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This Article Full Text Full Text (PDF) All Versions of this Article: 566/2/409    most recent jphysiol.2005.089326v1 Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Daoud, G. Articles by Lafond, J. Search for Related Content PubMed PubMed Citation Articles by Daoud, G. Articles by Lafond, J.

¹ Laboratoire de Physiologie materno-ftale, Département des Sciences Biologiques, Université du Québec à Montréal, Montréal, Québec, Canada, H3C 3P8
² Centre de recherche Biomed, Département des Sciences Biologiques, Université du Québec à Montréal, Montréal, Québec, Canada, H3C 3P8
³ Département d'obstétrique-gynécologie, Hôpital St-Luc, Université de Montréal, Montréal, Québec, Canada, H2L 4M1

Mitogen-activated protein kinases (MAPKs) control many cellular events from complex programmes, 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 phenotypically resemble 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 with increasing days of culture, to reach an undetectable level after 5 days of culture. Moreover, pretreatment of cells with an ERK1/2-specific inhibitor (PD98059) and/or a p38-specific inhibitor (SB203580) suppressed trophoblast differentiation. Our results also demonstrate that the p38 pathway is highly solicited as compared to the 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 that of ERK1/2. In summary, this study showed that ERK1/2 and p38 pathways are essential to mediate initiation of trophoblast differentiation.

(Received 25 April 2005; accepted after revision 6 May 2005; first published online 12 May 2005)
Corresponding author J. Lafond: Laboratoire de Physiologie materno-ftale, Université du Québec à Montréal, Département des Sciences Biologiques, C.P. 8888, Succursale Centre-ville, Montréal, Canada, H3C 3P8. Email: lafond.julie{at}uqam.ca

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