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Human Reproduction, Vol. 8, No. 3, pp. 475-484, 1993
© 1993 European Society of Human Reproduction and Embryology


other

Expression of integrins by human trophoblast and differential adhesion to laminin or fibronectin

Tanya D. Burrows1, Ashley King and Y.W. Loke

Research Group in Human Reproductive Immunobiology, Department of Pathology, University of Cambridge Tennis Court Road, Cambridge CB2 1QP, UK

Correspondence: 1To whom correspondence should be addressed

The process of placental implantation involves a series of transformations of trophoblast from a single polarized epithelial layer resting on a basement membrane (villous trophoblast), to cellular aggregates (trophoblast columns) which ultimately disperse to invade uterine decidua as individual cells (interstitial trophoblast). Such tissue re-modelling is associated with changes in the constituents of the extracellular matrix and in the expression of matrix receptors by the cells, the most relevant being the family of integrins which bind to laminin and fibronectin. In this study we show, by immunohistology and flow cytometry, a gradual loss of laminin receptors with the concomitant acquisition of fibronectin receptors as trophoblast is transformed from the villous phenotype, through the cell columns, into the extravillous population. The pattern of staining for the {alpha}5, {alpha}6, {beta}1 and {beta}4 subunits indicates that the integrins expressed by trophoblast are predominantly the {alpha}5{beta}1 and the {alpha}6{beta}4 heterodimers. We have also shown that isolated trophoblast cells assume a flattened, sessile phenotype when cultured on laminin but exhibit a more spreading, motile morphology when plated on fibronectin. In addition, numerous multinucleated giant cells are observed on a fibronectin substrate. Our data suggest that the relative expression of laminin and fibronectin receptors may determine the morphology and behaviour of trophoblast during the process of implantation.

Key words: fibronectin/implantation/integrin/laminin/trophoblast


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