The N-glycan profile of placental membrane glycoproteins alters during gestation and aging

• Published in: Mechanisms of ageing and development 2014-06, Vol.138, p.1-9
• Main Authors: Robajac, Dragana, Masnikosa, Romana, Vanhooren, Valerie, Libert, Claude, Miković, Željko, Nedić, Olgica
• Format: Article
• Language: English
• Subjects: Adult; Aging; alpha-L-Fucosidase - metabolism; alpha-L-Fucosidase - pharmacology; Electrophoresis, Polyacrylamide Gel - methods; Female; Gestation; Gestational Age; Humans; Maternal Age; Membrane Glycoproteins - analysis; Membrane Glycoproteins - metabolism; N-glycome; Placenta - metabolism; Placental membrane; Placentation - physiology; Polysaccharides - analysis; Polysaccharides - metabolism; Pregnancy; Pregnancy Proteins - analysis; Pregnancy Proteins - metabolism; Pregnancy Trimesters - physiology; Reproducibility of Results
• ISSN: 0047-6374; 1872-6216
• DOI: 10.1016/j.mad.2014.01.010

•The first N-glycan profile of human placental membrane proteins was obtained.•DNA sequencer-assisted fluorophore-assisted carbohydrate electrophoresis was used.•Membrane N-glycans were isolated from first and third trimester placenta.•Women of different ages were included in the study.•N-glycome is dependent on placental development stage and of mother's age. Alterations in the glycosylation of few membrane proteins from human placenta during gestation have been documented, but data on N-glycome of placental membrane proteins are still missing. The primary goal of this study was to obtain N-glycan profiles of human placental membrane proteins using a reliable, simple and high-throughput method. The second goal was to examine whether the N-glycan profile alters during gestation. Placental membrane proteins were isolated from women of different ages after first and third trimesters of pregnancy. The N-glycan fingerprint of membrane proteins was obtained using DNA sequencer-assisted fluorophore-assisted carbohydrate electrophoresis (DSA-FACE). Lectin blotting was used to confirm DSA-FACE results. Observed gestation-related alterations were: greater abundance of core-fucosylated and multiantennary N-glycans, but lower amounts of bisected biantennary N-glycans together with a decrease in α2,3-sialylation. Age-related alterations were: more core Fuc and more α2,3-Sia in first trimester placentas from older women than in those from younger women; also less core Fuc and less α2,6-Sia in third trimester placentas from older women compared to those from younger women. This study represents the first N-glycan profiling of placental cell membrane proteins. These data represent a basis for future research on the N-glycome of placental proteins in different (patho)physiological conditions.