Distribution of carbohydrates in the zona pellucida of human oocytes

Maymon, Batia Bar-Shira; Maymon, Ron; Ben-Nun, Isaac; Ghetler, Yehudith; Shalgi, R.; Skutelsky, Ehud

doi:10.1530/jrf.0.1020081

Cited by 46 publications

(21 citation statements)

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“…In man, results of lectin binding studies of human zonae (Maymon et al, 1994) are consistent with results from sugar competition of sperm binding to intact zona structures (Mori et al, 1989;Oehninger et al, 1990Oehninger et al, , 1991Miranda et al, 1997). These data indicate that mannosyl, N-acetylglucosaminyl and fucosyl residues contribute to the sperm receptor on the human zona.…”

Section: Zona Bindingsupporting

confidence: 68%

“…Binding of spermatozoa to ZP3 is primarily regulated by the glycan side chains. The structure of these glycans is quite complex and heterogeneous (Mori et al, 1991;Hokke et al, 1993Hokke et al, , 1994 and differs among species (Shalgi et al, 1991;Maymon et al, 1994). A small class of O-linked glycans, attached to the carboxy-terminal half of the ZP3 polypeptide (Litscher and Wassarman, 1996) and terminating in either galactose-α1-3-galactose (Florman and Wassarman, 1985;Bleil and Wassarman, 1988) or galactose-β1-4N-acetylglucosamine (Miller et al, 1992), act as the primary receptor for mouse spermatozoa.…”

Section: Zona Bindingmentioning

confidence: 99%

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Modelling human sperm-egg interactions in vitro: signal transduction pathways regulating the acrosome reaction

Benoff

1998

Molecular Human Reproduction

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Recent advances in characterizing sperm surface receptors and ion channels, when combined with the rapidly expanding knowlege of interactions among second messenger systems in somatic cells, permit formulation of a tentative molecular mechanism for the regulation of the human sperm acrosome reaction. As spermatozoa pass through the cumulus mass, progesterone binds to its sperm surface receptor, alkalinizes the sperm head cytosol and potentiates changes in intracellular ionized calcium. Primary binding of spermatozoa to egg involves receptors for mannosyl, N-acetyglucosaminyl and, possibly, fucosyl residues of the glycosylated zona protein, ZP3. These receptors aggregate on multivalent ligand binding, migrate to the equatorial region along an actin filament network formed between the plasma and acrosomal membranes during capacitation, and activate a G protein/protein kinase A/protein kinase C second messenger system and a secondary proteolysis signal. Binding of a receptor tyrosine kinase to ZP3 amino acid residues simultaneous with the sugar recognition event triggers tyrosine phosphorylation signalling. All signals combine to open a voltagedependent calcium channel. The resulting elevated calcium signal depolymerizes the inter-membrane actin network and activates phospholipases, leading to an acrosome reaction.

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Section: Zona Bindingsupporting

confidence: 68%

Section: Zona Bindingmentioning

confidence: 99%

Modelling human sperm-egg interactions in vitro: signal transduction pathways regulating the acrosome reaction

Benoff

1998

Molecular Human Reproduction

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“…As outlined by Gabius [1998] and in this issue by von der Lieth et al [1998], these sugar receptors frequently select a low-energy conformation for ligand binding. The wide panel of commercially available lectins with narrow sugar specificity allows the identification of distinct carbohydrate structures and particularly their in situ localization [Shalgi et al, 1991;Aviles et al, 1994;Maymon et al, 1994;Skutelsky et al, 1994]. Comparative cytochemical studies manifest species-dependent variations in the expression and distribution of sugar moieties throughout the ZP.…”

Section: Carbohydrate Composititon Of Zona Glycoproteinsmentioning

confidence: 99%

Protein-Carbohydrate Interactions during Fertilization

Sinowatz

Plendl

Kölle

1998

Cells Tissues Organs

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Interaction between gametes during fertilization is at least in part regulated by carbohydrate moieties of the zona pellucida (ZP) and carbohydrate binding proteins of the sperm surface. This review focuses on the protein-carbohydrate interactions during the primary binding of the sperm to the ZP in different species. Synthesis, structure and composition of the ZP are summarized. The functional significance of carbohydrate residues of the ZP as sperm receptor is discussed. Sperm surface proteins known to have specific ZP and carbohydrate-binding sites including the mouse β1,4-galactosyltransferase and sp56, the rabbit protein Sp17, a human mannose-binding protein and several members of the spermadhesin family are presented. oooooooooooooooooooo

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“…73 Human Binding studies with various lectins suggest that the human ZP matrix has a high concentration of D-mannose. 95,96 The presence of mannose-binding sites has been reported on human sperm. 97,98 Several oligosaccharide moieties, such as mannose, GlcNAc, fucose and galac- 83 The N-terminal fragment of ZP3 failed to induce the AR, whereas both C-terminal fragments induced the AR.…”

Section: Zp4mentioning

confidence: 99%

Acrosome reaction: relevance of zona pellucida glycoproteins

Gupta

Bhandari²

2010

Asian J Androl

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During mammalian fertilisation, the zona pellucida (ZP) matrix surrounding the oocyte is responsible for the binding of the spermatozoa to the oocyte and induction of the acrosome reaction (AR) in the ZP-bound spermatozoon. The AR is crucial for the penetration of the ZP matrix by spermatozoa. The ZP matrix in mice is composed of three glycoproteins designated ZP1, ZP2 and ZP3, whereas in humans, it is composed of four (ZP1, ZP2, ZP3 and ZP4). ZP3 acts as the putative primary sperm receptor and is responsible for AR induction in mice, whereas in humans (in addition to ZP3), ZP1 and ZP4 also induce the AR. The ability of ZP3 to induce the AR resides in its C-terminal fragment. O-linked glycans are critical for the murine ZP3-mediated AR. However, N-linked glycans of human ZP1, ZP3 and ZP4 have important roles in the induction of the AR. Studies with pharmacological inhibitors showed that the ZP3-induced AR involves the activation of the G i -coupled receptor pathway, whereas ZP1-and ZP4-mediated ARs are independent of this pathway. The ZP3-induced AR involves the activation of T-type voltage-operated calcium channels (VOCCs), whereas ZP1-and ZP4-induced ARs involve both T-and L-type VOCCs. To conclude, in mice, ZP3 is primarily responsible for the binding of capacitated spermatozoa to the ZP matrix and induction of the AR, whereas in humans (in addition to ZP3), ZP1 and ZP4 also participate in these stages of fertilisation. Keywords: acrosome reaction; fertilisation; oocyte; signalling pathways; spermatozoa; zona pellucida glycoproteins INTRODUCTION Mammalian fertilisation is a highly synchronized process that involves a complex series of interactions between the spermatozoon and the egg, culminating in their unison. The initial steps in fertilisation involves the binding of the spermatozoon to the zona pellucida (ZP) matrix surrounding the egg, followed by induction of the acrosome reaction (AR) in the zona-bound spermatozoon, a pre-requisite for penetration of the ZP matrix by the spermatozoon. The spermatozoon acrosome is a Golgi-derived organelle that forms a cap over the anterior two-thirds of its nucleus. The AR involves the fusion of the sperm membrane with the outer acrosomal membrane, resulting in release of the acrosomal contents and exposure of the inner acrosomal membrane on the anterior head of the spermatozoon. Various physiological agents, such as progesterone, serum albumin, follicular fluid, hormones (including biogenic amines), hydrolytic enzymes (particularly proteases), hyaluronic acid and ZP glycoproteins, have been implicated in the induction of the AR. [1][2][3] In the present paper, we review the role of the ZP matrix and its constituents in AR induction. Various downstream signalling pathways involved in the ZP glycoprotein-induced AR will also be discussed. On the basis of the current literature and studies from our group, the salient differences in the ZP glycoprotein-mediated induction of the AR in mouse versus human will be highlighted.

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Distribution of carbohydrates in the zona pellucida of human oocytes

Cited by 46 publications

References 1 publication

Modelling human sperm-egg interactions in vitro: signal transduction pathways regulating the acrosome reaction

Modelling human sperm-egg interactions in vitro: signal transduction pathways regulating the acrosome reaction

Protein-Carbohydrate Interactions during Fertilization

Acrosome reaction: relevance of zona pellucida glycoproteins

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