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binding protein-4, insulin-like growth factor binding protein-6 and placental growth factor expression in human breast cancer cells. The urokinase receptor (uPAR) is a transmembrane glycoprotein originally identified as a high-affinity binding site for urokinase-type plasminogen activator (uPA). It is present in a wide variety of normal cell types and tissues including proliferating and migrating cells,
which suggests that it could also be an important component for other cell functions. Here we report the expression of uPAR mRNA and protein in a panel of well characterized human breast cancer cell lines and in primary cultures of human breast cancer cells derived from tumor biopsy specimens and also in the human breast carcinoma cell line MDA-MB-231. uPAR protein was visualized byimmunofluorescence microscopy as cytosolic and/or membrane-associated clusters. Two-dimensional immunoelectricpH focusing followed by specific immunoblotting of the separated protein spots revealed distinct uPAR isoforms. In each cell type, uPAR expression was shown to be regulated at the transcriptional as well as the translational level. uPAR regulated the expression of its three best
characterized ligands, the plasminogen activator inhibitor type 1 (PAI-1), tissue-type plasminogen activator (tPA) and insulin-like growth factor binding protein-4 (IGFBP-4). For PAI-1 and tPA, upregulation was observed in response to uPAR expression as well as the presence of uPAR in the cell membrane. In contrast, IGFBP-4 expression was consistently reduced in response to uPAR expression.
The importance of this effect was underscored by the finding that uPAR-mediated IGFBP-4 downregulation inhibited the IGFBP-4-mediated autocrine loop of growth, migration and invasion in these cells. In summary, these data reveal that uPAR is an important regulator of IGFBP-4 expression in breast carcinoma cells, and may therefore contribute f678ea9f9e
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