Glycoanalysis of the placental membrane glycoproteins throughout placental development.

Abstract:

:Structural changes of glycans are observed in different (patho)physiological conditions. Human placental membrane (glyco)proteins were isolated from the first and third trimester placentas of mothers at different ages. By using lectin microarray, we demonstrated that the placental membrane N-glycome contains several N-glycan groups: high mannose, asialylated and sialylated biantennary moieties, bisected, core fucosylated, fucosylated at other positions (bearing terminal and/or antennary Fuc), α2-6 and α2-3 sialylated structures. Employing MALDI-TOF MS enabled identification of over sixty different N-glycan structures in all samples, with 17 moieties exceeding the relative abundance of 2%. The major MS peaks originated from: 1) biantennary complex type N-glycan with a bisecting GlcNAc residue and 2) a core Fuc paucimannosidic and high mannose type structures M3-M9. Age of mothers and the stage of placental development affected N-glycome. The work presented in this article is the first comprehensive mass spectrometric study of the N-glycome of human placental membrane proteins. Our results may be seen as the baseline which can serve for future MALDI MS profiling of the placental membrane N-glycome in different pathophysiological conditions.

journal_name

Mech Ageing Dev

authors

Robajac D,Masnikosa R,Nemčovič M,Križáková M,Belická Kluková Ľ,Baráth P,Katrlík J,Nedić O

doi

10.1016/j.mad.2019.111151

subject

Has Abstract

pub_date

2019-10-01 00:00:00

pages

111151

eissn

0047-6374

issn

1872-6216

pii

S0047-6374(19)30156-3

journal_volume

183

pub_type

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