scholarly journals p-Aminobenzamidine, an acrosin inhibitor, inhibits mouse sperm penetration of the zona pellucida but not the acrosome reaction

Reproduction ◽  
1982 ◽  
Vol 65 (1) ◽  
pp. 185-194 ◽  
Author(s):  
L. R. Fraser
Keyword(s):  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Mouse Sperm ◽  
Sperm Penetration

Functional interactions between sulphated polysaccharides and proacrosin: implications in sperm binding and digestion of zona pellucida

Zygote ◽  
1999 ◽  
Vol 7 (2) ◽  
pp. 105-111 ◽  
Author(s):  
R. D. Moreno ◽  
M. Hoshi ◽  
C. Barros
Keyword(s):  
Zona Pellucida ◽  
Active Site ◽  
Acrosome Reaction ◽  
Penetration Rate ◽  
Limited Proteolysis ◽  
Sulphated Polysaccharides ◽  
Functional Interactions ◽  
Sperm Binding ◽  
Sperm Penetration ◽  
Sperm Acrosome Reaction

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 binding of the monoclonal antibody against human acrosin C5F10 to boar or human proacrosin. These results suggest that fucoidan, solubilised ZPGs and ARIS bind to a related domain on the proacrosin surface. Moreover, ARIS was able to induce human proacrosin activation. On the other hand, neither ARIS nor heparin from porcine intestinal mucosa or bovine lung induced hamster sperm acrosome reaction or sperm motility. Recent data showed that acrosin is involved in dispersal of the acrosomal matrix after acrosome reaction. Thus, the control of the ZPG glycan chains over proacrosin activation may regulate both sperm penetration rate and limited proteolysis of zona pellucida proteins.

Interactions between gametes leading to fertilization: the sperm's eye view

1995 ◽  
Vol 7 (4) ◽  
pp. 927 ◽  
Author(s):  
BT Storey
Keyword(s):  
Plasma Membrane ◽  
Acrosome Reaction ◽  
Mammalian Species ◽  
Sperm Chromatin ◽  
Peptide Backbone ◽  
Mouse Sperm ◽  
Gamete Interactions ◽  
Sperm Plasma Membrane ◽  
Sperm Penetration ◽  
Strong Candidate

Sexual reproduction requires that the gamete carrying the male-derived haploid chromatin join with the gamete carrying the female-derived haploid chromatin during fertilization to produce the diploid zygote. To accomplish this feat, the sperm must not only meet the egg, it must recognize the egg and be recognized in turn by the egg, and in the end must enter and be engulfed by the egg. In this selective overview of gamete interactions that lead to fertilization, encounters of three kinds, followed by the finale of gamete fusion, are considered from the sperm's viewpoint, with particular emphasis on the mammalian species with the mouse as the principal model. The first encounter is with the zona pellucida of the egg, to whose surface the sperm must bind. Mouse sperm appear to have four binding sites for zona ligands. Three interact with sugar moieties of the oligosaccharide chains of the mouse zona glycoprotein ZP3; the fourth binds a peptide backbone arginine. Capacitation is not required for this encounter, but is obligate for the second encounter--induction of the acrosome reaction in the bound sperm. The acrosome reaction is an exocytotic process that makes available the enzymatic machinery needed for sperm penetration the zona which is the end point of a sequence of reactions directed by intracellular signalling systems. In mouse sperm, these systems are presumed to be activated by ligands on ZP3 binding to ligand-specific sperm receptors with consequent aggregation of receptors. No receptor has been identified with certainty, nor have candidates for putative ZP3 ligands been identified. Completion of the acrosome reaction allows the sperm to penetrate the zona and, bind to the egg plasma membrane, thereby completing the third encounter. In the mouse, a 94-kDa protein appears essential for this binding. In the guinea-pig, a sperm plasma membrane protein (formerly PH-30, now fertilin), is a strong candidate for the mediator of the fusion process by which the egg engulfs the sperm. Decondensation of the sperm chromatin reverses the remarkable packing of DNA organized by sperm protamines. Mitochondrial DNA is also engulfed by the egg; the question of whether this DNA makes a small finite, or null, contribution to cytosolic inheritance is still in debate. The puzzles attending these encounters are presented as reminders of the intricacy and fascination, as well as of the vital necessity, of gamete interaction.

scholarly journals Epididymal Maturation and the Acrosome Reaction in Mouse Sperm: Response to Zona Pellucida Develops Coincident with Modification of M42 Antigen1

1988 ◽  
Vol 38 (1) ◽  
pp. 221-233 ◽  
Author(s):  
Katherine A. Lakoski ◽  
Christopher P. Carron ◽  
Christine L. Cabot ◽  
Patricia M. Saling
Keyword(s):  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Mouse Sperm ◽  
Epididymal Maturation

Effects of oviductal fluid and heparin on fertility and characteristics of porcine spermatozoa

Zygote ◽  
1997 ◽  
Vol 5 (1) ◽  
pp. 61-65 ◽  
Author(s):  
Nam-Hyung Kim ◽  
Billy N. Day ◽  
Joon-Gyo Lim ◽  
Hoon Taek Lee ◽  
Kil Saeng Chung
Keyword(s):  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Time Points ◽  
Sperm Penetration ◽  
The Mean ◽  
Oviductal Fluid ◽  
Porcine Spermatozoa

SummaryThe objective of this study was to determine the effects of oviductal fluid and heparin on sperm penetration and the characteristics of spermatozoa. The addition of oviductal fluid and heparin to the fertilisation medium decreased sperm penetration and the mean number of spermatozoa in penetrated eggs. The number of spermatozoa firmly bound to zona pellucida was also decreased in the presence of oviductal fluid and heparin. Chlortetracycline (CTC) fluorescence patterns were used to determine the incidence of capacitation and the acrosome reaction. The proportion of capacitated and acrosome-free spermatozoa increased when spermatozoa were exposed for 1.5 and 3 h to oviductal fluid and heparin. In contrast heparin alone did not increase the number of capacitated spermatozoa at these time points. These results suggest that factor(s) in oviductal secretions reduce polyspermic fertilisation and the number of spermatozoa that will penetrate porcine oocytes. The reduction of polyspermic penetration by oviductal secretions may be due to a reduced number of spermatozoa in the fertilisation medium with an intact acrosome.

Interaction of mouse sperm with purified sperm receptors covalently linked to silica beads

1989 ◽  
Vol 92 (4) ◽  
pp. 713-722
Author(s):  
M.H. Vazquez ◽  
D.M. Phillips ◽  
P.M. Wassarman
Keyword(s):  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Solid Phase ◽  
Galactose Oxidase ◽  
Flow Cytofluorometry ◽  
Mouse Sperm ◽  
Sperm Binding ◽  
Silica Beads ◽  
Covalently Linked ◽  
Solid Phase Assay

We describe a solid-phase assay that has permitted further analysis of zona pellucida glycoprotein, ZP3, as sperm receptor and acrosome reaction-inducer during fertilization in mice. The assay employs silica beads that contain epoxy groups to which purified, mouse oocyte ZP3 is covalently linked (ZP3-beads). ZP3-beads were characterized, e.g. by whole-mount autoradiography and flow cytofluorometry, incubated with capacitated mouse sperm under a variety of conditions, and the extent of sperm binding determined by light microscopy. Results of experiments presented suggest the following: (1) sperm bind specifically to ZP3-beads, but not to silica beads either exposed to 2-aminoethanol or derivatized with oocyte ZP2, fetuin or bovine serum albumin. (2) In nearly all cases, only one sperm binds per ZP3-bead and binding occurs via the sperm head. (3) The extent of sperm binding to ZP3-beads is dependent on ZP3 and sperm concentrations, as well as on incubation time and temperature. (4) Sperm binding to ZP3-beads is unaffected by antibodies directed against ZP3, but is inhibited in a reversible manner by treatment of ZP3-beads with galactose oxidase. (5) Only acrosome-intact sperm bind to ZP3-beads but, once bound, sperm can undergo the acrosome reaction, which results in their release from ZP3-beads. (6) Islet-activating protein and 3-quinuclidinyl benzilate, two inhibitors of the zona pellucida-induced acrosome reaction, prevent sperm bound to ZP3-beads from undergoing the acrosome reaction. These results confirm and extend previous studies of sperm-egg interaction in mice, and suggest that the solid-phase assay will be useful for both cellular and biochemical analyses of mammalian fertilization.

Effect of Epidermal Growth Factor on Mouse Sperm Acrosome Reaction Induced by Zona Pellucida

1994 ◽  
Vol 31 (2-3) ◽  
pp. 116-122 ◽  
Author(s):  
Satoru Furuya ◽  
Yoshihiro Endo ◽  
Mikiko Oba ◽  
Yukari Matsui ◽  
Shuetu Suzuki ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Mouse Sperm ◽  
Epidermal Growth ◽  
Sperm Acrosome Reaction ◽  
Sperm Acrosome
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