Zona pellucida binding

Figure 3. A Model for Acrosin s Role in Zona Pellucida Binding and Penetration of Sperm. The model uses the m -acrosin form depicted in Figure 2. Acrosin is bound to the sperm plasma membrane (PM) via its hydrophobic domain and interacts with the egg zona pellucida (ZP) via its protease and carbohydrate binding domains. The ZP is composed of three glycoproteins which have unique polypeptide chains and both shared and unique oligosaccharide moieties. Symbols used - oligosaccharide...

K. Ozgur, M. S. Patankar, S. Oehninger, and G. F. Clark, Direct evidence for the involvement of carbohydrate sequences in human sperm-zona pellucida binding. Molecular Human Reproduction, 4 (1998) 318-324. 

Millar, S. E., Lader, E., Liang, L-F., and Dean, J. (1991). Oocyte-specific factors bind a conserved upstream sequence required for mouse zona pellucida promoter activity. Mol. Cell. Biol. 11 6197-6204. 

Fertilization is the fusion of the sperm and ovum. The sperm head binds to the plasma membrane of the egg (oolemma), and the entire spermatozoon enters the cytoplasm of the ovum. Only capacitated spermatozoa with intact acrosomes can enter and pass through the cumulus oophorus. The acrosome is a membrane-bound, cap-like structure covering the anterior portion of the sperm nucleus. The acrosomal reaction is the release of materials that lyse the glycoprotein coat (zona pellucida) surrounding the ovum. This is necessary for fertilization to take place. Before undergoing the acrosomal reaction, sperm go through a type of hypermotility called hyperactivation. The... 

The acrosome reaction is the loss of the acrosomal and plasma membranes in the acrosome region and the release of acrosin, hyaluronidase and other enzymes that disperse the cumulus complex and allow the sperm to penetrate the zona pellucida. After capacitation and the acrosome reaction, sperm penetrate the extracellular cumulus matrix and bind with zona protein 3, a heavily glycosylated protein of the zona pellucida. The first segment of the sperm to make contact with the oolemma is usually the inner acrosomal membrane, followed by the postacrosomal region. The plasma membrane of the sperm attaches to microvilli on the oolemma. Sperm-egg fusion is apparent from reduced movement of the sperm tail (Yanagimachi, 1970,1988 Takano et al.,... 

N-glycans or SA had no effect [138]. A Gal residue at the nonreducing terminus of these O-glycans is essential for binding of sperm to the zona pellucida. 

Heffner, L.J. and Storey, B.T. (1982). Cold lability of sperm binding to zona pellucida. J. Exp. Zool. 279 155-161. 

Inoue, M. and Wolf, D.P. (1975). Sperm binding characteristics of the murine zona pellucida. Biol. Reprod. 73 340-348. 

Saling, P.M., Storey, B.T., and Wolf, D.P. (1978). Calcium-dependent binding of mouse epididymal spermatozoa to the zona pellucida. Dev. Biol. 65 515-525. 

Primakoff, P., Hyatt, H., and Myles, D.G. (1985). A role for the migrating sperm surface antigen PH-20 in guinea pig sperm binding to the egg zona pellucida. J. Cell Biol. 707 2239-2244. 

Endo, Y., Lee, M.A., and Kopf, G.S. (1987). Evidence for a role of a guanine nucleotide-binding regulatory protein in the zona pellucida-induced mouse sperm acrosome reaction. Dev. Biol. 7 79 210-216. 

McLaughlin, J.D. and Shur, B.D. (1987). Binding of caput epididymal mouse sperm to the zona pellucida. Dev, Biol. 724 557-561. 

In Chapter 7, Florman and coauthors review the mechanisms of egg-regulated acrosome reactions of mammalian sperm. Among the aspects discussed are the nature of primary signal transducers and targets stimulated by binding of acrosome-intact sperm to receptors in the egg zona pellucida. In a detailed presentation, the potential roles of several sperm components including G proteins, cation channels, tyrosine kinases, calcium, and cellular pH are considered. 

AM356 [1.0 nM Inhibits Tight Binding of Sperm to Human Zona Pellucida in the Hemizona Assay... 

Burkman LJ, Coddington CC, Franken DR, Oehninger SC, Hodgen GD. 1990. The hemizona assay (HZA) assessment of fertilizing potential by means of human sperm binding to the human zona pellucida. in Keel BA and Webster B, Eds. Laboratory Diagnosis and Treatment of Infertility. Boca Raton, FL CRC Press, pp. 213-228. 

Franken DR, Burkman LJ, Oehninger SC, Coddington CC, Veeck LL, Kruger TF, Rosenwaks Z, Hodgen GD. 1989. Hemizona assay using salt-stored human oocytes evaluation of zona pellucida capacity for binding human spermatozoa. Gamete Res 22 15-26. 

Results obtained" from the reaction of periodate with oligosaccharide structures in erythropoietin are consistent with the proposal that antibodies directed against the recombinant hormone are anti-carbohydrate . That oligosaccharide sequences are involved in the binding of human spermatozoa to a glycoprotein of the zona pellucida, is indicated " " by a marked decrease in binding that accompanies selective periodate oxidation of terminal sialic acid residues of the glycoprotein. 

Neiz RK, Ahmad K. 1994. Molecular identities of human sperm proteins that bind human zona pellucida nature of sperm-zona interaction, tyrosine kinase activity, and involvement of FA-1. Mol Reprod Dev 39(4) 397-408. 

G.F., Yeung, W.S.B. et al. (2011) Human sperm binding is mediated by the Sialyl-Lewis(x) oligosaccharide on the zona pellucida. Science, 333, 1761-1764. 

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