Urokinase-receptor/integrin complexes are functionally involved in adhesion and progression of human breast cancer in vivo.

ABSTRACT: Interactions between specific cell-surface molecules, which include the urokinase receptor (uPAR) and integrins, are crucial to processes of tumor invasion and metastasis. Here we demonstrate that uPAR and beta1-integrins may cluster at distinct sites at the cell surface of metastatic MDA-MB-231 breast cancer cells and form functional complexes. Attachment assays performed in the presence of a synthetic peptide (p25), which interferes with the formation of uPAR-integrin complexes, reveal that uPAR is able to regulate the adhesive function of integrins in breast cancer cells. On dissociation of the uPAR-integrin complexes by p25, tumor cell attachment to the extracellular matrix was either decreased (vitronectin) or increased (fibronectin). Moreover, the tumor cells display remarkable morph

SUBMITTER: van der Pluijm G 

PROVIDER: S-EPMC1850470 | biostudies-literature | 2001 Sep

REPOSITORIES: biostudies-literature