Glycoconjugate Expression and Interactions at the Cell Surface of Mouse Uterine Epithelial Cells and Periimplantation-Stage Embryo

Carson, Daniel D.; Wilson, Oswald; Dutt, Anuradha

doi:10.1007/978-1-4613-0615-3_11

Cited by 19 publications

(10 citation statements)

References 73 publications

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“…Thus, uterine stroma cultured in vitro do not provide a n effective barrier to either melanoma cell or embryo attach-ment and invasion. These observations are consistent with the suggested primary regulatory role of UEC with regard to uterine receptivity (Schlafke and Enders, 1975;Carson et al, 1990b). It is of interest that polarized UEC do not support embryo attachment in vitro since UEC grown on plastic do so readily regardless of the state of the uterus from which they are derived (Farach et al, 1987;Sherman and Salomon, 1975).…”

Section: Discussionsupporting

confidence: 87%

WGA‐binding, mucin glycoproteins protect the apical cell surface of mouse uterine epithelial cells

Valdizan

Julian

Carson

1992

Journal Cellular Physiology

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Expression of apical cell surface proteins and glycoproteins was examined in polarized primary cultures of mouse uterine epithelial cells (UEC). Lectin-gold cytochemistry revealed that wheat germ agglutinin (WGA) bound specifically to the components of the apical glycocalyx as well as intracellular vesicles. Double labeling with the pH sensitive dye 3-(2,4-dinitroanilino)-3'amino-N-methyldipropylamine (DAMP) demonstrated the acidic nature of the WGA-staining intracellular vesicles. The enzymatic and chemical sensitivities of the WGA binding sites on the apical cell surface were monitored both by WGA-gold staining as well as by 125I-WGA binding assays. In thin sections, a large fraction of these sites were removed by pronase; however, application of a wide variety of proteases, glycosidases, or chemical treatments to the apical surface of intact UEC failed to reduce WGA binding. In no case did treatments designed to remove sialic acids reduce 125I-WGA binding more than 12%. In contrast, endo-beta-galactosidase as well as a combination of beta-galactosidase with beta-hexosaminidase succeeded in removing 28% and 77% of these sites, respectively. These studies suggested that the majority of the apically disposed WGA binding sites involved N-acetylglucosamine residues rather than sialic acids and included lactosaminoglycans. Many of the proteins detected at the apical cell surface by lactoperoxidase-catalyzed radioiodination were WGA-binding glycoproteins. A major class of these glycoproteins displayed Mr > 200 kDa by SDS-PAGE and was heavily labeled metabolically by 3H-glucosamine or by vectorial labeling at the apical cell surface with galactosyl transferase and UDP-3H-galactose. Analyses of the 3H-labeled oligosaccharides labeled by either procedure indicated that a large fraction of the apically disposed WGA-binding oligosaccharides consisted of neutral, O-linked mucin-type structures with median MW of approximately 1,500. Oligosaccharides in this fraction were partially (15%) sensitive to endo-beta-galactosidase digestion and bound to Datura stramonium agglutinin (68%), demonstrating the presence of lactosaminoglycan sequences. UEC were an extremely effective barrier to attachment or invasion by either a highly invasive melanoma cell line, B16-BL6, or implantation-competent mouse blastocysts. In contrast, neither uterine stromal cells nor a non-polarizing UEC cell line, RL95, prevented B16-BL6 attachment.(ABSTRACT TRUNCATED AT 400 WORDS)

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Section: Discussionsupporting

confidence: 87%

WGA‐binding, mucin glycoproteins protect the apical cell surface of mouse uterine epithelial cells

Valdizan

Julian

Carson

1992

Journal Cellular Physiology

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“…A recent report has documented the presence of mRNAs encoding several distinct MDC proteins in Xenopus laevis testis, including an ortholog of mammalian MDC9 (Shilling et al 1997); peptides corresponding to the predicted integrin-binding sequences of three of these MDC proteins, including MDC9, inhibit fertilization in a concentration-dependent manner (Shilling et al 1997). The cell-cell binding function of ADAM proteins is relevant to the present study, since trophoblast attachment to uterine epithelium is believed to involve receptor-ligand interactions (Carson et al 1990). The integrin-binding sequence of MDC9 could serve as a ligand for integrins on the trophoblast or, in the rabbit, on adjacent epithelial cells prior to their fusion.…”

Section: Discussionmentioning

confidence: 99%

“…This attachment is thought to require receptor-ligand interactions between the plasma membrane of the trophoblast and of the uterine epithelium (Carson et al 1990). Events following the initial attachment of blastocysts to uterine epithelium differ among mammalian species and include the penetration of the trophoblast between epithelial cells (ªintrusionº), replacement by the trophoblast of detaching epithelial cells (ªdisplacementº), or a fusion of the trophoblast with uterine epithelial cells (Schlafke and Enders 1975).…”

Section: Introductionmentioning

confidence: 98%

Blastocyst-dependent upregulation of metalloproteinase/disintegrin MDC9 expression in rabbit endometrium

Olson

Winfrey

Matrisian

et al. 1998

Cell and Tissue Research

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Blastocyst attachment to mammalian uteri at implantation involves the adhesion of the trophoblast to the uterine epithelial surface. In the rabbit, fusion between adjacent epithelial cells precedes the initial attachment phase and is followed by fusion between the trophoblast and the epithelium. The reverse transcription/polymerase chain reaction method has been used to prepare a partial cDNA (rbMDC9) from periimplantation-stage endometrium; this represents the rabbit ortholog of MDC9, a member of the cellular metalloproteinase/disintegrin (ADAM) gene family. We demonstrate here the reproductive stage-specific expression of rbMDC9 mRNA in uterine epithelium during the periimplantation period. Furthermore, this expression is upregulated at implantation sites, and in situ hybridization analysis has revealed that the epithelial cells with the most prominent signal are those apposed to blastocysts. Immunostaining with E-cadherin has been used to trace lateral membranes of epithelial cells and, together with nuclear staining, has enabled the identification of cells fusing to become multinucleated cells, and later, to become an epithelial syncytium (symplasma). These fusing cells express the highest level of rbMDC9 mRNA. The results suggest that MDC9, a transmembrane modular protein with domains having potential integrin-binding, metalloproteinase, and fusogenic functions, is probably critical for the cellular interactions accompanying blastocyst implantation.

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“…Murine uterine epithelial cells exhibit characteristics that are typical of a simple epithelium, including the polar organization of surface membrane components into apical and basolateral domains. At the time of implantation, rapid changes in the epithelial cells result in flattening and a less distinctly polar organization of the cells [2,3,11,12,[14][15][16][17][18].…”

Section: Introductionmentioning

confidence: 99%

Desmosomes Are Reduced in the Mouse Uterine Luminal Epithelium During the Preimplantation Period of Pregnancy: A Mechanism for Facilitation of Implantation1

Illingworth

Kiszka

Bagley

et al. 2000

Biology of Reproduction

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Dynamic regulation of intercellular junctions is an essential aspect of many developmental, reproductive, and physiological processes. We have shown that expression of the desmosomal protein desmoplakin decreases in the luminal uterine epithelium during the preimplantation period of pregnancy in mice. By the time of implantation (between Days 4.5 and 5 of pregnancy), desmoplakin protein can barely be detected by SDS-PAGE and Western blotting, and by immunocytochemistry, it is restricted to well-spaced, punctate dots at the apicolateral junction. Using confocal XZ series and electron microscope quantitation, both the density and distribution of desmosomes along the lateral cell surfaces of luminal epithelial cells were observed to change during early pregnancy. On Day 1 of pregnancy, desmosomes were found at high density in the apicolateral junctional complex, being present here in 79% of ultrathin sections examined, whereas on Day 5, the density was much reduced (present in only 18% of ultrathin sections examined). Desmosomes were found along the lateral surfaces, at or below the level of the nucleus, in 15% of ultrathin sections examined on Day 1 of pregnancy but in only 1% on Day 5. Desmoplakin mRNA declined during the first 4-5 days of pregnancy, along with the protein, suggesting that these changes are controlled at the level of mRNA. This study shows that desmosomes are regulated during early pregnancy, and we propose that a reduction in desmosome adhesion facilitates penetration of the luminal epithelium by trophoblast cells at implantation.

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Glycoconjugate Expression and Interactions at the Cell Surface of Mouse Uterine Epithelial Cells and Periimplantation-Stage Embryo

Cited by 19 publications

References 73 publications

WGA‐binding, mucin glycoproteins protect the apical cell surface of mouse uterine epithelial cells

WGA‐binding, mucin glycoproteins protect the apical cell surface of mouse uterine epithelial cells

Blastocyst-dependent upregulation of metalloproteinase/disintegrin MDC9 expression in rabbit endometrium

Desmosomes Are Reduced in the Mouse Uterine Luminal Epithelium During the Preimplantation Period of Pregnancy: A Mechanism for Facilitation of Implantation1

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