Progesterone-regulated B4galnt2 expression is a requirement for embryo implantation in mice

Li, Pei-Tzu; Liao, Chi-Jr; Wu, Wen‐guey; Yu, Lung-Chi; Chu, Shih‐I

doi:10.1016/j.fertnstert.2011.03.043

Cited by 11 publications

(12 citation statements)

References 27 publications

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“…The expression of HAS-1 and HAS-2 was inhibited by progesterone treatment whereas HAS-3 was substantially increased [87]. Chu and coworkers showed that the progesterone regulated expression of the gene for a specific β1-4 N-acetylgalactosaminyltransferase (B4GALNT2) was required from the time of embryo implantation in mice [88]. Administration of tamoxifen (an estrogen receptor α antagonist) to pregnant mice on d15 resulted in reduce hyaluronan synthase 2 (HAS-2) gene expression in the cervix as quantified by qPCR.…”

Section: Introductionmentioning

confidence: 99%

Functional glycosylation in the human and mammalian uterus

Clark

2015

Fertil Res and Pract

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BackgroundGlycosylation is the most common and structurally diverse of all the post-translational modifications of proteins. Lipids and extracellular matrices are also often glycosylated. The mammalian uterus is highly enriched in glycoconjugates that are associated with the apical surfaces of epithelial cells and the secretions released by both epithelial and stromal cells. These glycoconjugates interact primarily with sperm, the implanting embryo, the fetus, and any pathogen that happens to gain entry into the uterus. Secretions of the endometrial glands increase substantially during the luteal phase of the menstrual cycle. These secretions are highly enriched in glycoproteins and mucins that promote specific uterine functions.FindingsLectins and antibodies have been employed in the majority of the studies focused on uterine glycosylation have employed to define the expression of carbohydrate sequences. However, while these studies provide insight about potential glycosylation, precise information about glycan structure is lacking. Direct sequencing studies that employ biochemical or mass spectrometric methods are far more definitive, but have rarely been employed with uterine glycoproteins. Both lectin/antibody binding and direct carbohydrate sequencing studies that have been focused on the mammalian uterus are reviewed. The primary functional role of the eutherian uterus is to facilitate fertilization and nurture the developing embryo/fetus. Trophoblasts are the primary cells that mediate the binding of the embryo and placenta to the uterine lining. In mammals that utilize hemochorial placentation, they invade the decidua, the specialized endometrial lining that forms during pregnancy. Trophoblasts have also been analyzed for their lectin/antibody binding as a complement to the analysis of the uterine cells and tissues. They will also be reviewed here.ConclusionsThe functional roles of the glycans linked to uterine and trophoblast glycoconjugates remain enigmatic. Another major question in the human is whether defects in placental or uterine glycosylation play a role in the development the Great Obstetrical Syndromes. More recent findings indicate that changes in glycosylation occur in trophoblasts obtained from patients that develop preeclampsia and preterm birth. The functional significance of these changes remain to be defined. Whether such shifts happen during the development of other types of obstetrical syndromes remains to be determined.

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Section: Introductionmentioning

confidence: 99%

Functional glycosylation in the human and mammalian uterus

Clark

2015

Fertil Res and Pract

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“…2A). There appears to be no RNA for b4galnt2 in the uterus at E0.5, E6.5, E15.5, and E18.5; this coincided with the P-induced gene expression during pregnancy in our previous findings (11). To investigate the protein localization in uterine tissue, uterine tissue was harvested from mice at different time points during pregnancy (including E0.5, E3.5, E10.5, and E18.5).…”

Section: Western Blot Analysis Of Membrane and Cytosolic Proteins Fromentioning

confidence: 69%

“…At present, we postulate that B4GALNT2 participates in embryo implantation. We propose that P induces B4GALNT2 expression during pregnancy (11) and triggers the post-translational modification required to provide Sd a -conjugated molecules in the uterine epithelium and in the blastocyst. We believe that B4GALNT2 expressed in the blastocyst serves as a plasma membrane receptor to mediate embryo implantation via ligand-receptor interaction and provides the Sd a antigen as a ligand for the acceptor on the endometrial epithelial cells (Supplemental Fig.…”

Section: Figurementioning

confidence: 99%

“…In mice, uterine implantation of the blastocyst takes places on day 3.5/4.5 of pregnancy (E3.5/E4.5) (3). Our previous work showed that the knockdown of b4galnt2 expression decreases implantation rates (11). This finding suggests that b4galnt2 expression plays a critical role in the interactions between the embryo and the uterine surface, leading to embryonic implantation at E3.5/ E4.5.…”

mentioning

confidence: 95%

“…In the uterus, B4GALNT2 is up-regulated by P and down-regulated by estrogen (11). P is essential for the endometrial receptivity required for blastocyst implantation and embryonic development; in particular, P induces the uterine endometrium to transform into a suitable uterine environment conducive to embryo attachment (12).…”

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confidence: 99%

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