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Journal articles on the topic 'Zona pellucida binding proteins (ZBP)'

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Published: 4 June 2021
Last updated: 1 February 2022

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1

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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2

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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3

Petit, F. M., C. Serres, F. Bourgeon, C. Pineau, and J. Auer. "Identification of sperm head proteins involved in zona pellucida binding." Human Reproduction 28, no. 4 (2013): 852–65. http://dx.doi.org/10.1093/humrep/des452.

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4

Blase, N., A. R. Fazeli, M. M. Bevers, B. Colenbrander, and E. Topfer-Petersen. "INHIBITION OF PORCINE SPERM BINDING TO HOMOLOGOUS ZONA PELLUCIDA USING HEMIZONA ASSAY and ANTIBODBES AGAINST ZONA PELLUCIDA PROTEINS." Reproduction in Domestic Animals 31, no. 1 (1995): 233–34. http://dx.doi.org/10.1111/j.1439-0531.1995.tb00030.x.

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5

Chirinos, Mayel, Cecilia Cariño, María Elena González-González, Ernesto Arreola, Rodrigo Reveles, and Fernando Larrea. "Characterization of Human Sperm Binding to Homologous Recombinant Zona Pellucida Proteins." Reproductive Sciences 18, no. 9 (2011): 876–85. http://dx.doi.org/10.1177/1933719111398146.

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6

Jones, R., and R. M. Williams. "Identification of zona- and fucoidan-binding proteins in guinea-pig spermatozoa and mechanism of recognition." Development 109, no. 1 (1990): 41–50. http://dx.doi.org/10.1242/dev.109.1.41.

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Binding of guinea-pig spermatozoa to the zona pellucida of homologous eggs has been reported to involve ‘receptors’ on the inner acrosomal membrane (Huang et al. 1981). These receptors can be blocked by sulphated polysaccharides such as fucoidan (Huang and Yanagimachi, 1984). The aims of the present investigation were to identify these putative zona receptors using 125I-fucoidan as a probe and examine their mechanism of recognition. Results show that 125I-fucoidan binds to several proteins extracted from guinea-pig spermatozoa with molecular masses of 95, 60, 48, 34, 30 and 18–20 × 10(3) (K) o
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7

Yauger, Belinda, Nathan A. Boggs, and Jurrien Dean. "Human ZP4 is not sufficient for taxon-specific sperm recognition of the zona pellucida in transgenic mice." REPRODUCTION 141, no. 3 (2011): 313–19. http://dx.doi.org/10.1530/rep-10-0241.

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The molecular basis of human fertilization remains enigmatic. Mouse models are often used to study sperm–egg recognition, but the mouse zona pellucida surrounding ovulated eggs contains three proteins (ZP1, ZP2, and ZP3) whereas the human zona contains four (ZP1, ZP2, ZP3, and ZP4). Human sperm are fastidious and recognize human but not mouse eggs. Transgenic mouse lines were established to ascertain whether human ZP4 is the sole determinant of human sperm binding. Human ZP4 expressed in transgenic mice had a molecular mass similar to the range of native protein isoforms and was incorporated i
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8

Lin, Yi-Nan, Angshumoy Roy, Wei Yan, Kathleen H. Burns, and Martin M. Matzuk. "Loss of Zona Pellucida Binding Proteins in the Acrosomal Matrix Disrupts Acrosome Biogenesis and Sperm Morphogenesis." Molecular and Cellular Biology 27, no. 19 (2007): 6794–805. http://dx.doi.org/10.1128/mcb.01029-07.

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ABSTRACT Zona pellucida binding protein 1 (ZPBP1), a spermatid and spermatozoon protein that localizes to the acrosome, was originally identified in pigs and named for its binding to the oocyte zona pellucida. In an in silico search for germ cell-specific genes, Zpbp1 and its novel paralog, Zpbp2, were discovered and confirmed to be expressed only in the testes in both mice and humans. To study the in vivo functions of both ZPBP proteins, we disrupted Zpbp1 and Zpbp2 in mice. Males lacking ZPBP1 were sterile, with abnormal round-headed sperm morphology and no forward sperm motility. Ultrastruc
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9

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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10

Moos, J., J. Pěknicová, Ts N. Sumeva-Nakova, and M. Pavlík. "Identification of 17-18 kDa zona pellucida binding proteins from boar spermatozoa." FEBS Letters 264, no. 2 (1990): 243–45. http://dx.doi.org/10.1016/0014-5793(90)80258-k.

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11

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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12

Walsh, A. K., K. L. Asquith, C. M. Thomas, L. A. Mitchell, B. Nixon, and R. J. Aitken. "214.Identification of potential zona pellucida-binding sperm proteins using heat shock protein 60." Reproduction, Fertility and Development 16, no. 9 (2004): 214. http://dx.doi.org/10.1071/srb04abs214.

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Sperm transit through the female tract is correlated with a number of biochemical and physical changes, termed capacitation, which culminate in acquisition of the ability to fertilise an egg. One of the important correlates of capacitation is an increase in tyrosine phosphorylation of multiple sperm proteins. Recent studies of the sperm surface proteome have demonstrated that, following capacitation, a number of tyrosine-phosphorylated proteins become expressed on the sperm surface. Analysing these proteins, we have identified at least three members of the chaperone family including heat shock
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13

Hanqing, Mo, Yan Tai-Ying, and Shen Zhao-Wen. "Isolation, characterization, and localization of the zona pellucida binding proteins of boar sperm." Molecular Reproduction and Development 28, no. 2 (1991): 124–30. http://dx.doi.org/10.1002/mrd.1080280204.

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14

Williams, R. M., and R. Jones. "Specificity of binding of zona pellucida glycoproteins to sperm proacrosin and related proteins." Journal of Experimental Zoology 266, no. 1 (1993): 65–73. http://dx.doi.org/10.1002/jez.1402660110.

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15

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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16

Moreno, R. D., M. Hoshi, and C. Barros. "Functional interactions between sulphated polysaccharides and proacrosin: implications in sperm binding and digestion of zona pellucida." Zygote 7, no. 2 (1999): 105–11. http://dx.doi.org/10.1017/s0967199499000453.

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Acrosin is a serine protease located within mammalian acrosome as inactive proacrosin. Sulphated polymers bind to proacrosin and acrosin, to a domain different from the active site. Upon binding, these polymers induce proacrosin activation and some of them, such as fucoidan, inhibit sperm binding to the zona pellucida. In this work we have studied the interaction of solubilised zona pellucida glycoproteins (ZPGs), heparin and ARIS (Acrosome Reaction Inducing Substance of Starfish) with boar and human acrosin. We have found that ARIS, solubilised ZPGs and fucoidan, but not heparin, inhibit the
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17

Björkgren, Ida, and Petra Sipilä. "The impact of epididymal proteins on sperm function." Reproduction 158, no. 5 (2019): R155—R167. http://dx.doi.org/10.1530/rep-18-0589.

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The epididymis is necessary for post-testicular sperm maturation as it provides the milieu required for spermatozoa to gain the ability for progressive movement and fertilization. In the epididymis the sperm protein, lipid and small RNA content are heavily modified due to interaction with luminal proteins secreted by the epididymal epithelium and extracellular vesicles, epididymosomes. This review focuses on epididymal proteins demonstrated to have an effect on sperm functions, such as motility, capacitation, acrosome reaction, sperm-zona pellucida binding and sperm-egg binding, as well as on
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18

Parry, R. V., P. J. Barker, and R. Jones. "Characterization of low Mr Zona Pellucida binding proteins from boar spermatozoa and seminal plasma." Molecular Reproduction and Development 33, no. 1 (1992): 108–15. http://dx.doi.org/10.1002/mrd.1080330115.

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19

Howes, Elizabeth, John C. Pascall, Wolfgang Engel, and Roy Jones. "Interactions between mouse ZP2 glycoprotein and proacrosin; a mechanism for secondary binding of sperm to the zona pellucida during fertilization." Journal of Cell Science 114, no. 22 (2001): 4127–36. http://dx.doi.org/10.1242/jcs.114.22.4127.

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The mouse zona pellucida glycoprotein, mZP2, is thought to be the secondary receptor on eggs for retention of acrosome-reacted sperm during fertilization. Here, we present evidence that one of its complementary binding proteins on sperm is proacrosin/acrosin. mZP2 binds to proacrosin null sperm considerably less effectively than to wild-type sperm. Binding is mediated by a strong ionic interaction between polysulphate groups on mZP2 and basic residues on an internal proacrosin peptide. The stereochemistry of both sulphate groups and basic amino acids determines the specificity of binding. Stru
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20

Yamaguchi, Ryo, Yoshitaka Fujihara, Masahito Ikawa, and Masaru Okabe. "Mice expressing aberrant sperm-specific protein PMIS2 produce normal-looking but fertilization-incompetent spermatozoa." Molecular Biology of the Cell 23, no. 14 (2012): 2671–79. http://dx.doi.org/10.1091/mbc.e11-12-1025.

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Eight kinds of gene-disrupted mice (Clgn, Calr3, Pdilt, Tpst2, Ace, Adam1a, Adam2, and Adam3) show impaired sperm transition into the oviducts and defective sperm binding to the zona pellucida. All of these knockout strains are reported to lack or show aberrant expression of a disintegrin and metallopeptidase domain 3 (ADAM3) on the sperm membrane. We performed proteomic analyses of the proteins of these infertile spermatozoa to clarify whether the abnormal function is caused exclusively by a deficiency in ADAM3 expression. Two proteins, named PMIS1 and PMIS2, were missing in spermatozoa from
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21

Gibbs, Gerard M., Jennifer Chi Yi Lo, Brett Nixon, et al. "Glioma Pathogenesis-Related 1-Like 1 Is Testis Enriched, Dynamically Modified, and Redistributed during Male Germ Cell Maturation and Has a Potential Role in Sperm-Oocyte Binding." Endocrinology 151, no. 5 (2010): 2331–42. http://dx.doi.org/10.1210/en.2009-1255.

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The glioma pathogenesis-related 1 (GLIPR1) family consists of three genes [GLIPR1, GLIPR1-like 1 (GLIPR1L1), and GLIPR1-like 2 (GLIPR1L2)] and forms a distinct subgroup within the cysteine-rich secretory protein (CRISP), antigen 5, and pathogenesis-related 1 (CAP) superfamily. CAP superfamily proteins are found in phyla ranging from plants to humans and, based largely on expression and limited functional studies, are hypothesized to have roles in carcinogenesis, immunity, cell adhesion, and male fertility. Specifically data from a number of systems suggests that sequences within the C-terminal
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22

Rattanachaiyanont, Manee, Wattana Weerachatyanukul, Marie-Claude Léveillé, et al. "Anti-SLIP1-reactive proteins exist on human spermatozoa and are involved in zona pellucida binding." MHR: Basic science of reproductive medicine 7, no. 7 (2001): 633–40. http://dx.doi.org/10.1093/molehr/7.7.633.

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23

Hardy, D. M., and D. L. Garbers. "Species-specific binding of sperm proteins to the extracellular matrix (zona pellucida) of the egg." Journal of Biological Chemistry 269, no. 29 (1994): 19000–19004. http://dx.doi.org/10.1016/s0021-9258(17)32265-2.

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24

Shi, X., S. Amindari, K. Paruchuru, et al. "Cell surface beta-1,4-galactosyltransferase-I activates G protein-dependent exocytotic signaling." Development 128, no. 5 (2001): 645–54. http://dx.doi.org/10.1242/dev.128.5.645.

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ZP3 is a protein in the mammalian egg coat (zona pellucida) that binds sperm and stimulates acrosomal exocytosis, enabling sperm to penetrate the zona pellucida. The nature of the ZP3 receptor/s on sperm is a matter of considerable debate, but most evidence suggests that ZP3 binds to beta-1,4-galactosyltransferase-I (GalTase) on the sperm surface. It has been suggested that ZP3 induces the acrosome reaction by crosslinking GalTase, activating a heterotrimeric G protein. In this regard, acrosomal exocytosis is sensitive to pertussis toxin and the GalTase cytoplasmic domain can precipitate G(i)
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25

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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26

Malette, B., and G. Bleau. "Biochemical characterization of hamster oviductin as a sulphated zona pellucida-binding glycoprotein." Biochemical Journal 295, no. 2 (1993): 437–45. http://dx.doi.org/10.1042/bj2950437.

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Oviductins are a family of glycoproteins, synthesized and released by oviductal secretory cells, which bind to the zona pellucida of the oocyte after ovulation. Hamster oviductin migrates as diffuse species of 160-350 kDa during SDS/PAGE under reducing as well as non-reducing conditions. In this report, we describe the one-step purification of hamster oviductin using either immuno- or lectin-affinity chromatography. Probing with specific lectins showed that the glycoprotein contains terminal alpha-D-GalNAc, and either terminal alpha-D-NeuAc or non-terminal beta-D-(GlcNAc)2 residues, but fails
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27

Ponce, Ruben H., Umbert A. Urch, and Ryuzo Yanagimachi. "Inhibition of sperm-egg fusion in the hamster and mouse by carbohydrates." Zygote 2, no. 3 (1994): 253–62. http://dx.doi.org/10.1017/s0967199400002057.

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SummaryAfter spermatozoa bind to and penetrate the extracellular matrix of the egg, the zona pellucida, they adhere to and fuse with the plasma membrane of the egg. Since sperm–egg fusion may involve membrane glycoproteins and/or carbohydrate binding proteins, we sought to test this hypothesis by challenging sperm–egg fusion in hamster and in mouse with added carbohydrates. In this study, a number of carbohydrate and glycoconjugates were examined for their ability to inhibit sperm–eggfusion. In the hamster, D(+)-glucosamine, D(+)-galactosamine, albumin-bovine-glucosamide and-galactosamide, fuc
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28

Breitbart, Haim, Gili Cohen, and Sara Rubinstein. "Role of actin cytoskeleton in mammalian sperm capacitation and the acrosome reaction." Reproduction 129, no. 3 (2005): 263–68. http://dx.doi.org/10.1530/rep.1.00269.

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In order to fertilize, the mammalian spermatozoa should reside in the female reproductive tract for several hours, during which they undergo a series of biochemical modifications collectively called capacitation. Only capacitated sperm can undergo the acrosome reaction after binding to the egg zona pellucida, a process which enables sperm to penetrate into the egg and fertilize it. Polymerization of globular (G)-actin to filamentous (F)-actin occurs during capacitation, depending on protein kinase A activation, protein tyrosine phosphorylation, and phospholipase D activation. F-actin formation
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29

Lin, Yi-Nan, Angshumoy Roy, Wei Yan, Kathleen H. Burns, and Martin M. Matzuk. "Loss of Zona Pellucida Binding Proteins in the Acrosomal Matrix Disrupts Acrosome Biogenesis and Sperm Morphogenesis." Molecular and Cellular Biology 28, no. 7 (2008): 2495. http://dx.doi.org/10.1128/mcb.00198-08.

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30

Jonáková, Věra, and Marie Tichá. "Boar Seminal Plasma Proteins and Their Binding Properties. A Review." Collection of Czechoslovak Chemical Communications 69, no. 3 (2004): 461–75. http://dx.doi.org/10.1135/cccc20040461.

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Binding properties of a group of proteins isolated from boar seminal plasma and their role in the fertilization process are discussed. Boar seminal plasma contains different types of proteins: spermadhesins of AQN and AWN family, DQH and PSP proteins belong to the most abundant. Some of these proteins are bound to the sperm surface during ejaculation and thus protein-coating layers are formed. Sperms coated with proteins participate in different types of interactions in the following steps of the fertilization process: formation of oviductal sperm reservoir, sperm capacitation, oocyte recognit
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31

Rowlison, Tricia, Timothy P. Cleland, Mary Ann Ottinger, and Pierre Comizzoli. "Novel Proteomic Profiling of Epididymal Extracellular Vesicles in the Domestic Cat Reveals Proteins Related to Sequential Sperm Maturation with Differences Observed between Normospermic and Teratospermic Individuals." Molecular & Cellular Proteomics 19, no. 12 (2020): 2090–103. http://dx.doi.org/10.1074/mcp.ra120.002251.

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Extracellular vesicles (EVs) secreted by the epididymal epithelium transfer to spermatozoa key proteins that are essential in promoting motility and subsequent fertilization success. Using the domestic cat model, the objectives were to (1) characterize and compare protein content of EVs between segments of the epididymis, and (2) compare EV protein compositions between normo- and teratospermic individuals (producing >60% of abnormal spermatozoa). Epididymal EVs from adult cats were isolated and assessed via liquid chromatography tandem MS. Both male types shared 3008 proteins in total, with
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32

Lathrop, W. F., E. P. Carmichael, D. G. Myles, and P. Primakoff. "cDNA cloning reveals the molecular structure of a sperm surface protein, PH-20, involved in sperm-egg adhesion and the wide distribution of its gene among mammals." Journal of Cell Biology 111, no. 6 (1990): 2939–49. http://dx.doi.org/10.1083/jcb.111.6.2939.

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Sperm binding to the egg zona pellucida in mammals is a cell-cell adhesion process that is generally species specific. The guinea pig sperm protein PH-20 has a required function in sperm adhesion to the zona pellucida of guinea pig eggs. PH-20 is located on both the sperm plasma membrane and acrosomal membrane. We report here the isolation and sequence of a full-length cDNA for PH-20 (available from EMBL/GenBank/DDBJ under accession number X56332). The derived amino acid sequence shows a mature protein of 468 amino acids containing six N-linked glycosylation sites and twelve cysteines, eight o
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33

Coutinho da Silva, Marco A., George E. Seidel, Edward L. Squires, James K. Graham, and Elaine M. Carnevale. "Effects of milk proteins on sperm binding to the zona pellucida and intracellular Ca2+ concentration in stallion sperm." Animal Reproduction Science 150, no. 1-2 (2014): 24–29. http://dx.doi.org/10.1016/j.anireprosci.2014.08.010.

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34

Gahlay, Gagandeep Kaur, and Neha Rajput. "The enigmatic sperm proteins in mammalian fertilization: an overview†." Biology of Reproduction 103, no. 6 (2020): 1171–85. http://dx.doi.org/10.1093/biolre/ioaa140.

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Abstract Mammalian fertilization involves a physical interaction between a sperm and an egg followed by molecular interactions amongst their various cell surface molecules. These interactions are initially mediated on the egg’s outermost matrix, zona pellucida (ZP), and then its plasma membrane. To better understand this process, it is pertinent to find the corresponding molecules on sperm that interact with ZP or the egg’s plasma membrane. Although currently, we have some knowledge about the binding partners for egg’s plasma membrane on sperm, yet the ones involved in an interaction with ZP h
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35

Ye, Zhan, Weifeng Wang, Yaqun Zhang, Liping Wang, Yu Cui, and Hengde Li. "Integrative analysis reveals pathways associated with sex reversal in Cynoglossus semilaevis." PeerJ 8 (March 19, 2020): e8801. http://dx.doi.org/10.7717/peerj.8801.

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Sex reversal is a complex biological phenomenon exhibited by Cynoglossus semilaevis. Some genetic females may irreversibly convert to pseudomales, thus increasing aquaculture costs because males grow much more slowly than females. In this study, an integrative analysis of transcriptome and proteome was performed to compare differences in gene and protein expression in females and pseudomales after gonad differentiation in C. semilaevis. Based on RNA-Seq results, 1893 genes showed differences in expression at the transcript level between females and pseudomales. Of these differentially expresse
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36

Yonezawa, Naoto, Saeko Kanai-Kitayama, Tetsushi Kitayama, Ayumi Hamano, and Minoru Nakano. "Porcine zona pellucida glycoprotein ZP4 is responsible for the sperm-binding activity of the ZP3/ZP4 complex." Zygote 20, no. 4 (2011): 389–97. http://dx.doi.org/10.1017/s0967199411000608.

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SummaryThe zona pellucida (ZP) is a transparent envelope that surrounds the mammalian oocyte and mediates species-selective sperm–egg interactions. Porcine and bovine ZPs consist of glycoproteins ZP2, ZP3, and ZP4. In both pig and bovine a heterocomplex consisting of ZP3 and ZP4 binds to sperm, however it is not clarified whether ZP3 or ZP4 in the complex is responsible for the sperm binding. Previously, we have established a baculovirus-Sf9 cell expression system for porcine ZP glycoproteins. A mixture of recombinant ZP3 (rZP3) and rZP4 displayed sperm-binding activity toward bovine sperm but
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37

Breed, William G., Dina Idriss, Christopher M. Leigh, and Richard J. Oko. "Temporal deposition and spatial distribution of cytoskeletal proteins in the sperm head of an Australian rodent." Reproduction, Fertility and Development 21, no. 3 (2009): 428. http://dx.doi.org/10.1071/rd08187.

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The Australian murine rodent, the plains mouse (Pseudomys australis), possesses a highly complex sperm head, in which there are, in addition to an apical hook, two ventral processes that extend from its upper concave surface. The present study set out to determine the temporal deposition and distribution of the proteins within these structures during late spermiogenesis by light and electron microscopy using various antibodies to bull and laboratory rat sperm-head cytoskeletal proteins. The findings show that there are two phases of protein deposition. In the first phase, perinuclear theca pro
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Mortillo, S., and P. M. Wassarman. "Differential binding of gold-labeled zona pellucida glycoproteins mZP2 and mZP3 to mouse sperm membrane compartments." Development 113, no. 1 (1991): 141–49. http://dx.doi.org/10.1242/dev.113.1.141.

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Egg zona pellucida glycoproteins mZP3 and mZP2 serve as primary and secondary sperm receptors, respectively, during initial stages of fertilization in mice [Wassarman (1988) A. Rev. Biochem. 57, 415–442]. These receptors interact with complementary egg-binding proteins (EBPs) located on the sperm surface to support species-specific gamete adhesion. Results of whole-mount autoradiographic experiments suggest that purified egg mZP3 and mZP2 bind preferentially to acrosome-intact (AI) and acrosome-reacted (AR) sperm heads, respectively [Bleil and Wassarman (1986) J. Cell Biol. 102, 1363–1371]. He
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Duckworth, J. A., X. Cui, F. C. Molinia, W. Lubitz, and P. E. Cowan. "208.Zona pellucida vaccines for fertility control of brushtail possums in New Zealand." Reproduction, Fertility and Development 16, no. 9 (2004): 208. http://dx.doi.org/10.1071/srb04abs208.

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Introduced marsupial brushtail possums (Trichosurus vulpecula) are a major pest in New Zealand because of their impacts on conservation values and agricultural production. Immunologically-based fertility control (immunocontraception) offers an effective and humane alternative approach to possum management. The zona pellucida (ZP) is an extracellular coat around all mammalian eggs and an attractive target for the development of immunocontraceptive vaccines. Antibodies against ZP are ovary-specific and act by preventing sperm from binding and penetrating the ova and/or by disrupting the developm
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Torabi, F., O. A. Bogle, J. M. Estanyol, R. Oliva, and D. Miller. "Zona pellucida-binding protein 2 (ZPBP2) and several proteins containing BX7B motifs in human sperm may have hyaluronic acid binding or recognition properties." MHR: Basic science of reproductive medicine 23, no. 12 (2017): 803–16. http://dx.doi.org/10.1093/molehr/gax053.

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Takahashi, Kazuya, Kazuhiro Kikuchi, Yasuomi Uchida, et al. "Binding of Sperm to the Zona Pellucida Mediated by Sperm Carbohydrate-Binding Proteins is not Species-Specific in Vitro between Pigs and Cattle." Biomolecules 3, no. 4 (2013): 85–107. http://dx.doi.org/10.3390/biom3010085.

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Ringleb, Jennifer, Marlies Rohleder, and Katarina Jewgenow. "Impact of feline zona pellucida glycoprotein B-derived synthetic peptides on in vitro fertilization of cat oocytes." Reproduction 127, no. 2 (2004): 179–86. http://dx.doi.org/10.1530/rep.1.00076.

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Although immunocontraception based on porcine zona pellucida (ZP) proteins is widely applied in many species, it is not suitable for cat contraception due to the lack of cross-reactivity. Since the first ZP gene expressed during oocyte growth in domestic cats is ZPB, we assumed that immunization with feline ZPB (fZPB)-derived synthetic peptides may cause irreversible infertility, which would be preferable in stray cats. Thus, the present study evaluated the immunogenicity and the contraceptive potential of synthetic fZPB peptides. Antigenic epitope sequences were detected via epitope mapping u
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Gonçalves, RF, AL Staros, and GJ Killian. "Oviductal Fluid Proteins Associated with the Bovine Zona Pellucida and the Effect onIn VitroSperm-Egg Binding, Fertilization and Embryo Development." Reproduction in Domestic Animals 43, no. 6 (2008): 720–29. http://dx.doi.org/10.1111/j.1439-0531.2007.00978.x.

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Matas, C., and L. Lefievre. "261 SUPPLEMENTATION OF SHEEP OOCYTE MATURATION MEDIA WITH NITRIC OXIDE SYNTHASE INHIBITORS MODIFIES THE ZONA PELLUCIDA AND DECREASES SPERM ZONA BINDING." Reproduction, Fertility and Development 25, no. 1 (2013): 278. http://dx.doi.org/10.1071/rdv25n1ab261.

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Nitric oxide plays a critical role in several reproductive functions, including sperm and egg maturation. Nitric oxide has complex and sometimes antagonistic biological effects. At low and controlled levels, NO aids gamete maturation, but at high levels, it has detrimental effects and often causes cell death. Both the female tract and egg vestment contain endothelial NO synthase (eNOS) and inducible NOS (iNOS). The knockout mouse for specific NOS has been shown to impair egg maturation and ovulation. The aim of this work was to study the effect of NOS inhibitors on in vitro sheep oocyte matura
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Anderson, A. L., L. Mitchell, E. A. McLaughlin, M. K. O'Bryan, R. J. Aitken, and B. Nixon. "322. PROTEOMIC AND FUNCTIONAL ANALYSIS OF HUMAN SPERM DETERGENT RESISTANT MEMBRANES." Reproduction, Fertility and Development 22, no. 9 (2010): 122. http://dx.doi.org/10.1071/srb10abs322.

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Mammalian spermatozoa attain the ability to fertilize an oocyte as they negotiate the female reproductive tract. This acquisition of functional competence is preceded by an intricate cascade of biochemical and functional changes collectively known as ‘capacitation’. Among the universal correlates of the capacitation process is a remarkable remodeling of the lipid and protein architecture of the sperm plasma membrane. While the fundamental mechanisms that underpin this dynamic reorganization remain enigmatic, emerging evidence has raised the prospect that it may be coordinated, at least in part
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Coutinho da Silva, Marco A., George E. Seidel, Edward L. Squires, James K. Graham, and Elaine M. Carnevale. "Effects of components of semen extenders on the binding of stallion spermatozoa to bovine or equine zonae pellucidae." REPRODUCTION 143, no. 5 (2012): 577–85. http://dx.doi.org/10.1530/rep-11-0099.

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The effects of semen extender components on the ability of stallion sperm to bind to the zona pellucida (ZP) and the suitability of using bovine ZP for a ZP-binding assay for stallion sperm were investigated in a series of experiments. In Experiment I, binding of stallion sperm to both bovine and equine ZP was significantly increased when a skim milk-based extender (EZM) was used. In Experiment II, a threefold increase in sperm binding to ZP was observed when sperm were diluted in EZM compared with diluents, which contained no milk (TALP, LAC, and EmCare). In Experiment III, centrifuging the s
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Harkema, W., B. Colenbrander, B. Engel, and H. Woelders. "Effects of exposure of epididymal boar spermatozoa to seminal plasma on the binding of zona pellucida proteins during in vitro capacitation." Theriogenology 61, no. 2-3 (2004): 215–26. http://dx.doi.org/10.1016/s0093-691x(03)00223-1.

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Swegen, A., N. D. Smith, Z. Gibb, B. J. Curry, and R. J. Aitken. "The serine protease testisin is present on the surface of capacitated stallion spermatozoa and interacts with key zona pellucida binding proteins." Andrology 7, no. 2 (2018): 199–212. http://dx.doi.org/10.1111/andr.12569.

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Evans, J. P., R. M. Schultz, and G. S. Kopf. "Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) beta." Journal of Cell Science 108, no. 10 (1995): 3267–78. http://dx.doi.org/10.1242/jcs.108.10.3267.

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The guinea pig sperm protein, PH-30 (also known as fertilin), is postulated to participate in the interaction between the sperm and egg plasma membranes. The beta subunit of guinea pig PH-30 (gpPH-30 beta) contains a domain with homology to disintegrins, snake venom proteins that bind to integrins via an integrin-binding domain containing the tripeptide RGD. This raises the question of whether an egg integrin serves as a receptor for PH-30. Although mouse eggs express integrin subunits, their role in mouse fertilization is unresolved. Therefore, we examined fertilization for two different hall
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Flesch, F. M., E. Wijnand, C. H. A. van de Lest, B. Colenbrander, L. M. G. van Golde, and B. M. Gadella. "Capacitation dependent activation of tyrosine phosphorylation generates two sperm head plasma membrane proteins with high primary binding affinity for the zona pellucida." Molecular Reproduction and Development 60, no. 1 (2001): 107–15. http://dx.doi.org/10.1002/mrd.1067.

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