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Trophoblast giant cell differentiation is characterized by endoreduplication and expression of members of the prolactin (PRL) gene family and can be simulated in vitro via manipulations of the Rcho-1 trophoblast cell line. The regulation of trophoblast cell proliferation and differentiation involves tyrosine protein kinase signaling pathways. Treatment of Rcho-1 trophoblast cells with tyrosine kinase inhibitors disrupted differentiation-dependent expression of members of the PRL gene family and cytoskeletal organization. Activated p60c-src, p62c-yes, and p53/56lyn were present in the Rcho-1 rat trophoblast cell line and in differentiated trophoblast cells isolated from the developing rat placenta. p60c-src and p62c-yes were active in proliferating and differentiating trophoblast cells. During proliferation, p62c-yes exhibited distinct associations with other phosphoproteins (34, 66, 76, and 150 kDa). p53/56lyn was activated only in differentiating trophoblast cells. p53/56lyn showed a differentiation-dependent accumulation in cytoskeletal and membrane fractions, whereas p60c-src levels were virtually invariant in both fractions. Expression patterns of csk, a negative regulator of Src family kinase activities, were not consistent with its involvement in the differentiation-dependent activation of p53/56lyn; however, there was some indication of the participation of a tyrosine phosphatase in the regulation of p53/56lyn. In conclusion, p60c-src, p62c-yes, and p53/56lyn patterns of activation in trophoblast cells are consistent with their involvement in the control of trophoblast cell proliferation and differentiation.

Signaling Pathways Controlling Trophoblast Cell Differentiation: Src Family Protein Tyrosine Kinases in the Rat1