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Sperm binding

While acrosin has been localized to the acrosome, there are conflicting reports as to exactly where in the acrosomal compartment acrosin is localized before the acrosome reaction and the timing of its release in the fertilization process. From the description of acrosin as a ZP binding lectin, acrosin must be available to bind the ZP, and this would place the molecule on the surface of the intact sperm, or in some species, of the aerosome-reacted sperm. In the mouse, only acrosome intact sperm bind the ZP (66). Once the sperm has undergone the acrosome reaction and the outer membranes (limiting... [Pg.218]

Figure 4. Scheme showing sperm-egg interaction in the abalone. 1. The sperm binds to the egg VE by the plasma membrane at the tip of the AV (AG), (F, flagellum M, mitochondrion N, nucleus). 2. The sperm acrosome reacts releasing lysin and the 18K protein from its anterior tip. 3. Lysin disrupts the fibers of the VE and the 18K coats the extending acrosome process as it extends. 4. The sperm passes through the hole in the VE and the membrane covering the tip of the acrosomal process fuses with the egg (from Vacquier and Lee, 1993). [Pg.55]

Heffner, L.J. and Storey, B.T. (1982). Cold lability of sperm binding to zona pellucida. J. Exp. Zool. 279 155-161. [Pg.104]

Inoue, M. and Wolf, D.P. (1975). Sperm binding characteristics of the murine zona pellucida. Biol. Reprod. 73 340-348. [Pg.105]

Wolf, D.P. and Inoue, M. (1976). Sperm concentration dependency in the fertilization and zona sperm binding properties of mouse eggs inseminated in vitro. J. Exp. Zool. 790 27-38. [Pg.107]

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. [Pg.196]

Johnston, D.S., Wright, W.W., Shaper, J.H., Hokke, C.H., van den Eijnden, D.H., and Joziasse, D.H. (1998). Murine sperm-zona binding, a fucosyl residue is required for a high affinity sperm-binding ligand. A second site on sperm binds a nonfucosylated, P galactosyl-capped oligosaeeharide. J. Biol. Chem. 275 1888-1895. [Pg.227]

Until now, no experimental results support the hypothesis of a carbohydrate-mediated species-speeifie sperm binding for amphibians, similar to that demonstrated for mammalians. Further studies will probably indicate if the pattern of glycan structures found in each amphibian species represent the support for a specifie recognition of the ovule by the spermatozoon. [Pg.170]

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. [Pg.499]

Focarelli R, Rosati F (1995) The 220-kDa vitelline coat glycoprotein mediates sperm binding in the polarized egg of Unio elongatulus through O-linked oligosaccharides. Dev Biol 171 606-614... [Pg.464]

Wikramanayake AH, Clark W Jr (1994) Two extracellular matrices from oocytes of the marine shrimp Sicyonia ingentis that independently mediate only primary or secondary sperm binding. Dev Growth Differ 36 89-101... [Pg.466]

Lefebvre, R. and Suarez, S.S. (1996). Effect of capacitation on bull sperm binding to homologous oviductal epithehum. Biol. Beprod. 54, 575—582. [Pg.450]

Olson, J.H., Xiang, X.Y., Ziegert, T, Kittelson, A., Rawls, A., Rieber, A.L. and Chandler, D.E. (2001). AUurin, a 21-kDa sperm chemoattractant from Xenopus egg jelly, is related to mammalian sperm-binding proteins. Proc. Natl. Acad. Sci. U.S.A. 98, 11205-11210. [Pg.451]

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. [Pg.154]

De Rauw, I. M. C. Van Soom, A. Laevens, H. Verberckmoes, S. De Kruif, A. Sperm binding to epithelial oviduct explants in bulls with different nonreturn rates investigated with a new in vitro model. Biol. Reprod. 2002, 67, 1073-1079. [Pg.253]


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