title: Increased adhesiveness in cultured endometrial-derived cells is related to the absence of moesin expression.
abstract: Human endometrial epithelial cells (EECs) are nonadhesive for embryos throughout most of the menstrual cycle. During the so-called implantation window, the apical plasma membrane of EECs acquire adhesive properties by undergoing a series of morphological and biochemical changes. The human endometrial-derived epithelial cell line, RL95-2, serves as an in vitro model for receptive uterine epithelium because of its high adhesiveness for trophoblast-derived cells. In contrast, the HEC-1-A cell line, which displays poor adhesive properties for trophoblast cells, is considered to be less receptive. The ezrin, radixin, and moesin protein family members, which are present underneath the apical plasma membrane, potentially act to link the cytoskeleton and membrane proteins. In the present study, we have further investigated the adhesive features in these two unrelated endometrial-derived cell lines using an established in vitro model for embryonic adhesion. We have also analyzed the protein pattern and mRNA expression of ezrin and moesin in RL95-2 cells versus HEC-1-A cells. The results demonstrate that RL95-2 cells were indeed more receptive (81% blastocyst adhesion) compared with HEC-1-A cells (46% blastocyst adhesion). An intermediate adhesion rate was found in primary EECs cultured on extracellular matrix gel, thus allowing a partial polarization of these cells (67% blastocyst adhesion). Furthermore, we found that moesin was absent from RL95-2 cells. In contrast, ezrin is expressed in both cell lines, yet it is reduced in adherent RL95-2 cells. Data are in agreement with the hypothesis that uterine receptivity requires down-regulation or absence of moesin, which is a less-polarized actin cytoskeleton.
authors.affiliation: Instituto Valenciano de Infertilidad, Research Department (FIVIER), Valencia 46020, Spain.
authors.forename: J C
authors.initials: JC
authors.lastname: Martín
authors.forename: M J
authors.initials: MJ
authors.lastname: Jasper
authors.forename: D
authors.initials: D
authors.lastname: Valbuena
authors.forename: M
authors.initials: M
authors.lastname: Meseguer
authors.forename: J
authors.initials: J
authors.lastname: Remohí
authors.forename: A
authors.initials: A
authors.lastname: Pellicer
authors.forename: C
authors.initials: C
authors.lastname: Simón
mesh_terms: D000818:Animals; D002448:Cell Adhesion / Q000502:physiology; D002478:Cells, Cultured; D003598:Cytoskeletal Proteins; D003599:Cytoskeleton / Q000378:metabolism; D004622:Embryo, Mammalian / Q000166:cytology / Q000378:metabolism; D004717:Endometrium / Q000166:cytology* / Q000378:metabolism; D005260:Female; D006801:Humans; D015151:Immunoblotting; D007202:Indicators and Reagents; D051379:Mice; D008815:Mice, Inbred Strains; D008840:Microfilament Proteins / Q000096:biosynthesis*; D008856:Microscopy, Fluorescence; D009841:Oligonucleotides / Q000138:chemical synthesis; D010750:Phosphoproteins / Q000096:biosynthesis; D011233:Precipitin Tests; D012333:RNA, Messenger / Q000096:biosynthesis; D020133:Reverse Transcriptase Polymerase Chain Reaction; D000099149:Ezrin
chemical_list: D003598:Cytoskeletal Proteins; D007202:Indicators and Reagents; D008840:Microfilament Proteins; D009841:Oligonucleotides; D010750:Phosphoproteins; D012333:RNA, Messenger; D000099149:Ezrin; C071058:moesin