Distribution of sugar residues in human placentas from pregnancies complicated by hypertensive disorders

Marini, Mirca; Bonaccini, Laura; Thyrion, Giorgia Donata Zappoli; Vichi, Debora; Parretti, Elena; Sgambati, Eleonora

doi:10.1016/j.acthis.2010.12.001

Cited by 34 publications

(24 citation statements)

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“…However, substantial binding of these lectins was observed on STB and CTB associated with the placentas of patients that developed PIH, PE or PE with HELLP syndrome. Binding sites for SNA were expressed on STB from the placentas of patients that developed PE with HELLP, but not on TB from any other patient group analyzed in this study [112]. Clearly, these results indicate that a shift in glycosylation is occurring during the development of these obstetrical syndromes, but how these changes impact this condition remains to be defined.…”

Section: Introductionmentioning

confidence: 70%

“…Sgambati and coworkers previously analyzed the distribution of sugar residues in human placentas from uncomplicated pregnancies and those affected by different hypertensive disorders (pregnancy-induced hypertension (PIH), PE, PE with hemolysis, elevated liver enzymes and low platelets (HELLP) syndrome) [112]. They employed ConA, WGA, PNA, SBA, DBA, UEA, GNA, DSA, MAA and DSA in combination with other chemical and enzymatic treatments to perform this analysis.…”

Section: Introductionmentioning

confidence: 99%

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Functional glycosylation in the human and mammalian uterus

Clark

2015

Fertil Res and Pract

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BackgroundGlycosylation is the most common and structurally diverse of all the post-translational modifications of proteins. Lipids and extracellular matrices are also often glycosylated. The mammalian uterus is highly enriched in glycoconjugates that are associated with the apical surfaces of epithelial cells and the secretions released by both epithelial and stromal cells. These glycoconjugates interact primarily with sperm, the implanting embryo, the fetus, and any pathogen that happens to gain entry into the uterus. Secretions of the endometrial glands increase substantially during the luteal phase of the menstrual cycle. These secretions are highly enriched in glycoproteins and mucins that promote specific uterine functions.FindingsLectins and antibodies have been employed in the majority of the studies focused on uterine glycosylation have employed to define the expression of carbohydrate sequences. However, while these studies provide insight about potential glycosylation, precise information about glycan structure is lacking. Direct sequencing studies that employ biochemical or mass spectrometric methods are far more definitive, but have rarely been employed with uterine glycoproteins. Both lectin/antibody binding and direct carbohydrate sequencing studies that have been focused on the mammalian uterus are reviewed. The primary functional role of the eutherian uterus is to facilitate fertilization and nurture the developing embryo/fetus. Trophoblasts are the primary cells that mediate the binding of the embryo and placenta to the uterine lining. In mammals that utilize hemochorial placentation, they invade the decidua, the specialized endometrial lining that forms during pregnancy. Trophoblasts have also been analyzed for their lectin/antibody binding as a complement to the analysis of the uterine cells and tissues. They will also be reviewed here.ConclusionsThe functional roles of the glycans linked to uterine and trophoblast glycoconjugates remain enigmatic. Another major question in the human is whether defects in placental or uterine glycosylation play a role in the development the Great Obstetrical Syndromes. More recent findings indicate that changes in glycosylation occur in trophoblasts obtained from patients that develop preeclampsia and preterm birth. The functional significance of these changes remain to be defined. Whether such shifts happen during the development of other types of obstetrical syndromes remains to be determined.

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Section: Introductionmentioning

confidence: 70%

Section: Introductionmentioning

confidence: 99%

Functional glycosylation in the human and mammalian uterus

Clark

2015

Fertil Res and Pract

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“…Mild oxidation abolishes the staining with neuraminidase/PNA-SBA or KOH/neuraminidase/PNA-SBA when sialic acid does not contain C 7 -and/or C 8 -and/or C 9 -O-acetyl groups in the side-chain. Strong oxidation affects sialic acid sidechains lacking acetyl substituents in C 9 as well as penultimate ␤-galactose linked via ␣-2,6, while it does not oxidize if C 9 acetylated sialic acids linked ␣-2,3 bound to the penultimate ␤-galactose are present (Gabrielli et al, 2004;Adembri et al, 2011;Marini et al, 2011).…”

Section: Enzymatic and Chemical Treatmentsmentioning

confidence: 96%

“…In the 'direct' technique, Maackia amurensis agglutinin (MAA) and Sambucus nigra agglutinin (SNA) were used to identify and differentiate between sialic acids linked ␣-2,3 and ␣-2,6 to galactose or galactosamine, respectively (Shibuya et al, 1987;Wang et al, 1988;Gabrielli et al, 2004;Mencucci et al, 2011). In the second method peanut agglutinin (Arachis hypogaea) (PNA) and soybean agglutinin (Glycine maximus) (SBA), combined with neuraminidase digestion, deacetylation and differential oxidation to reveal acetylic groups, were used to investigate the expression of sialic acid linked to d-Gal(␤1→3)-d-GalNAc and to d-GalNAc > dGal respectively, and the structure of sialic acids (Gabrielli et al, 2004;Adembri et al, 2011;Marini et al, 2011). Lectins and their sugar residue specificity are listed in the Table 1. MAA and SNA were digoxigenin (DIG) labeled lectins (Roche Diagnostic, Mannheim, Germany).…”

Section: Lectin Histochemistrymentioning

confidence: 99%

“…Efficacy of digestion was tested treating adjacent sections, with and without prior deacetylation, with the enzyme solution, then submitting them to MAA and SNA labeling. Some control sections were treated with a desulfation procedure to eliminate sulfated groups present on the carbohydrate chains that could interfere with lectin binding (Gabrielli et al, 2004;Adembri et al, 2011;Marini et al, 2011).…”

Section: Controlsmentioning

confidence: 99%

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Expression and characterization of anionic components in the tubulointerstitial compartment of rat kidney during polymicrobial sepsis

et al. 2014

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Novel Spatiotemporal Glycome Changes in the Murine Placenta During Placentation Based on BS‐I Lectin Binding Patterns

Charalambous

Drakou

Nicolaou

et al. 2013

The Anatomical Record

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Although spatiotemporal changes of the glycome (full set of glycans, otherwise known as saccharides or carbohydrates) during placenta formation (placentation) are functionally and clinically important, they are poorly defined. Here, we elucidated novel aspects of the glycome during mouse placentation, from embryonic day 6.5 (E6.5) to E12.5, by investigating the largely unexplored binding distribution of lectin I from Bandeiraea simplicifolia (BS-I lectin), a glycan-binding protein that recognizes the DGalNAc and DGal glycans found at the terminal ends of specific oligosaccharides attached to lipids or proteins. We show that BS-I lectin binding marks all trophoblast cells during early placentation (E7.5 and E8.5 stages), continues in labyrinthine and junctional zone trophoblast but is lost from parietal trophoblast giant cells by E10.5/E11.5 (definitive placenta stage) and is lost from all trophoblast types, but marks the fetal capillary endothelium of the labyrinth, by E12.5. In the decidua basalis (the maternal part of the placenta), BS-I lectin positivity mainly marks the decidual stroma cells of the venous sinusoid area (E7.5 and E8.5 stages) and the entire decidua basalis by E10.5, as well as the osteopontin-positive subset of uterine natural killer (uNK) cells from E7.5 onwards. This work provides the first comprehensive description of the hitherto ill-defined spatiotemporal binding distribution of BS-I lectin in the fetal and maternal placenta between E6.5 and E12.5, thereby contributing to glycome elucidation during placentation. It also establishes BS-I lectin positivity as a novel pan-trophoblast marker during early placentation and as a new marker for mature uNK cells from E7.5 onwards. Anat Rec, 296:921-932, 2013. V C 2013 Wiley Periodicals, Inc.Key words: glycome; Bandeiraea simplicifolia lectin I; placenta; trophoblast development; uNK cellsThe glycome, or complete set of glycans (sugars or saccharides), of an organ includes the glycan part of all glycoconjugates (proteins or lipids covalently attached to glycans) present in it. Although glycans are best known for their ubiquitous role in energy metabolism, they also have more specific functions during embryonic development by

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Distribution of sugar residues in human placentas from pregnancies complicated by hypertensive disorders

Cited by 34 publications

References 48 publications

Functional glycosylation in the human and mammalian uterus

Functional glycosylation in the human and mammalian uterus

Expression and characterization of anionic components in the tubulointerstitial compartment of rat kidney during polymicrobial sepsis

Novel Spatiotemporal Glycome Changes in the Murine Placenta During Placentation Based on BS‐I Lectin Binding Patterns

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