Human trophoblast adhesion to matrix proteins: inhibition and signal transduction |
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Authors: | Burrows, Tanya Dee King, Ashley Smith, S.K. Loke, Y.W. |
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Affiliation: | 1Research Group in Human Reproductive Immunobiology Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP 2Department of Obstetrics and Gynaecology University of Cambridge, Rosie Maternity Hospital, Robinson Way, Cambridge CB2 2SW, UK |
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Abstract: | At the time of implantation, the extracellular matrix proteinslaminin and fibronectin are abundant in the decidua and aredistributed pericellularly around each individual stromal cell.First trimester human trophoblast expresses both laminin andfibronectin receptors, specifically the 1ß1 5ß1 6ß1 and 6ß4 integrin heterodimers. In thisstudy we have demonstrated that in-vitro adhesion of first trimesterhuman trophoblast to purified extracellular matrix proteinsand to purified decidual stromal cell monolayers can be inhibitedby monoclonal antibodies directed against appropriate integrinsubunits and by synthetic peptides containing an arginine-glycine-asparticacid sequence. Monoclonal antibodies (mAbs) to the 5 and ß1integrin subunits and a synthetic peptide significantly inhibitedadhesion to fibronectin. Binding of trophoblast to laminin wasblocked with mAbs to the 6 and ß1 but not 1 and ß4integrinsubunits. Similarly, integrin-mediated adhesion to monolayersof decidual stromal cells could be blocked with mAbs to the 5, 6, ß6 and ß4 integrin subunits. Integrin-mediatedsignal transduction in normal and malignant trophoblast wasinvestigated by Western blotting. A 115 kDa protein was themajor tyrosine phosphorylated protein detected in trophoblastafter binding to laminin or fibronectin. The profile of tyrosinephosphorylated proteins differed for malignant trophoblast. integrins/matrix/signal transduction/trophoblast |
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