The vitronectin receptor plays a role in the adhesion of human cytotrophoblast cells to endothelial cells

Twanda L. Thirkill, Gordon C Douglas

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

During placental development in higher primates trophoblast cells invade maternal blood vessels and migrate along the luminal surface of endothelium. In the present study, the adherence of human cytotrophoblast cells to endothelial cells has been characterized to test the hypothesis that vitronectin receptors (αv integrins) play a role in intra-luminal trophoblast migration. Adherence was measured using a quantitative fluorescence-based assay and was found to increase in a time-dependent fashion up to about 2 h after which it leveled off. Adhesion was detectable at 4°C but was greatly reduced compared to that seen at 37°C. Adhesion was partially blocked by antibodies against αvβ3/β5 integrin, β1 integrin and by antibodies against P-selectin. Antibodies against β3 integrin subunits had no effect. Adhesion was reduced by galactose-6-phosphate and fructose-6-phosphate. Flow cytometric analysis revealed αv integrin on the surface of cytotrophoblast and endothelial cells. β1 Integrin was detected on the surface of endothelial cells and on cytokine stimulated cytotrophoblast cells. β3 and β5 integrins were not detected on the surface of either cell type, although β3 was detected using permeabilized endothelial cells. These results raise the possibility that αv integrins expressed by both cytotrophoblast cells and endothelial cells, and P-selectin expressed by endothelial cells, may be important in facilitating trophoblast adhesion and migration along the uterine microvasculature.

Original languageEnglish (US)
Pages (from-to)277-290
Number of pages14
JournalEndothelium: Journal of Endothelial Cell Research
Volume6
Issue number4
StatePublished - 1999

Fingerprint

Integrin alphaVbeta3
Trophoblasts
Integrins
Endothelial Cells
P-Selectin
Vitronectin Receptors
Antibodies
Placentation
Microvessels
Primates
Endothelium
Blood Vessels
Fluorescence
Mothers
Cytokines

Keywords

  • Adhesion
  • Cytotrophoblast
  • Endothelium
  • Integrins
  • Placenta
  • Vitronectin receptor

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

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abstract = "During placental development in higher primates trophoblast cells invade maternal blood vessels and migrate along the luminal surface of endothelium. In the present study, the adherence of human cytotrophoblast cells to endothelial cells has been characterized to test the hypothesis that vitronectin receptors (αv integrins) play a role in intra-luminal trophoblast migration. Adherence was measured using a quantitative fluorescence-based assay and was found to increase in a time-dependent fashion up to about 2 h after which it leveled off. Adhesion was detectable at 4°C but was greatly reduced compared to that seen at 37°C. Adhesion was partially blocked by antibodies against αvβ3/β5 integrin, β1 integrin and by antibodies against P-selectin. Antibodies against β3 integrin subunits had no effect. Adhesion was reduced by galactose-6-phosphate and fructose-6-phosphate. Flow cytometric analysis revealed αv integrin on the surface of cytotrophoblast and endothelial cells. β1 Integrin was detected on the surface of endothelial cells and on cytokine stimulated cytotrophoblast cells. β3 and β5 integrins were not detected on the surface of either cell type, although β3 was detected using permeabilized endothelial cells. These results raise the possibility that αv integrins expressed by both cytotrophoblast cells and endothelial cells, and P-selectin expressed by endothelial cells, may be important in facilitating trophoblast adhesion and migration along the uterine microvasculature.",
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AU - Thirkill, Twanda L.

AU - Douglas, Gordon C

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N2 - During placental development in higher primates trophoblast cells invade maternal blood vessels and migrate along the luminal surface of endothelium. In the present study, the adherence of human cytotrophoblast cells to endothelial cells has been characterized to test the hypothesis that vitronectin receptors (αv integrins) play a role in intra-luminal trophoblast migration. Adherence was measured using a quantitative fluorescence-based assay and was found to increase in a time-dependent fashion up to about 2 h after which it leveled off. Adhesion was detectable at 4°C but was greatly reduced compared to that seen at 37°C. Adhesion was partially blocked by antibodies against αvβ3/β5 integrin, β1 integrin and by antibodies against P-selectin. Antibodies against β3 integrin subunits had no effect. Adhesion was reduced by galactose-6-phosphate and fructose-6-phosphate. Flow cytometric analysis revealed αv integrin on the surface of cytotrophoblast and endothelial cells. β1 Integrin was detected on the surface of endothelial cells and on cytokine stimulated cytotrophoblast cells. β3 and β5 integrins were not detected on the surface of either cell type, although β3 was detected using permeabilized endothelial cells. These results raise the possibility that αv integrins expressed by both cytotrophoblast cells and endothelial cells, and P-selectin expressed by endothelial cells, may be important in facilitating trophoblast adhesion and migration along the uterine microvasculature.

AB - During placental development in higher primates trophoblast cells invade maternal blood vessels and migrate along the luminal surface of endothelium. In the present study, the adherence of human cytotrophoblast cells to endothelial cells has been characterized to test the hypothesis that vitronectin receptors (αv integrins) play a role in intra-luminal trophoblast migration. Adherence was measured using a quantitative fluorescence-based assay and was found to increase in a time-dependent fashion up to about 2 h after which it leveled off. Adhesion was detectable at 4°C but was greatly reduced compared to that seen at 37°C. Adhesion was partially blocked by antibodies against αvβ3/β5 integrin, β1 integrin and by antibodies against P-selectin. Antibodies against β3 integrin subunits had no effect. Adhesion was reduced by galactose-6-phosphate and fructose-6-phosphate. Flow cytometric analysis revealed αv integrin on the surface of cytotrophoblast and endothelial cells. β1 Integrin was detected on the surface of endothelial cells and on cytokine stimulated cytotrophoblast cells. β3 and β5 integrins were not detected on the surface of either cell type, although β3 was detected using permeabilized endothelial cells. These results raise the possibility that αv integrins expressed by both cytotrophoblast cells and endothelial cells, and P-selectin expressed by endothelial cells, may be important in facilitating trophoblast adhesion and migration along the uterine microvasculature.

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