8-Bromo-3′5′ -Adenosine Monophosphate Stimulates the Endocrine Activity of Human Cytotrophoblasts in Culture*

Feinman, Michael; Kliman, Harvey J.; Caltabiano, S; Strauss, Jerome F.

doi:10.1210/jcem-63-5-1211

Cited by 131 publications

(46 citation statements)

References 27 publications

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“…This enhanced the expression of genes representative of syncytiotrophoblast endocrine activity (Kao et al 1992). It is also reported that treatment with 8-bromo-cAMP causes cytotrophoblasts isolated from term placenta to aggregate within hours and an increase in hCG and progestin secretion in serum-supplemented medium (Feinman et al 1986). Moreover, Wice et al (1990) showed that BeWo cells underwent fusion and morphological differentiation in standard medium after treatment with effectors of cAMP metabolism.…”

Section: Discussionmentioning

confidence: 82%

“…aggregate to form syncytia, in spite of a significant increase in hCG secretion induced by 8-bromo-cAMP in a serumfree medium (Feinman et al 1986). These results suggest that the functional differentiation of trophoblast induced by 8-bromo-cAMP is not accompanied by morphological differentiation under serum-free conditions.…”

Section: Discussionmentioning

confidence: 99%

“…In human trophoblast cells, cAMP has been shown to stimulate functional differentiation: it stimulates human chorionic gonadotropin (hCG) secretion (Feinman et al 1986). Another study showed that cAMP stimulated morphological differentiation: it stimulated cell fusion or syncytiotrophoblast formation from mononuclear cytotrophoblast-like cells in a human choriocarcinoma (BeWo) cell line (Wice et al 1990).…”

Section: Introductionmentioning

confidence: 99%

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8-bromo-cyclicAMP stimulates glucose transporter-1 expression in a human choriocarcinoma cell line

Ogura¹,

Sakata²,

Okamoto³

et al. 2000

Journal of Endocrinology

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Facilitative glucose transporter-1 (GLUT1) is abundant in trophoblast cells and is responsible for glucose transport in the placenta. However, the change in GLUT expression in human placenta upon trophoblast differentiation remains to be clarified. Therefore, we first examined the localization of GLUT1 and GLUT3 using human firsttrimester chorionic villi. We found that GLUT1 and GLUT3 were mainly localized to syncytiotrophoblast and cytotrophoblast cells respectively. We analyzed whether placental GLUT1 and GLUT3 expression changes during differentiation using a human choriocarcinoma (BeWo) cell line which is known to show functional and morphological differentiation in response to cAMP in culture. Treatment of BeWo cells with 8-bromocyclicAMP (8-bromo-cAMP) increased the level of hCG secretion and induced cell fusion leading to the formation of large syncytia. Treatment of BeWo cells with 8-bromocAMP also resulted in a significant increase in glucose uptake on days 2-3 of culture. The stimulating effect of 8-bromo-cAMP on glucose uptake was concentration dependent. Northern and immunoblot analyses revealed that the levels of mRNA and protein of GLUT1, but not of GLUT3, were significantly increased by 8-bromocAMP. These findings suggest that 8-bromo-cAMP stimulates GLUT1 expression with differentiation in BeWo cells.

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Section: Discussionmentioning

confidence: 82%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

8-bromo-cyclicAMP stimulates glucose transporter-1 expression in a human choriocarcinoma cell line

Ogura¹,

Sakata²,

Okamoto³

et al. 2000

Journal of Endocrinology

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“…However, except cAMP/protein kinase A (PKA) signaling pathway, its regulatory mechanism has not been definitively characterized. Activation of the cAMP signaling increases ERVWE1 gene expression (Frendo et al 2003, Chen et al 2008 and can induce syncytia formation in primary cytotrophoblasts and human choriocarcinoma BeWo cells (Feinman et al 1986, Mi et al 2000. Activation of the cAMP/PKA signaling pathway in turn increases the expression of a transcription factor, glial cell missing factor homolog 1 (GCM1, previously called hGCMa), which binds to the upstream region of the ERVWE1 gene and then stimulates ERVWE1 gene transcription in a cellspecific manner (Yu et al 2002, Chang et al 2005.…”

Section: Introductionmentioning

confidence: 99%

CD9 regulates transcription factor GCM1 and ERVWE1 expression through the cAMP/protein kinase A signaling pathway

Muroi¹,

Sakurai²,

Hanashi³

et al. 2009

Reproduction

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ERVWE1 (SYNCYTIN-1), a membrane protein originating from the envelope gene of human endogenous retrovirus-W (HERV-W), mediates the fusion of mononucleated cytotrophoblasts into multinucleated syncytiotrophoblast. Though ERVWE1 has been characterized since its discovery, regulatory mechanisms associated with ERVWE1 expression have not been firmly established. We hypothesized that membrane protein CD9, involved in cell-cell fusion of fertilization and myogenesis, could be involved in the regulation of ERVWE1 gene expression. In this study, regulatory mechanisms of ERVWE1 expression were studied using human choriocarcinoma BeWo cells. Forskolin is an activator of adenylate cyclase, which increased CD9 and ERVWE1 expression. The increase in CD9 expression was inhibited by a protein kinase A (PKA) inhibitor, Rp-cAMPS. These results indicate that CD9 expression is regulated by the cAMP/PKA signaling pathway. Overexpression of CD9 increased expression levels of ERVWE1 as well as GCM1 (hGCMa), which is a transcription factor known to activate ERVWE1 gene transcription. However, high ERVWE1 expression induced by CD9 overexpression did not result in the increase in chorionic gonadotropin, beta polypeptide production. Moreover, CD9-induced increase in ERVWE1 and GCM1 expressions were inhibited by Rp-cAMPS. These results suggest that CD9 increases GCM1 expression via the cAMP/PKA signaling pathway, resulting in the increase in ERVWE1 expression.

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“…Progesterone can be synthesized from cholesterol by the syncytiotrophoblast (Tuckey 2005). A variety of endogenous factors such as estrogen, HCG, and cyclic AMP are known to regulate placental progesterone production (Feinman et al 1986, Rodway et al 1988, Chaudhary et al 1992. Thus, further study of the mechanism by which the hormone network controls progesterone production in placenta is a prerequisite to gain insight into the mechanism of pregnancy and parturition.…”

Section: Introductionmentioning

confidence: 99%

Corticotropin-releasing hormone inhibits progesterone production in cultured human placental trophoblasts

Yang¹,

You²,

Tang³

et al. 2006

Journal of Molecular Endocrinology

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Placental-derived corticotropin-releasing hormone (CRH) seems to play a major role in the mechanisms controlling human pregnancy and parturition. It has been suggested that CRH directly modulates the endocrine function of placental trophoblasts, including the production of estrogen, ACTH, and prostaglandin. In this study, we sought to investigate the effect of CRH, locally produced by placenta, on progesterone production. Percoll-purified placental trophoblasts were obtained from uncomplicated term pregnancies and cultured for 72 h. Progesterone concentration in culture media was measured by RIA. The mRNA transcripts encoding CYP11A1 and HSD3B1, the enzymes for progesterone synthesis, were determined by quantitative real-time reverse transcription (RT)-PCR. Results showed that CRH (10K6 mol/l) caused a significant decrease in progesterone levels in a dose-dependent manner. The CRH antagonist, a-helical CRH 9-41, at 10K5 mol/l stimulated progesterone secretion. Consistent with this thesis, CRH decreased, whereas a-helical CRH increased, the mRNA levels of CYP11A1 and HSD3B1. Since CRH has been shown to activate the phospholipase C-protein kinase C (PKC) signal pathway in placenta, we examined whether the effect of CRH on progesterone synthesis was dependent on PKC signal pathway. Treatment of cells with PKC inhibitor, Gö 6976, resulted in a significant increase in progesterone production, and exogenous CRH restored progesterone production. In conclusion, placental CRH exhibits a tonic inhibitory effect on progesterone production in a PKC-dependent fashion.

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8-Bromo-3′5′ -Adenosine Monophosphate Stimulates the Endocrine Activity of Human Cytotrophoblasts in Culture*

Cited by 131 publications

References 27 publications

8-bromo-cyclicAMP stimulates glucose transporter-1 expression in a human choriocarcinoma cell line

8-bromo-cyclicAMP stimulates glucose transporter-1 expression in a human choriocarcinoma cell line

CD9 regulates transcription factor GCM1 and ERVWE1 expression through the cAMP/protein kinase A signaling pathway

Corticotropin-releasing hormone inhibits progesterone production in cultured human placental trophoblasts

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