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Interaction of extravillous trophoblast galectin-1 and mucin(s)-Is there a functional relevance?

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TLDR
The possibility that mucins, as heavily glycosylated proteins, might be among the functionally relevant galectin ligands in human trophoblast is considered, based on both published data and original research.
Abstract
In the course of embryo implantation extensive interaction of the trophoblast with uterine tissue is crucial for adequate trophoblast invasion. This interaction is highly controlled, and it has been pointed out that a specific glycocode and changes in glycosylation may be important for successful implantation and maintenance of pregnancy. Both uterine and trophoblast cells have been shown to express cell surface glycoconjugates and sugar binding proteins, such as mucins (MUC) and galectins (gals). An increasing number of studies have investigated potential candidates interacting in this process. However, knowledge about the biochemical nature of the interactions and their importance for trophoblast cell function, and, consequently, for pregnancy outcome are still lacking. This review is aimed at deliberating the possibility that mucins, as heavily glycosylated proteins, might be among the functionally relevant galectin ligands in human trophoblast, based on both published data and our original research.

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Exploration of the regulation and control mechanisms of miR‑145 in trophoblast cell proliferation and invasion

TL;DR: The results suggest that miR-145 may serve key roles in the regulation of trophoblast cell proliferation and invasion by targeting MUC1.
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The expression and role of glycans at the feto-maternal interface in humans

TL;DR: In this article, the role of important glycan-epitopes at the feto-maternal interface in the human species is explored and some unpublished interesting results on changes of glycan residues in human placenta tissues from the first trimester of pregnancy.
References
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Journal ArticleDOI

Mucins in cancer: Protection and control of the cell surface

TL;DR: Mucins — large extracellular proteins that are heavily glycosylated with complex oligosaccharides — establish a selective molecular barrier at the epithelial surface and engage in morphogenetic signal transduction.
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Mucins in cancer: function, prognosis and therapy.

TL;DR: The findings that certain transmembrane mucins induce transformation and promote tumour progression have provided the experimental basis for demonstrating that inhibitors of their function are effective as anti-tumour agents in preclinical models.
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Episialin (MUC1) overexpression inhibits integrin-mediated cell adhesion to extracellular matrix components.

TL;DR: There is a delicate balance between adhesion and anti- adhesion forces in episialin expressing cells, which can be shifted towards adhesion by strengthening the integrin-mediated adhesion, or towards anti-adhesion by increasing the level of expression of episIALin.
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Galectins: A Family of Animal Lectins That Decipher Glycocodes

TL;DR: Crystallographic studies revealed that galectins and legume lectins such as concanavalin A have a common topology in spite of the absence of sequence homology, which suggests a possible relationship between animal and plant lectins, and the existence of a lectin super family.
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