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Updated: Mar 28, 2026

Author Spotlight: Modeling an Aspect of Preeclampsia in Female Mice Using Hypoxic Human Placenta-Derived Small Extracellular Vesicles
Published on: January 26, 2024
Preeclampsia transforms membrane N-glycome in human placenta
Dragana Robajac1, Valerie Vanhooren2, Romana Masnikosa1
1Institute for the Application of Nuclear Energy - INEP, University of Belgrade, Belgrade 381, Serbia.
Preeclampsia with foetal growth restriction alters placental N-glycans, reducing fucosylation and increasing simpler mannose structures. Specific receptor changes, like reduced sialylation on the insulin receptor, highlight the need for targeted glycoprotein analysis.
Area of Science:
- Biochemistry
- Reproductive Biology
- Pathology
Background:
- Posttranslational modifications (PTM) like glycosylation impact protein function.
- Preeclampsia, a gestational complication, often leads to intrauterine growth restriction (IUGR).
- Placental function is crucial for foetal development.
Purpose of the Study:
- To investigate the impact of preeclampsia complicated with IUGR on the placental membrane N-glycome.
- To analyze glycosylation changes in specific growth-related membrane receptors (Insulin Receptor and IGF1R) in IUGR placentas.
Main Methods:
- Analysis of the N-glycome of placental membranes from preeclampsia with IUGR pregnancies.
- Quantification and structural analysis of N-glycans.
- Investigation of glycosylation on isolated Insulin Receptor (IR) and Insulin-like Growth Factor 1 Receptor (IGF1R) from placental membranes.
Main Results:
- Preeclampsia with IUGR significantly altered placental N-glycans, characterized by reduced fucosylation and increased paucimannosidic/mannosidic structures.
- The Insulin Receptor (IR) in IUGR placentas showed a significant decrease in α2,6-Sialic acid (Sia) compared to controls.
- No significant glycosylation difference was observed in the homologous IGF1R between groups.
Conclusions:
- Placental membrane glycosylation is significantly altered in preeclampsia with IUGR.
- Changes in the overall N-glycome may not reflect alterations in specific glycoproteins.
- Direct analysis of target glycoproteins, such as the Insulin Receptor, is essential, as general assumptions about glycosylation changes are not applicable.
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