Abstract
Successful placentation is a key event for fetal development, which commences following embryo implantation into the uterine wall, eliciting decidualization, placentation, and remodeling of blood vessels to provide physiological exchange between embryo-fetus and mother. Several signaling pathways are recruited to modulate such important processes and specific proteins that regulate placental function are a target for the glycosylation with O-linked β-N-acetylglucosamine (O-GlcNAc), or O-GlcNAcylation. This is a reversible post-translational modification on nuclear and cytoplasmic proteins, mainly controlled by O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). O-GlcNAcylation has been implicated as a modulator of proteins, both in physiological and pathological conditions and, more recently, O-GlcNAc has also been shown to be an important modulator in placental tissue. In this mini-review, the interplay between O-GlcNAcylation of proteins and placental function will be addressed, discussing the possible implications of this post-translational modification through placental development and pregnancy.
Highlights
The hemochorial placenta allows blood coming from the maternal circulation to directly contact the fetal chorion, favoring nutrient exchange to the embryo and fetus (Croy et al, 2009)
OGA and O-GlcNAc transferase (OGT) are extensively expressed in placentas (Lubas et al, 1997; Gao et al, 2001) and several proteins that play important roles in placental function are targets for O-GlcNAcylation
It was demonstrated that the histone variant H2A is a target for O-GlcNAc at Ser40, and this post-translational modification is required for H2A to contribute to the trophoblast stem cell differentiation process, being correlated with the evolution of placental tissue (Hirosawa et al, 2016)
Summary
The hemochorial placenta allows blood coming from the maternal circulation to directly contact the fetal chorion, favoring nutrient exchange to the embryo and fetus (Croy et al, 2009). OGA and OGT are extensively expressed in placentas (Lubas et al, 1997; Gao et al, 2001) and several proteins that play important roles in placental function are targets for O-GlcNAcylation. Inhibition of OGT was able to partially restore cell proliferation and blastocyst formation under hyperglycemic conditions, suggesting that dysregulation of both HBP and O-GlcNAcylation may favor embryotoxic effects during pre-implantation development (Pantaleon et al, 2010).
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