Uteroglobin-binding protein (UG-BP)

The Uteroglobin-binding protein (UG-BP) is a high-molecular-weight (~190 kDa), nonglycosylated cell surface receptor that mediates the biological activities of Uteroglobin (also known as SCGB1A1 or CC10) (Kundu et al., 1996). It was first identified on human trophoblasts and fibroblasts, where its activation by Uteroglobin leads to the suppression of cellular invasiveness and chemotaxis (Mandal et al., 1998). This receptor plays a critical role in regulating the maternal-fetal interface during embryo implantation and has significant implications in cancer, as its expression is often lost in highly invasive tumors like choriocarcinoma (Kundu et al., 1996). Therapeutic strategies involving recombinant Uteroglobin (rhUG) or its peptide derivatives, such as antiflammins, target this receptor to exert anti-inflammatory and anti-metastatic effects (Mandal et al., 1998). The protein is notable for being nonglycosylated, which is a rare feature for a cell surface receptor of this size. It is also expressed in the lung and trachea, where it mediates the homeostatic and anti-inflammatory effects of Uteroglobin in the respiratory system (Mandal et al., 1998). Loss of this receptor or its ligand is associated with increased susceptibility to chronic inflammatory diseases and cancer progression. Research into this receptor has led to the development of recombinant human Uteroglobin (rhUG, also known as CG100) as a potential treatment for neonatal respiratory distress and other inflammatory conditions (Therabron Therapeutics).

Other names

hUG-binding proteinNovel ~190 kDa nonglycosylated cell surface binding proteinSecretoglobin family 1A member 1 receptorCC10 receptorCCSP receptor

Binding of uteroglobin to the receptor suppresses extracellular matrix (ECM) invasion and chemotaxis of inflammatory cells.