Glycosylation patterns of proteins in trophoblast and decidua of the cat placenta

BARBEITO; FERNANDEZ ; DIESSLER; ORTEGA; GIMENO; PORTIANSKY

Simposio; VI Latin American Symposium on Maternal-Fetal Interaction and Placenta and V Latin American Symposium on Reproductive Immunology Meeting; 2015

The aim of this study was to characterize glycoconjugates of syncytiotrophoblast, cytotrophoblast and decidual cells of mature feline placenta. Samples from 12 normal pregnant female cats, after 45±5 days of gestation were obtained by hysterectomy. Sections were processed for routine observation. Lectinhistochemistry was performed using biotinylated lectins to characterize the expression of saccharides. Trophoblast expressed a varied composition of glycans, highly exposing terminal N-Acetylglucosamine residues and non-sialylated galactose and N-Acetyl galactosamine oligomers. Phaseolus vulgaris erythroagglutinin lectin, which recognized highly branched N-linked residues, was restricted to the syncytiotrophoblast. Unlike results reported in humans, mice and rats on lectin affinity of decidual cells, sialic acids and complex N-linked oligosaccharides were not demonstrated in cats. Glycosylation of proteins determines many of their final properties, thus becoming essential for the embryo-maternal relation during implantation and placentation. Knowledge about the glycosylation profile of the normal cat placenta may lead to a better understanding of both normal and pathological reproductive events.