Urokinase plasminogen activator surface receptor (uPAR) (uPAR)

The Urokinase plasminogen activator surface receptor (uPAR) is a glycosylphosphatidylinositol (GPI)-anchored membrane protein that plays a central role in the regulation of pericellular proteolysis, cell adhesion, and migration [UniProt: P14317]. By binding its primary ligand, the urokinase-type plasminogen activator (uPA), uPAR localizes plasminogen activation to the cell surface, facilitating the degradation of the extracellular matrix (ECM) which is essential for tissue remodeling and tumor invasion [PubMed: 21151585]. Beyond its proteolytic function, uPAR acts as a signaling scaffold by interacting with various co-receptors, including integrins and vitronectin, to activate intracellular pathways such as the MAPK/ERK and PI3K/Akt cascades [PubMed: 17641041]. In pathological conditions, uPAR is significantly overexpressed in various solid tumors, where it correlates with increased metastatic potential and poor patient prognosis, as well as in chronic inflammatory and fibrotic diseases [PubMed: 28652343]. Therapeutic strategies targeting the uPAR pathway include monoclonal antibodies, small molecules, and peptides designed to block uPA binding or disrupt uPAR-integrin interactions, as well as radiopharmaceuticals for targeted imaging and therapy [PubMed: 30154114].

Other names

PLAURCD187Monocyte activation antigen Mo3U-PARUrokinase-type plasminogen activator receptor

Inhibition of uPA-uPAR binding to prevent localized plasminogen activation and disruption of uPAR-integrin signaling complexes to halt cell migration and survival.