Syncytiotrophoblast membrane protein glycosylation patterns in normal human pregnancy and changes with gestational age and parturition |
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Authors: | PD Arkwright CWG Redman PJ Williams RA Dwek TW Rademacher |
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Institution: | Nuffield Department of Obstetrics, John Radcliffe Hospital, Headington, Oxford, UK. |
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Abstract: | The fetally derived syncytiotrophoblast in the placenta form the major interface with the maternal circulation. Cell surface N-linked oligosaccharides are known to influence cell-cell interactions in a variety of ways. The N-linked oligosaccharide component of the human syncytiotrophoblast membrane has been purified from term placentae, and its biochemical structure analysed. Ninety-five per cent of structures were complex N-linked oligosaccharides, with the remaining 5 per cent being of the oligomannose type. Seventy-two per cent of oligosaccharides were sialylated; 50 per cent having two or more sialic acid residues. Such a population of N-linked oligosaccharides would be expected to provide a surface which inhibits interactions between trophoblast and maternal leukocytes. The temporal changes in syncytiotrophoblast N-linked oligosaccharides from the end of the second, and through the third trimester (25-41 weeks) were analysed, as were the changes which occur during parturition. There was no change in the degree of sialylation of these structures. The only significant change was a 37 per cent decrease in core fucosylation of complex N-linked sugars during gestation (P less than 0.005). Women delivered by caesarean section at term, had significantly higher levels of fucosylation (equivalent to women with a gestational age of 31-36 weeks), than those who laboured at term. Present knowledge of core fucosylation of N-linked oligosaccharides is discussed in relation to trophoblast functioning. |
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