Open Access
Article
Multiple activities of a multifaceted receptor: roles of cleaved and soluble uPAR
Nunzia Montuori1,Pia Ragno1
1
Department of Cellular and Molecular Biology and Pathology, University Federico II, Naples, Italy
DOI: 10.2741/3392 Volume 14 Issue 7, pp.2494-2503
Published: 01 January 2009
(This article belongs to the Special Issue Urokinase-mediated plasminogen activation system)
Abstract

The urokinase-type plasminogen activator receptor (uPAR) is a GPI-anchored cell-surface receptor involved in many physiological and pathological events that include cell migration and tissue invasion. uPAR traditional role was considered the focusing of uPA proteolytic activity on the cell surface; however, different uPAR activities have been demonstrated in the last years. In fact, cell surface uPAR functionally interacts with integrins, fMLP-receptors (fMLP-Rs) and growth factor receptors, thus regulating cell adhesion, migration and proliferation. uPAR also exists in a soluble form (suPAR) that has been detected in human body fluids. Both cell surface and suPAR can be proteolytically cleaved, thus generating truncated forms lacking the N-terminal domain and exposing the specific sequence able to interact with the fMLP-Rs. The cleaved form of suPAR binds and activates the fMLP-Rs and regulates the activity of MCP-1, RANTES and SDF1 receptors. Here, we review the role that shedding and cleavage could play in regulating uPAR structural/functional interaction with other cell-surface receptors and in uPAR-mediated biological and pathological processes.

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Nunzia Montuori, Pia Ragno. Multiple activities of a multifaceted receptor: roles of cleaved and soluble uPAR. Frontiers in Bioscience-Landmark. 2009. 14(7); 2494-2503.