Kurzfassung

The human placenta plays a major role in the formation of the maternal-fetal interface. Placenta growth involves highly complex processes like cell proliferation, migration and invasion. These processes require the up-regulation of factors normally found in early embryonal development or stem cell differentiation. Not unexpected, these proteins are often aberrantly expressed in human tumors, too. One placenta-specific protein with no detectable expression in any other normal human tissue that...The human placenta plays a major role in the formation of the maternal-fetal interface. Placenta growth involves highly complex processes like cell proliferation, migration and invasion. These processes require the up-regulation of factors normally found in early embryonal development or stem cell differentiation. Not unexpected, these proteins are often aberrantly expressed in human tumors, too. One placenta-specific protein with no detectable expression in any other normal human tissue that is highly expressed in a wide range of tumor is the trophoblast-specific gene PLAC1 (placenta-specific 1). Although the regulation of the PLAC1 gene is understood in greater detail, insights into the function of the PLAC1 protein are spares. Here we biochemically analyze PLAC1. We show that Plac1 is a dimerizing protein that is secreted from the cell and interacts with FGF7 and glycosaminoglycans within the extracellular matrix. This interaction in turn leads to the specific activation of the FGFR2IIIb receptor and enhances cell proliferation. The biochemical characterization of PLAC1 presented here thus provides the first mechanistic hint how PLAC1 promote cancer cell proliferation or regulate cell fusion event specific for syncytiotrophoblast formation in the placenta.

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