Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding.
Philip C.N. Chiu,MK Chung,Riitta Koistinen,Hannu Koistinen,Markku Seppälä,Pak Chung Ho,Ernest Hung Yu Ng,Kai-Fai Lee,William S.B. Yeung +8 more
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TLDR
Observations suggest that human sperm FUT5 is a receptor of glycodelin-A and zona pellucida proteins, and that glycodzin-A inhibits spermatozoa-zona binding by blocking the binding of sperm Fut5 to the zonapellucIDA.Abstract:
Fertilization depends on successful binding of the spermatozoa to the zona pellucida of the oocyte. Glycodelin-A inhibits spermatozoa-zona pellucida binding. Previous data showed that glycodelin-A receptor(s) and zona pellucida protein receptor(s) on human spermatozoa are closely related. Using a chemical cross-linking approach, the glycodelin-A-sperm receptor complex was isolated. The receptor was identified to be fucosyltransferase-5 (FUT5) by mass spectrometry and confirmed with the use of anti-FUT5 antibodies. Sperm FUT5 was an externally oriented integral membrane protein in the acrosomal region of human spermatozoa. Biologically active FUT5 was purified from spermatozoa. Co-immunoprecipitation confirmed the interaction between glycodelin-A and sperm FUT5. Solubilized zona pellucida reduced the binding of glycodelin-A to sperm FUT5. An anti-FUT5 antibody and FUT5 acceptor blocked the binding of glycodelin-A to spermatozoa and the zona binding inhibitory activity of glycodelin-A. Sperm FUT5 bound strongly to intact and solubilized human zona pellucida. The equilibrium dissociation constant of sperm FUT5 binding to solubilized zona pellucida was 42.82 pmol/ml. These observations suggest that human sperm FUT5 is a receptor of glycodelin-A and zona pellucida proteins, and that glycodelin-A inhibits spermatozoa-zona binding by blocking the binding of sperm FUT5 to the zona pellucida.read more
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Human sperm binding is mediated by the sialyl-Lewis(x) oligosaccharide on the zona pellucida.
Poh-Choo Pang,Philip C.N. Chiu,Cheuk-Lun Lee,Lan-Yi Chang,Maria Panico,Howard R. Morris,Stuart M. Haslam,Kay-Hooi Khoo,Gary F. Clark,William S.B. Yeung,Anne Dell +10 more
TL;DR: In this paper, the sialyl-Lewis(x) sequence [NeuAcα2-3Galβ1-4(Fucα1-3)GlcNAc], a well-known selectin ligand, is the most abundant terminal sequence on the N- and O-glycans of human ZP.
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Oviductal secretions: will they be key factors for the future ARTs?
TL;DR: The ZP changes produced in the oviduct result in an increased efficiency of the in vitro fertilization technique in some animal models, contributing in particular to the control of polyspermy and suggesting that a similar role could be played by ovidUCTal factors in human beings.
Atlas of Genetics and Cytogenetics in Oncology and Haematology
TL;DR: WWTR1 (also called TAZ in publications) is a WW domaing-containing transcriptional coactivator, which was first identified as a 14-3-3 binding protein that is involved in mesenchymal stem cell differentiation as well as tumorigenesis.
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Developmental sperm contributions: fertilization and beyond.
Gerardo Barroso,Carlos Valdespin,Eva Vega,Ruben Kershenovich,R. Avila,Conrado Avendaño,Sergio Oehninger +6 more
TL;DR: Clinical evidence from assisted reproduction suggests that failure to complete the fertilization process, syngamy, or early cleavage might be the result of an early paternal effect, and it is speculated that an abnormal release of a putative OAF and/or dysfunctions of the centrosome and cytoskeletal apparatus may mediate these effects.
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Sugar‐coated sperm: Unraveling the functions of the mammalian sperm glycocalyx
Eillen Tecle,Pascal Gagneux +1 more
TL;DR: The sperm glycocalyx mediates numerous functions in the female reproductive tract, including the following: inhibition of premature capacitation; passage through the cervical mucus; protection from innate and adaptive female immunity; formation of the sperm reservoir; and masking sperm proteins involved in fertilization.
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Mammalian Fertilization: Molecular Aspects of Gamete Adhesion, Exocytosis, and Fusion
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