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Mammalian fertilization
TLDR
Bustards are generally very solitary, only meeting at leks in spring when the males gather to dance competitively, displaying their fluffy wing and tail feathers to the females, and far fewer males than females are needed for breeding. Expand
Identification of Mouse Sperm SED1, a Bimotif EGF Repeat and Discoidin-Domain Protein Involved in Sperm-Egg Binding
TLDR
It is illustrated that Notch-like EGF and discoidin/C domains, protein motifs that facilitate a variety of cellular interactions, participate in gamete recognition as well. Expand
Complementarity between sperm surface beta-1,4-galactosyltransferase and egg-coat ZP3 mediates sperm-egg binding.
TLDR
Mouse sperm Gal-transferase specifically recognizes those oligosaccharides on ZP3 that have sperm-binding activity, but does not interact with other zona pellucida glycoproteins, demonstrating a more stringent substrate specificity for the sperm enzyme. Expand
Egg cortical granule N-acetylglucosaminidase is required for the mouse zona block to polyspermy
TLDR
It is demonstrated that N-acetylglucosaminidase is localized in cortical granules and is responsible for the loss in sperm-binding activity leading to the zona block to polyspermy, and a related glycosidase may be present in corticalgranules and be responsible for ZP3's loss of sperm- binding activity at fertilization. Expand
Estrogen, Efferent Ductules, and the Epididymis1
TLDR
Ligand-independent and DNA-binding Esr1 mutant models further demonstrate the complexity and importance of both signaling pathways in maintenance of efferent ductules and epididymis, and the presence of not only classical nuclear receptors but also cytoplasmic ESR and rapid responding membrane receptors. Expand
Targeted mutation in beta1,4-galactosyltransferase leads to pituitary insufficiency and neonatal lethality.
TLDR
A requirement for terminal oligosaccharide sequences for anterior pituitary hormone function is supported by mice created bearing a targeted mutation in beta1,4-galactosyltransferase, an enzyme responsible for elaboration of many of the proposed biologically active carbohydrate epitopes. Expand
Complementarity between sperm surface β-l,4-galactosyl-transferase and egg-coat ZP3 mediates sperm–egg binding
TLDR
Mouse sperm Gal-transferase specifically recognizes those oligosaccharides on ZP3 that have sperm-binding activity, but does not interact with other zona pellucida glycoproteins, demonstrating a more stringent substrate specificity for the sperm enzyme. Expand
Sperm require beta-N-acetylglucosaminidase to penetrate through the egg zona pellucida.
TLDR
Investigating the presence and function of acrosomal glycosidases capable of removing the GalTase-binding site from zona pellucida glycoproteins demonstrated 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. Expand
Sperm from beta 1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly.
TLDR
The effects of targeted mutations in beta1,4-galactosyltransferase, the best studied of the candidate receptors for ZP3, are described and it is shown that the defective sperm-egg interactions in gt(-/-) mice are due directly to a loss of the long galacto-transferase isoform from the sperm surface and are independent of the state of intracellular galactosyation during spermatogenesis. Expand
Activation of a G protein complex by aggregation of beta-1,4-galactosyltransferase on the surface of sperm.
TLDR
The cytoplasmic domain of cell surface GalTase appears to enable it to function as a signal-transducing receptor for extracellular oligosaccharide ligands. Expand
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