Richard L. Easton

TL;DR: The potent inhibitory effect of glycodelin on initial human sperm-zona pellucida binding is consistent with previous suggestion that this cell adhesion event requires a selectin-like adhesion process and raises the possibility that a convergence between immune and gamete recognition processes may have occurred in the types of carbohydrate ligands recognized in the human.

TL;DR: In this study, oligosaccharides linked to CA125 derived from the human ovarian tumor cell line OVCAR-3 were subjected to rigorous biophysical analysis and indicated the presence of both core type 1 and type 2 glycans, thereby promoting tumor progression.

TL;DR: This study provides the first evidence for gender-specific glycosylation that may serve to regulate key processes involved in human reproduction and contribute to the immunosuppressive activity of human seminal plasma and to the low immunogenicity of sperm.

TL;DR: Biophysical analyses have revealed the presence of both high mannose and complex-type N-glycans in murine zona pellucida, and Oligosaccharides terminated with GalNAcβ1–4Gal have been implicated in the secondary binding interaction that occurs following the acrosome reaction.

TL;DR: The evidence indicates that gly codelin-A mediated its biological activities via its unusual oligosaccharide sequences that are not associated with glycodelin-S, and the results of sugar analysis and neuraminidase digestion lead us to conclude that glycodelo-S and glycodel-A are differentially glycosylated forms of similar proteins.