May 12, 2016

Prominin-1 glycosylation changes throughout early pregnancy in uterine epithelial cells under the influence of maternal ovarian hormones

Reproduction, Fertility, and Development
Samson N DowlandChristopher R Murphy


In preparation for uterine receptivity, the uterine epithelial cells (UECs) exhibit a loss of microvilli and glycocalyx and a restructuring of the actin cytoskeleton. The prominin-1 protein contains large, heavily glycosylated extracellular loops and is usually restricted to apical plasma membrane (APM) protrusions. The present study examined rat UECs during early pregnancy using immunofluorescence, western blotting and deglycosylation analyses. Ovariectomised rats were injected with oestrogen and progesterone to examine how these hormones affect prominin-1. At the time of fertilisation, prominin-1 was located diffusely in the apical domain of UECs and 147- and 120-kDa glycoforms of prominin-1 were identified, along with the 97-kDa core protein. At the time of implantation, prominin-1 concentrates towards the APM and densitometry revealed that the 120-kDa glycoform decreased (P<0.05), but there was an increase in the 97-kDa core protein (P<0.05). Progesterone treatment of ovariectomised rats resulted in prominin-1 becoming concentrated towards the APM. The 120-kDa glycoform was increased after oestrogen treatment (P<0.0001), whereas the 97-kDa core protein was increased after progesterone treatment (P<0.05). Endoglycosidase H a...Continue Reading

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Mentioned in this Paper

Immunofluorescence Assay
Protein Deglycosylation
Glycoform C receptor, human
Prom1 protein, mouse
Post-Translational Protein Processing

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