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5 Vitronectin Receptor, Promoting Urokinase-dependent Cell Migration in Breast Cancer1
National Cancer Institute [M. V. C., M. C., P. F., A. Z., G. B., G. D.], Nuclear Medicine Center (C. N. R.), University Federico II [S. D. V., M. S.], and International Institute of Genetics and Biophysics [L. F., M. P. S.], 80131 Naples, Italy
Perturbation of adhesive interactions at cell-substratum and cell-cell contact sites is a critical event in the multistep process of cancer invasion. Recent studies indicate that the urokinase receptor (uPAR) is associated in large molecular complexes with other molecules, such as integrins. To test the possibility that uPAR may physically and functionally interact with vitronectin (Vn) receptors, we determined the expression level of uPAR, 
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3, and v5 Vn receptors in 10 human breast carcinomas. Here, we show the ability of uPAR to physically associate with v5 in the breast carcinomas examined. The functional effects of this interaction were studied using HT1080 human fibrosarcoma and MCF-7 human breast carcinoma cell lines, both exhibiting a urokinase-dependent physical association between uPAR and v5. Both cell lines respond to urokinase or to its noncatalytic amino-terminal fragment by exhibiting remarkable cytoskeletal rearrangements that are mediated by v5 and require protein kinase C activity. On the contrary, binding of Vn to v5 results in the protein kinase C-independent formation of F-actin containing microspike-type structures. Furthermore, v5 is required for urokinase-directed, receptor-dependent MCF-7 and HT1080 cell migration. These data show that uPAR association with v5 leads to a functional interaction of these receptors and suggest that uPAR directs cytoskeletal rearrangements and cell migration by altering v5 signaling specificity.
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