Differentiaton of Human Cytotrophoblast into Syncytiotrophoblast in Culture

Kliman, Harvey J.; Feinman, Michael; StraussIII, Jerome F.

doi:10.1007/978-1-4757-1936-9_29

Cellular Biology and Pharmacology of the Placenta 1987

DOI: 10.1007/978-1-4757-1936-9_29

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Differentiaton of Human Cytotrophoblast into Syncytiotrophoblast in Culture

Harvey J. Kliman

Michael Feinman

Jerome F. StraussIII

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Cited by 23 publications

(29 citation statements)

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“…The major barrier to exchange, and the site of transport of most solutes between the mother and fetus in the placenta, is the syncytiotrophoblast cell layer. This is a multinucleate epithelium which is formed by differentiation and fusion of stem cytotrophoblast cells (Kaufmann & Scheffen, 1992), a process which is coupled to increasing expression of human chorionic gonadotrophin (hCG) and expression of human placental lactogen (hPL) on terminal differentiation (Kliman, Feinman & Strauss, 1987). Although these morphological and hormonal changes during the differentiation process have been well characterized, few studies have investigated whether changes in transporter activity and expression also occur.…”

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“…Cytotrophoblast cells, isolated from human term placenta, exhibit at least two stages of differentiation similar to those occurring in vivo. Early in culture (less than 24 h) they are mononucleate and produce little hCG, whereas later in culture (over 48 h) they are multinucleate, reminiscent of the in vivo syncytiotrophoblast, and produce significant quantities of hCG and hPL (Kliman et al 1987). Recent data suggest that the activity of the methyl a-aminoisobutyric acid (meAIB)-insensitive Nae-dependent amino that there are changes in expression at the acid transporter (Furesz, Smith & Moe, 1993) and the number of iron-transporting transferrin receptors (Kennedy, Douglas & King, 1992) are different at these two stages of cytotrophoblast cell differentiation.…”

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confidence: 99%

“…Na+-K+-ATPase activity is most probably a key determinant of electrochemical gradients across the mature syncytiotrophoblast. Furthermore, changes in activity and expression of Na+-K+-ATPase are frequently associated with differentiation in a number of other cell types (Ladoux, Abita & Geny, 1986;Larsson, Aperia & Lechene, 1988;Russo, Manuli, Ismail-Beigi, Sweadner & Edelman, 1990;Burke, Jaffe & Brzeski, 1991;Wilson-Hammerton, Krezeminski, Mays, Ryan, Wollner & Nelson, 1991 (Kliman et al 1987;. Therefore, for comparison, a dividing, choriocarcinoma-derived cell line (JAr) was also studied.…”

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confidence: 99%

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Activity and expression of Na(+)‐K(+)‐ATPase in human placental cytotrophoblast cells in culture.

Clarson

Glazier

Greenwood

et al. 1996

The Journal of Physiology

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1. To determine whether there is a change during differentiation, the activity and expression of Na(+)‐K(+)‐ATPase were studied in mononucleate cytotrophoblast cells (18 h culture) and syncytiotrophoblast‐like cells (66 h culture). A choriocarcinoma‐derived cell line (JAr) which, unlike the cytotrophoblast cells, divides in culture, was also studied for comparison. 2. Na(+)‐K(+)‐ATPase activity was assessed by measurement of ouabain‐sensitive 86Rb+ uptake. Na(+)‐K(+)‐ATPase expression was determined by (i) measurement of [3H]ouabain binding and (ii) Northern hybridization to measure expression of alpha‐1 and beta 1‐subunit mRNA. 3. There was no significant difference in either activity or expression of Na(+)‐K(+)‐ATPase during differentiation of cytotrophoblast cells. However, expression of alpha 1‐ and beta 1‐subunit mRNA was significantly lower in 66 vs. 18 h cultured cytotrophoblast cells. 4. Both Na(+)‐K(+)‐ATPase activity and [3H]ouabain binding was significantly greater in JAr cells than either cytotrophoblast cell groups, although expression of alpha 1‐ and beta 1‐subunit mRNA was the same as cytotrophoblast cells cultured for 18 h. 5. It is concluded that N(+)‐K(+)‐ATPase activity and protein expression does not change during differentiation of cytotrophoblast cells but that there are changes in expression at the transcriptional or post‐transcriptional level.

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Activity and expression of Na(+)‐K(+)‐ATPase in human placental cytotrophoblast cells in culture.

Clarson

Glazier

Greenwood

et al. 1996

The Journal of Physiology

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“…Once isolated from the placental villi, these mononuclear cells undergo morphologic as well as biochemical differentiation in vitro. Cytotrophoblasts form multinucleated syncytia and carry out de novo secretion of human chorionic gonadotropin (hCG), human placental lactogen, and progesterone (2)(3)(4). During this differentiation process cytotrophoblasts also attach to ECM proteins (5) and synthesize fibronectin (6) and laminin (7).…”

mentioning

confidence: 99%

Human trophoblast-extracellular matrix (ECM) interactions in vitro: ECM thickness modulates morphology and proteolytic activity.

Kliman

Feinberg

1990

Proc. Natl. Acad. Sci. U.S.A.

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Trophoblast invasion of the uterine extracellular matrix, a critical process for human implantation and uteroplacental vascular development, is a striking example of controlled invasiveness. To examine cellular behavior relevant to this process, human trophoblasts were cultured on (a) Millicell filters prelayered with Matrigel and (it) coverslips precoated with a gentle slope of Matrigel (Matribeach). Histologic sections of the Millicell system demonstrated significant invasion. However, on Matribeach the cells exhibited markedly different characteristics depending on the thickness of the Matrigel. On zone 1 (1-4 ,um thick), flat aggregates and syncytia were seen. In contrast, cells on zone 2 (4-14 pzm) formed rounded aggregates with intercellular processes. In this zone, prominent degradation of pericellular Matrigel proteins was assessed by both light microscopy and scanning electron microscopy. Treatment with 8-bromo-cAMP inhibited this proteolytic process. On zone 3 (14-60 pmm), unicellular trophoblasts or small aggregates caused minimal matrix degradation. JEG-3 human choriocarcinoma cells exhibited similar morphologic and degradative properties on Matribeach, but zone 2 proteolysis was not affected by 8-bromo-cAMP. Our results suggest that extracellular matrix thickness has profound effects on cellular morphology and proteolytic activity. Furthermore, while both normal and malignant human trophoblasts can degrade extracellular matrix proteins, only normal trophoblast extracellular matrix degradation is inhibited by 8-bromo-cAMP.During human gestation, trophoblasts invade the uterine extracellular matrix (ECM), remodel the maternal vasculature, and line vascular channels in the placental bed (1). The biological repertoire necessary for these unique trophoblast-ECM interactions is unknown. Although trophoblast behavior has been compared to that of tumor cells with invasive activity, trophoblasts generally exhibit tightly regulated growth and invasion in vivo.Certain features of cytotrophoblast differentiation in vivo can be recapitulated in vitro when human cytotrophoblasts are purified and cultured from term placentae (2). Once isolated from the placental villi, these mononuclear cells undergo morphologic as well as biochemical differentiation in vitro. Cytotrophoblasts form multinucleated syncytia and carry out de novo secretion of human chorionic gonadotropin (hCG), human placental lactogen, and progesterone (2-4). During this differentiation process cytotrophoblasts also attach to ECM proteins (5) and synthesize fibronectin (6) and laminin (7). Urokinase-type plasminogen activator (u-PA) is secreted by cytotrophoblasts in culture (8), as are the plasminogen activator inhibitor (PAI) types 1 and 2 (9). cAMP has profound effects on cytotrophoblasts in culture by affecting their intracellular morphology and synthesis of hCG, fibronectin, and u-PA (4,6,8).Since cytotrophoblasts in culture are capable of exhibiting multiple facets of the trophoblast differentiation process, we wished to determine whet...

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“…Term placental trophoblasts were separated on a Percoll gradient (Kliman et al, 1987). Cultures used for IFN induction were composed of 97 % trophoblasts, with fibroblasts and macrophages in roughly equal amounts.…”

mentioning

confidence: 99%

Purification and Initial Characterization of Human Placental Trophoblast Interferon Induced by Polyriboinosinic {middle dot} Polyribocytidylic Acid

Aboagye-Mathiesen

Tóth

Juhl

et al. 1990

Journal of General Virology

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Differentiaton of Human Cytotrophoblast into Syncytiotrophoblast in Culture

Cited by 23 publications

References 10 publications

Activity and expression of Na(+)‐K(+)‐ATPase in human placental cytotrophoblast cells in culture.

Activity and expression of Na(+)‐K(+)‐ATPase in human placental cytotrophoblast cells in culture.

Human trophoblast-extracellular matrix (ECM) interactions in vitro: ECM thickness modulates morphology and proteolytic activity.

Purification and Initial Characterization of Human Placental Trophoblast Interferon Induced by Polyriboinosinic {middle dot} Polyribocytidylic Acid

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