A lectin binding analysis of glycosylation patterns during development of the equine placenta.
Abstract: The glycosylation of the equine interhaemal barrier and areola was studied throughout the period of gestation. Placentae of 35, 37, 50, 119, 152, 200, 280 and 300 days gestation were investigated, using semithin plastic embedded sections and a panel of 15 biotinylated lectins with an avidin-peroxidase revealing system. Glycosylation of the trophoblast and maternal epithelium showed the most change during the first 50 days of gestation, being associated with the initial stages of adhesion and attachment. In the trophoblast, non-bisected tri/tetraantennary complex N-glycan was only evident after day 37 and terminal N-acetyl galactosamine, alpha2,3- and alpha2,6-linked sialic acids disappeared at the same time. The areolar trophoblast exhibited some differences from microcotyledonary areas, especially with respect to 2-deoxy, 2-acetamido alpha-galactose and tri/tetraantennary, non-bisected complex N-glycan, suggesting that the differences in function between microcotyledonary and areolar trophoblast are reflected at both the morphological and the biochemical level. Granules of the maternal uterine epithelium bound many lectins, particularly those with specificity for bisected and non-bisected bi/triantennary N-linked glycan, 2-deoxy, 2-acetamido alpha-galactosyl, beta-galactosyl and some fucosylated termini. Binding to sialic acids in alpha2,3- and alpha2,6-linkage was sparse. Maternal and fetal capillaries showed little change in glycan expression over the period studied, being rich in bisected and non-bisected bi/triantennary N-linked glycan and sialic acids, with some terminal N-acetyl galactosamine and no detectable terminal fucosyl residues.
Publication Date: 1999-02-09 PubMed ID: 9950144DOI: 10.1053/plac.1998.0354Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research examined the sugar molecule patterns, known as glycosylation, in the placenta of a horse during different stages of pregnancy. The study found that these patterns change over time, especially during early pregnancy when the placenta is sticking onto the uterus, suggesting that these molecules could be important for early fetal development.
Introduction
- This research focuses on studying the process of glycosylation, where sugar molecules are added to proteins and other organic molecules, in the horse placenta during pregnancy.
- Glycosylation is a crucial process that affects the structure and function of cells and proteins, and is crucial in biological processes such as cell-cell adhesion and immune response.
Methodology
- The researchers examined the placenta at several points – 35, 37, 50, 119, 152, 200, 280 and 300 days into the gestation period.
- They used semithin plastic embedded sections and a set of 15 biotinylated lectins (proteins that bind to specific sugar molecules) along with an avidin-peroxidase system, which aids in the visualisation of sugar molecule patterns.
Findings
- The most significant changes in glycosylation of the trophoblast (part of the placenta) and maternal epithelium occurred in the first 50 days of gestation, associated with the initial stages of adhesion and attachment of the placenta to the uterus.
- In the trophoblast, a type of complex sugar structure (non-bisected tri/tetraantennary complex N-glycan) was only seen after day 37 while other sugar forms disappeared at the same time.
- The researchers noted differences in glycosylation between areolar trophoblast (specially modified placental cells) and microcotyledonary areas, suggesting that the biochemical and structural difference between these areas could be attributed to their differing functions during pregnancy.
- The study also identified a variety of sugars bound to the maternal uterine epithelium, with a sparse binding to sialic acids in a particular linkage pattern.
- The study reports little change in sugar expression in both maternal and fetal capillaries throughout the investigated period, with no detectable terminal fucosyl residues.
Conclusion
- The research showcases how the glycosylation pattern changes over the course of a horse’s pregnancy, particularly documenting the biochemical and structural variations during the placenta adhesion and attachment period.
- The insights provided by this study could be paramount in understanding the placental biology and in the study of pregnancy complications related to placental adhesion and development.
Cite This Article
APA
Jones CJ, Wooding FB, Dantzer V, Leiser R, Stoddart RW.
(1999).
A lectin binding analysis of glycosylation patterns during development of the equine placenta.
Placenta, 20(1), 45-57.
https://doi.org/10.1053/plac.1998.0354 Publication
Researcher Affiliations
- Department of Pathological Sciences, University of Manchester, UK. carolyn.jones@man.ac.uk
MeSH Terms
- Acetylgalactosamine / metabolism
- Animals
- Biotinylation
- Capillaries / metabolism
- Epithelium / metabolism
- Female
- Fucose / metabolism
- Galactose / metabolism
- Gestational Age
- Glycosylation
- Histocytochemistry
- Horses / physiology
- Lectins / metabolism
- Microvilli / metabolism
- Placenta / anatomy & histology
- Placenta / blood supply
- Placenta / physiology
- Polysaccharides / metabolism
- Pregnancy
- Sialic Acids / metabolism
- Trophoblasts / metabolism
- Uterus / metabolism
Citations
This article has been cited 2 times.- Navarrete Zamora MB, da Silva TS, da Silva MD, Almeida GHDR, da Silva-Júnior LN, Horvath-Pereira BO, Baracho Hill AT, Acuña F, Carreira ACO, Barreto RDSN, Sato AS, Miglino MA. Term alpaca placenta glycosylation profile and its correlation with pregnancy maintenance and fetal survival. Front Cell Dev Biol 2023;11:1193468.
- Clark GF. Functional glycosylation in the human and mammalian uterus. Fertil Res Pract 2015;1:17.
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