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Received April 25, 2005
Revised May 6, 2005
Accepted after revision May 6, 2005
1 Université du Québec é Montréal
2 Universitéde Monréal
* To whom correspondence should be addressed. E-mail: lafond.julie{at}uqam.ca.
Mitogen-activated protein kinases (MAPKs) control many cellular events from complex programs, such as embryogenesis, cell differentiation and proliferation, and cell death, to short-term changes required for homeostasis and acute hormonal responses. However, little is known about expression and activation of classical MAPKs, extracellular signal-regulated kinase1/2 (ERK1/2) and p38 in human placenta. Therefore, we examined the expression of ERK1/2 and p38 in trophoblasts from human term placenta and their implication in differentiation. In vitro, freshly isolated cytotrophoblast cells, cultivated in 10% fetal bovine serum (FBS), spontaneously aggregate and fuse to form multinucleated cells that resemble phenotypically to mature syncytiotrophoblasts, that concomitantly produce human chorionic gonadotropin (hCG) and human placental lactogen (hPL). This study shows that the level of ERK1/2 and p38 decreases along the days of culture to reach an undetectable level after 5 days of culture. Moreover, cells pre-treatment with an ERK1/2 specific inhibitor (PD98059) and/or a p38 specific inhibitor (SB203580) suppressed trophoblasts differentiation. Our results also demonstrated that p38 pathway is highly solicited as compared to ERK1/2 pathway in the differentiation process. Furthermore, ERK1/2 and p38 are rapidly activated upon addition of FBS, but the activation of p38 is delayed compared to ERK1/2. In summary, this study showed that ERK1/2 and p38 pathways are essential to mediate initiation of trophoblasts differentiation.
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