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Prostaglandin E 2 receptor modulation affects tumor cell adhesion to laminin
Author(s) -
Zhang ShaoZeng,
Fulton Amy M.
Publication year - 1991
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041490206
Subject(s) - laminin , receptor , prostaglandin e , cell adhesion , prostaglandin e2 receptor , chemistry , prostaglandin , microbiology and biotechnology , cancer research , endocrinology , cell , biology , medicine , biochemistry , agonist
We have shown previously that murine mammary adenocarcinoma cells both synthesize prostaglandin E 2 (PGE 2 ) and have a high affinity receptor for this ligand. Modulation of either PGE synthesis or PGE receptor function changes the metastatic potential of these cells. Because of the importance of laminin and laminin receptors to the metastatic process, we asked whether or not the PGE receptor participates in tumor cell‐laminin interactions. As has been reported for many other tumor cells, laminin and the laminin‐derived peptide PA22‐2, containing the sequence IKVAV, mediate attachment of line 410.4 mammary tumor cells in vitro. We now demonstrate that the attachment of 410.4 cells to laminin or peptide PA22‐2 was significantly inhibited by three PGE receptor antagonists, LE0101, SC19220, and sodium meclofenamate. LE0101 was most active, inhibiting tumor cell adhesion in a dose‐dependent manner in the absence of nonspecific toxicity. These receptor antagonists had no effect on the PA22‐2‐mediated attachment of a PGE receptor negative tumor cell line, except at the highest concentration of LE0101 tested. No inhibition of adhesion to Type I collagen was seen. These results indicate that the PGE 2 receptor modulates tumor cell adhesion to laminin which may subsequently affect the in vivo process of metastasis.