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 linked β-N-acetylglucosamine (GlcNAc), or GlcNAcylation. This is a reversible post-translational modification on nuclear and cytoplasmic proteins, mainly controlled by GlcNAc transferase (OGT) and GlcNAcase (OGA). GlcNAcylation has been implicated as a modulator of proteins, both in physiological and pathological conditions and, more recently, -GlcNAc has also been shown to be an important modulator in placental tissue. In this mini-review, the interplay between GlcNAcylation of proteins and placental function will be addressed, discussing the possible implications of this post-translational modification through placental development and pregnancy.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6160872 | PMC |
http://dx.doi.org/10.3389/fphys.2018.01263 | DOI Listing |
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!