title: Preeclampsia transforms membrane N-glycome in human placenta.
abstract: Posttranslational modifications (PTM) which accompany pathological conditions affect protein structure, characteristics and modulate its activity. Glycosylation is one of the most frequent PTM influencing protein folding, localisation and function. Hypertension is a common gestational complication, which can lead to foetal growth restriction (IUGR) and even to foetal or maternal death. In this work we focused on the impact of preeclampsia complicated with IUGR on placental membrane N-glycome. Results have shown that preeclampsia reduced fucosylation of placental glycans, increased the appearance of paucimannosidic and mannosidic structures with lower number of mannose residues and decreased the amount of glycans with more mannose residues. Since preeclampsia is tightly connected to IUGR, glycosylation changes were investigated also on the functional membrane receptors responsible for growth: insulin receptor and the type 1 insulin-like growth factor receptor (IR and IGF1R). It was found that IR present in the IUGR placenta contained significantly less α2,6-Sia. Therefore, glycans on placental membranes alter due to preeclampsia, but changes seen at the level of the entire N-glycome may be different from the changes detected at the level of a specific glycoprotein. The difference recorded due to pathology in one membrane molecule (IR) was not found in another homologous molecule (IGF1R). Thus, besides studying the glycosylation pattern of the entire placental membrane due to preeclampsia, it is inevitable to study directly glycoprotein of interest, as no general assumptions or extrapolations can be made.
authors.affiliation: Institute for the Application of Nuclear Energy - INEP, University of Belgrade, Belgrade 381, Serbia. Electronic address: draganar@inep.co.rs.
authors.forename: Dragana
authors.initials: D
authors.lastname: Robajac
authors.affiliation: Department for Molecular Biomedical Research, VIB, Ghent 32, Belgium; Department of Biomedical Molecular Biology, Ghent University, Ghent 32, Belgium.
authors.forename: Valerie
authors.initials: V
authors.lastname: Vanhooren
authors.affiliation: Institute for the Application of Nuclear Energy - INEP, University of Belgrade, Belgrade 381, Serbia.
authors.forename: Romana
authors.initials: R
authors.lastname: Masnikosa
authors.affiliation: Department of High-risk Pregnancies, Clinic of Gynaecology and Obstetrics "Narodni Front", University of Belgrade, Belgrade 381, Serbia.
authors.forename: Željko
authors.initials: Ž
authors.lastname: Miković
authors.affiliation: Department of High-risk Pregnancies, Clinic of Gynaecology and Obstetrics "Narodni Front", University of Belgrade, Belgrade 381, Serbia.
authors.forename: Vesna
authors.initials: V
authors.lastname: Mandić
authors.affiliation: Department for Molecular Biomedical Research, VIB, Ghent 32, Belgium; Department of Biomedical Molecular Biology, Ghent University, Ghent 32, Belgium.
authors.forename: Claude
authors.initials: C
authors.lastname: Libert
authors.affiliation: Institute for the Application of Nuclear Energy - INEP, University of Belgrade, Belgrade 381, Serbia.
authors.forename: Olgica
authors.initials: O
authors.lastname: Nedić
mesh_terms: D002462:Cell Membrane / Q000378:metabolism*; D004730:Endothelium, Vascular / Q000378:metabolism / Q000473:pathology; D005260:Female; D006023:Glycoproteins / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D006973:Hypertension / Q000378:metabolism; D010920:Placenta / Q000378:metabolism*; D011225:Pre-Eclampsia / Q000378:metabolism*; D011247:Pregnancy
chemical_list: D006023:Glycoproteins
keywords: DSA-FACE; Glycosylation; IGF1R; IR; IUGR; Placental membrane; Preeclampsia