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Department of Biological Sciences, Wayne State University, Detroit, Michigan 48202 [W. X., H. R. P.], and Department of Internal Medicine, University of Michigan Medical School, Ann Arbor, Michigan 48109 [I. M., R. F. T.]
We have shown previously that the urokinase-type plasminogen activator receptor (uPAR) physically associates with ß2 integrins on human leukocyte membranes. We now report that uPAR associates with certain members of the ß1 and ß3 integrin families expressed by a nonhematopoietic fibrosarcoma cell line (HT1080) when adherent to certain extracellular matrix molecules. Flow cytometry studies indicated that HT1080 cells expressed uPAR and ß1 and ß3 integrins. Double staining immunofluorescence was used to label uPAR and ß1 and ß3 integrins. The staining patterns of uPAR and ß1 integrins were strikingly similar when attached to fibronectin, laminin, or vitronectin but not polylysine-coated substrates. Resonance energy transfer (RET) between uPAR and ß1 integrins was observed, especially at focal adhesion plaques; this indicates that these molecules are within about 7 nm of each other on these cell membranes. uPAR and ß3 integrin coclustering and RET were also observed on tumor cells adherent to vitronectin but not to fibronectin, laminin, or polylysine-coated surfaces. Because N-acetyl-D-glucosamine was found previously to inhibit ß2 integrin-uPAR association, we tested the effect of saccharides on the ß1-uPAR and ß3-uPAR colocalization and RET. Colocalization and RET between uPAR and ß1 or ß3 integrins were effectively inhibited by N-acetyl-D-glucosamine on extracellular matrix-coated surfaces. To better define which members of ß1 and ß3 integrin families associate with uPAR, we studied the association of several 
subunits with uPAR on tumor cells. We found that: (a) 5 colocalizes with uPAR on cells attached to fibronectin-coated surfaces; (b) 5 and v colocalize with uPAR on cells adherent to vitronectin; and (c) 3 and 6 associate with uPAR on cells attached to laminin. In further support of physical associations between integrins and uPAR on tumor cells, uPAR was found to coimmunoprecipitate with ß1 integrins in Brij-58 lysates of HT1080 cells (as detected by anti-uPAR Western blotting of material isolated from an anti-ß1 integrin immunoaffinity column). Thus, uPAR may laterally associate with integrins of tumor cells when attached to specific extracellular matrix elements to enable directional proteolysis for tumor cell migration and invasion.
1 This work was supported by NIH Grant AI/CA27409 and the Research Stimulation Fund of Wayne State University (to H. R. P.) and NIH Grants CA39064 and CA42246 (to R. F. T.).
2 To whom requests for reprints should be addressed. Phone: (313) 577-2896; Fax: (313) 577-9008.
Received 9/16/96. Accepted 3/ 1/97.
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S. Hapke, H. Kessler, N. A. de Prada, A. Benge, M. Schmitt, E. Lengyel, and U. Reuning Integrin alpha vbeta 3/Vitronectin Interaction Affects Expression of the Urokinase System in Human Ovarian Cancer Cells J. Biol. Chem., July 6, 2001; 276(28): 26340 - 26348. [Abstract] [Full Text] [PDF]
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S. Mukhina, V. Stepanova, D. Traktouev, A. Poliakov, R. Beabealashvilly, Y. Gursky, M. Minashkin, A. Shevelev, and V. Tkachuk The Chemotactic Action of Urokinase on Smooth Muscle Cells Is Dependent on Its Kringle Domain. CHARACTERIZATION OF INTERACTIONS AND CONTRIBUTION TO CHEMOTAXIS J. Biol. Chem., May 26, 2000; 275(22): 16450 - 16458. [Abstract] [Full Text] [PDF]
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D. H. D. Nguyen, D. J. Webb, A. D. Catling, Q. Song, A. Dhakephalkar, M. J. Weber, K. S. Ravichandran, and S. L. Gonias Urokinase-type Plasminogen Activator Stimulates the Ras/Extracellular Signal-regulated Kinase (ERK) Signaling Pathway and MCF-7 Cell Migration by a Mechanism That Requires Focal Adhesion Kinase, Src, and Shc. RAPID DISSOCIATION OF GRB2/SOS-SHC COMPLEX IS ASSOCIATED WITH THE TRANSIENT PHOSPHORYLATION OF ERK IN UROKINASE-TREATED CELLS J. Biol. Chem., June 16, 2000; 275(25): 19382 - 19388. [Abstract] [Full Text] [PDF]
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A. Woods and J. R. Couchman Integrin Modulation by Lateral Association J. Biol. Chem., August 4, 2000; 275(32): 24233 - 24236. [Full Text] [PDF]
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