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Relevant bibliographies by topics / Zona pellucida binding proteins (ZBP)

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Academic literature on the topic 'Zona pellucida binding proteins (ZBP)'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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

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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Dissertations / Theses on the topic "Zona pellucida binding proteins (ZBP)"

1

Bull, Leonard. "Characterization of the 95 kDa sperm adhesion protein." Doctoral thesis, 2004. http://hdl.handle.net/11858/00-1735-0000-0006-B63B-0.

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2

Zigo, Michal. "Izolace a studium proteinů se zona pellucida vazebnou aktivitou." Doctoral thesis, 2014. http://www.nusl.cz/ntk/nusl-342676.

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Binding of sperm to the oocyte is mediated by complementary molecules on the surface of both gametes and involves the interaction of sperm protein receptors with the zona pellucida (ZP) saccharide structures. It has been shown that many proteins receptors are involved in the sperm-ZP interaction, and potential primary sperm receptors for ZP glycoproteins have been investigated in various mammals. The majority of proteins with identified sperm-ZP binding activity belong to the plasma membrane proteins. However, the exact methods for isolation of sperm membrane proteins are still to be standardi

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3

Pohlová, Alžběta. "Studium proteinů spermií různých savčích druhů." Master's thesis, 2016. http://www.nusl.cz/ntk/nusl-344113.

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Reproduction is an essential feature of all animals and a fundamental step to produce new generations. Study of sperm proteins is crucial for understanding of the sperm-egg recognition. We searched out sperm surface proteins involving in the zona pellucida (ZP) binding and studied whether these proteins are preserved throughout mammalian species. Indirect immunofluorescent technique was used to test a panel of monoclonal antibodies prepared against boar sperm surface proteins on spermatozoa of bull and mice. We found a cross-reactivity of some antibodies against boar sperm with bull ejaculated

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