Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.21 (beta-glucosidase)
 3,280 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Fertilization in the mouse is initiated by sperm beta 1,4-galactosyltransferase (GalTase) binding to terminal N-acetylglucosamine residues on the zona pellucida glycoprotein ZP3. Binding of ZP3 induces exocytosis of the sperm acrosome, whose contents are believed to digest a penetration slit in the zona matrix through which sperm reach the egg. As a consequence of acrosomal exocytosis, GalTase is redistributed to the lateral aspect of the sperm head, where its function remains unknown. In this location, GalTase could conceivably impede zona penetration by binding to N-acetylglucosamine residues exposed on zona pellucida glycoproteins. Therefore, in this study we investigated the presence and function of acrosomal glycosidases capable of removing the GalTase-binding site from zona pellucida glycoproteins. beta-N-acetylglucosaminidase was found at very high levels in sperm, being more than 20-fold higher than other glycosidases assayed. The specific isozymic variant was identified as beta-hexosaminidase B. beta-N-acetylglucosaminidase was localized to sperm acrosomes by biochemical and indirect immunofluorescence studies and was released during the acrosome reaction, as expected for an enzyme involved in zona penetration. To determine if, in fact, acrosomal beta-N-acetylglucosaminidase facilitated penetration through the zona, an assay was developed using eggs that were rendered incapable of triggering the block to polyspermy. A specific competitive inhibitor of beta-N-acetylglucosaminidase activity, PUGNAC, inhibited sperm penetration of the zona in a dose-dependent manner, whereas a closely related beta-glucosidase inhibitor, PUGLU, had no effect on zona penetration or on beta-N-acetylglucosaminidase activity. Neither glycosidase inhibitor affected sperm motility or induction of the acrosome reaction. These results demonstrate that beta-N-acetylglucosaminidase is found in sperm acrosomes and is released during the acrosome reaction, at which time it facilitates sperm penetration through the zona. These results also imply that sperm have developed mechanisms to prevent the formation of stable interactions between surface receptors and their zona pellucida ligands during penetration.
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PMID:Sperm require beta-N-acetylglucosaminidase to penetrate through the egg zona pellucida. 826 54

Our understandings of the molecular and cellular mechanisms underlying tubal transport of embryos are poor. This study describes the essential role of the molecules on the zona pellucida (ZP) in the tubal transport of mouse embryos. The bovine and porcine embryos that were interspecifically transferred to the mouse oviduct were selectively retained in the oviduct and rarely transported to the uterus. Antiserum ZP3-9 against synthetic peptides that are specific for mouse ZP3, significantly interfered with tubal transport of the treated embryos. The treatment of mouse embryos with antiserum ZP2-20 against the synthetic peptides, deduced from the sequences that are conserved in the structure of ZP2 from mouse and human, also inhibited their tubal transport. Among various proteolytic and glycosidic enzymes, treatments with trypsin and beta-glucosidase prior to transfer to the oviduct, significantly interfered with the tubal transport of the enzyme-treated mouse embryos. We hypothesize that species-specific epitopes on the ZP may be recognized by the oviductal cilia and/or the epithelial cells of ducts for tubal transport.
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PMID:Essential role of ZP molecules in tubal transport of embryos in mice. 1183 78