Urokinase plasminogen activator receptor (uPAR) mRNA (PLAUR mRNA)

Urokinase plasminogen activator receptor (uPAR), encoded by the PLAUR gene, is a glycosylphosphatidylinositol (GPI)-anchored cell surface protein that plays a pivotal role in the regulation of pericellular proteolysis (UniProt Q03405). By binding its ligand, urokinase-type plasminogen activator (uPA), uPAR facilitates the conversion of plasminogen to plasmin, leading to the degradation of the extracellular matrix (ECM) and basement membranes. This process is essential for physiological functions such as wound healing and tissue remodeling, but it is also a key driver of pathological processes, including tumor invasion, metastasis, and angiogenesis. Furthermore, uPAR acts as a signaling hub by interacting with various transmembrane proteins, such as integrins and G protein-coupled receptors, to activate intracellular pathways like MAPK/ERK and PI3K/AKT. In many cancers, uPAR is significantly overexpressed and serves as a marker of poor prognosis and aggressive disease. Targeting uPAR at the mRNA level using antisense oligonucleotides (ASOs) or small interfering RNAs (siRNAs) is a therapeutic strategy designed to downregulate receptor expression post-transcriptionally. This approach aims to disrupt the uPA/uPAR signaling axis and its interactions with co-receptors, thereby inhibiting the mitogenic and migratory signals that promote cancer progression. While most clinical-stage uPAR inhibitors target the protein directly, mRNA-based therapies offer a potent alternative for complete gene silencing and are currently being explored in preclinical and early clinical research.

Other names

CD87 mRNAPLAUR mRNAMonocyte activation antigen Mo3 mRNAUrokinase-type plasminogen activator receptor mRNAuPAR mRNA

Antisense inhibition, RNA interference (RNAi), and post-transcriptional gene silencing.