Mannose receptor C-type 2 (MRC2)

Mannose receptor C-type 2 (MRC2, also known as ENDO180, UPARAP, and others) is a type I transmembrane glycoprotein in the C-type lectin domain family that functions primarily as an endocytic receptor[1][2]. It mediates the binding, internalization, and lysosomal degradation of collagens and other extracellular matrix (ECM) components via its fibronectin type II domain and C-type lectin-like domains[1][2]. This receptor is expressed in several stromal cell types such as fibroblasts and macrophages and is central to tissue remodeling, cell adhesion, and cytoskeletal reorganization[1][2]. MRC2 also participates in immune regulation by facilitating antigen uptake and presentation, and can interact with the plasminogen activation system, influencing cell-surface protease activity[2]. In the context of cancer, MRC2 is upregulated in the tumor microenvironment, particularly in cancer-associated fibroblasts, where it promotes tumor invasion, metastasis, and influences immune microenvironment features[1][2][4]. High MRC2 expression has been linked to poor prognosis in several tumors and may predict lower response to certain immunotherapies, such as checkpoint inhibitors[4]. Its unique collagen-binding and endocytic properties make it a potential target for anti-cancer therapeutics, although approved drugs directly targeting MRC2 are not currently available[4].

Other names

ENDO180UPARAPCLEC13ECD280KIAA0709Urokinase receptor-associated proteinEndocytic receptor 180Macrophage mannose receptor 2Urokinase-type plasminogen activator receptor-associated protein

Inhibits collagen internalization and extracellular matrix remodeling, potentially interfering with tumor-stroma interactions and cell invasion.