. In this study, we asked if the elastic modulus of the zona pellucida

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Brown, C. R., and R. Jones. "Binding of zona pellucida proteins to a boar sperm polypeptide of Mr 53,000 and identification of zona moieties involved." Development 99, no. 3 (1987): 333–39. http://dx.doi.org/10.1242/dev.99.3.333.

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Experiments have been carried out to identify proteins on boar spermatozoa that bind to components of the zona pellucida. Polypeptides in sodium deoxycholate extracts of boar spermatozoa and in whole seminal plasma have been separated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, transferred onto nitrocellulose sheet by electroblotting and probed with 125I-labelled heat-solubilized zona pellucida from pig oocytes or ovulated eggs. Zona proteins bound avidly and consistently to a polypeptide of Mr 53,000 on blots of capacitated and noncapacitated sperm and weakly to polypeptide

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Ueno, S., M. Kurome, R. Tomii, et al. "185 EMBRYONIC LOSS IN PIGS ASSOCIATED WITH OVIDUCT TRANSPLANTATION OF EARLY-STAGE EMBRYOS WITH DAMAGES IN THE ZONA PELLUCIDA." Reproduction, Fertility and Development 18, no. 2 (2006): 200. http://dx.doi.org/10.1071/rdv18n2ab185.

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It is assumed that if porcine early-stage embryos with damages in their zonae pellucidae are transplanted to the recipient's oviduct, they may suffer from mechanical and immunological stresses by oviduct contraction and the recipient's immune response. This study aimed to examine the impact of zona pellucida damages, which might arise during nuclear transfer and intra cytoplasmic sperm injection (ICSI), on the development and survival of transplanted embryos. Cumulus-oocyte complexes were collected from ovaries obtained at a local slaughterhouse and matured in vitro in NCSU23 to prepare MII-st

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Mustofa, Imam. "Immunocontraceptive Potential of Goat Zona pellucida as Monkey Population Control." International Journal of Zoology and Animal Biology 6, no. 2 (2023): 1–9. http://dx.doi.org/10.23880/izab-16000459.

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A series of studies have explored the immunocontraceptive potential of zona pellucida-3 in local Indonesian goats. Goat zona pellucida-3 (gZP3) proteins have been identified and isolated. It has 82 kDa molecular weight and comprises 63.47% of the total goat zona pellucida protein. Immunofluorescence staining showed that gZP3 protein recognized goat sperm plasma membrane, whereas gZP3 antibodies recognized goat zona pellucida in native smear. In vitro fertilization study showed that gZP3 protein-supplemented in sperm capacitation medium and gZP3 antibody supplemented in oocyte maturation medium

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Epifano, O., and J. Dean. "Biology and structure of the zona pellucida: a target for immunocontraception." Reproduction, Fertility and Development 6, no. 3 (1994): 319. http://dx.doi.org/10.1071/rd9940319.

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Although reversible interference of sperm-egg interactions with pharmacological agents has not yet been achieved, animal models have provided increasing evidence that immunological reagents directed against mammalian gametes can effectively inhibit fertilization. One potential target of immunocontraception is the zona pellucida, an extracellular matrix that surrounds the growing oocyte and ovulated egg. Recent advances in our knowledge of the biosynthesis and molecular biology of the zona pellucida have provided much information useful in the rational design of immunocontraceptive vaccines. Th

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Zhao, Longmei, Kerstin Reim, and David J. Miller. "Complexin-I-deficient sperm are subfertile due to a defect in zona pellucida penetration." REPRODUCTION 136, no. 3 (2008): 323–34. http://dx.doi.org/10.1530/rep-07-0569.

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Upon adhesion to the zona pellucida, sperm undergo regulated exocytosis of the acrosome. Although it is necessary for sperm to penetrate the zona pellucida and fertilize an egg, the acrosomal membrane fusion process is poorly understood. Complexins I and II are small, cytosolic proteins that bind to a complex of proteins termed the solubleN-ethylmaleimide-sensitive factor attachment protein receptor complex to regulate synaptic vesicle exocytosis. Complexin-II-deficient mice are fertile but the fertility of sperm from complexin-I-deficient male mice is unclear because the mice have ataxia and

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Azarkh, Danyil, Yuan Cao, Julia Floehr, and Uwe Schnakenberg. "Viscoelastic Properties of Zona Pellucida of Oocytes Characterized by Transient Electrical Impedance Spectroscopy." Biosensors 13, no. 4 (2023): 442. http://dx.doi.org/10.3390/bios13040442.

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The success rate in vitro fertilization is significantly linked to the quality of the oocytes. The oocyte’s membrane is encapsulated by a shell of gelatinous extracellular matrix, called zona pellucida, which undergoes dynamic changes throughout the reproduction cycle. During the window of highest fertility, the zona pellucida exhibits a softening phase, while it remains rigid during oocyte maturation and again after fertilization. These variations in mechanical properties facilitate or inhibit sperm penetration. Since successful fertilization considerably depends on the state of the zona pell

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Gu, Yi-Fan, Chang-Fu Lu, Ge Lin, and Guang-Xiu Lu. "A comparative analysis of the zona pellucida birefringence of fresh and frozen–thawed human embryos." REPRODUCTION 139, no. 1 (2010): 121–27. http://dx.doi.org/10.1530/rep-09-0227.

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The cryopreservation of human embryos is thought to induce alteration in the glycoprotein matrix and lead to zona change. However, this assumption has been full of controversies till now. The objective of this study was to evaluate the effect of cryopreservation on zona pellucida of human embryos. Fresh (n=106, from 40 patients) and frozen–thawed embryos (n=123, from 40 patients) were obtained from consenting patients who received conventional IVF and ICSI treatment. The birefringence of zona pellucida in human fresh and frozen–thawed embryos was imaged and quantitatively analyzed using polari

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Hino, Toshiaki, Kanako Oda, Kenji Nakamura, Hiroyuki Tateno, Yutaka Toyoda, and Minesuke Yokoyama. "Accelerated modification of the zona pellucida is the primary cause of decreased fertilizability of oocytes in the 129 inbred mouse strain." Zygote 19, no. 4 (2010): 315–22. http://dx.doi.org/10.1017/s0967199410000481.

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SummaryWe investigated whether the small litter size in the 129 inbred mouse strain results from a reduction in oocyte fertilizability. Sensitivity of the zona pellucida to α-chymotrypsin was examined for oocytes collected at 14 h (shortly after ovulation), 17 h, and 20 h after hCG injection. Passage of spermatozoa through the zona pellucida (using an in vitro fertilization (IVF) technique) and the density of cortical granules were examined for oocytes collected at 14 and 17 h after hCG injection. The capability of the oolemma to fuse with the sperm plasma membrane was also evaluated by IVF us

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Redgrove, K. A., E. A. McLaughlin, M. K. O'Bryan, R. J. Aitken, and B. Nixon. "168. IDENTIFICATION AND CHARACTERISATION OF SURFACE PROTEIN COMPLEXES IN HUMAN SPERMATOZOA." Reproduction, Fertility and Development 21, no. 9 (2009): 86. http://dx.doi.org/10.1071/srb09abs168.

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Upon leaving the testis mammalian spermatozoa are functionally incompetent and are thus unable to fertilize an oocyte. As the spermatozoa ascend the female reproductive tract, functional maturity is achieved through a complex cascade of biophysical and biochemical changes known as capacitation. An important aspect of this final maturation phase is the remodelling of the sperm surface architecture to enable it to interact with the zona pellucida, a glycoprotein matrix that surrounds the oocyte, and initiate fertilisation. While originally thought to be underpinned by a simple lock and key mecha

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Yurchuk, Taisiia A., Maryna P. Petrushko, Volodymyr I. Piniaiev, and Natalya A. Buderatska. "Vitrification of Human Embryos After Manipulation with Zona Pellucida." Problems of Cryobiology and Cryomedicine 28, no. 2 (2018): 184. http://dx.doi.org/10.15407/cryo28.02.184.

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Rankin, T., P. Talbot, E. Lee, and J. Dean. "Abnormal zonae pellucidae in mice lacking ZP1 result in early embryonic loss." Development 126, no. 17 (1999): 3847–55. http://dx.doi.org/10.1242/dev.126.17.3847.

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All vertebrates have an egg shell that surrounds ovulated eggs and plays critical roles in gamete recognition. This extracellular matrix is known as the zona pellucida in eutherian mammals and consists of three glycoproteins, ZP1, ZP2 and ZP3 in the mouse. To investigate the role of ZP1 in fertilization and early development, we have used targeted mutagenesis in embryonic stem cells to create mouse lines (Zp1(tm/tm)) lacking ZP1. Although a zona pellucida composed of ZP2 and ZP3 was formed around growing Zp1(tm/tm) oocytes, the matrix was more loosely organized than zonae around normal oocytes

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Redgrove, K. A., B. Nixon, E. A. McLaughlin, M. K. O'Bryan, and R. J. Aitken. "119. IDENTIFICATION AND CHARACTERISATION OF SURFACE PROTEIN COMPLEXES IN HUMAN SPERMATOZOA." Reproduction, Fertility and Development 22, no. 9 (2010): 37. http://dx.doi.org/10.1071/srb10abs119.

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A unique characteristic of mammalian spermatozoa is that upon ejaculation, they are unable to recognise and bind to an ovulated oocyte. These functional attributes are only realised following the sperms ascent of the female reproductive tract whereupon they undergo a myriad of biochemical and biophysical changes collectively referred to as ‘capacitation’. Since spermatozoa are both transcriptionally and translationally quiescent cells, this functional transformation must be engineered by a combination of post-translational modification and spatial reorganisation of existing sperm proteins. Ind

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Dun, M. D., B. Nixon, and R. J. Aitken. "150. THE CAPACITATION INDUCED FORMATION OF A MULTIMERIC SPERM - ZONA PELLUCIDA RECEPTOR COMPLEX." Reproduction, Fertility and Development 21, no. 9 (2009): 68. http://dx.doi.org/10.1071/srb09abs150.

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The ability of mammalian spermatozoa to fertilize the oocyte is dependent on a complex cascade of biophysical and biochemical changes collectively known as capacitation. This final phase of sperm maturation is characterised by a dramatic remodelling of the sperm surface architecture to render the cell competent to recognise and bind to the zona pellucida. Although the current paradigm suggests this interaction is mediated by a single receptor-ligand interaction, recent evidence emerging from our laboratory suggests that this event is more complex and involves the capacitation-dependent formati

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Lai, AC, JP Ryan, and DM Saunders. "Removal of the zona pellucida and parthenogenetic activation affect rates of survival of ultrarapidly frozen mouse oocytes." Reproduction, Fertility and Development 6, no. 6 (1994): 771. http://dx.doi.org/10.1071/rd9940771.

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Survival rates on thawing were assessed for ultrarapidly frozen mouse oocytes following the removal of zonae pellucidae using an acid Tyrode's solution, pronase or a mechanical dissection technique. Significantly higher rates of survival were observed for zona-free oocytes than for zona-intact control oocytes (303/684, 44% v. 130/498, 26%; P < 0.001). The rates of survival observed for pronuclear stage embryos (72-76%) were much greater than those observed for oocytes and were not influenced by zona removal techniques. Parthenogenetic activation of oocytes by exposure to a 7% (v/v) ethanol

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Rankin, T. L., M. O'Brien, E. Lee, K. Wigglesworth, J. Eppig, and J. Dean. "Defective zonae pellucidae in Zp2-null mice disrupt folliculogenesis, fertility and development." Development 128, no. 7 (2001): 1119–26. http://dx.doi.org/10.1242/dev.128.7.1119.

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All vertebrate eggs are surrounded by an extracellular matrix. This matrix is known as the zona pellucida in mammals and is critically important for the survival of growing oocytes, successful fertilization and the passage of early embryos through the oviduct. The mouse zona pellucida is composed of three glycoproteins (ZP1, ZP2 and ZP3), each encoded by a single copy gene. Using targeted mutagenesis in embryonic stem cells, Zp2-null mouse lines have been established. ZP1 and ZP3 proteins continue to be synthesized and form a thin zona matrix in early follicles that is not sustained in pre-ovu

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