Human Basigin (BSG) Protein

Background

Basigin (BSG), also known as CD147 or extracellular matrix metalloproteinase inducer (EMMPRIN), is a transmembrane glycoprotein widely expressed across tissues and involved in diverse physiological and pathological processes, including cell adhesion, metabolism, and immune responses. BSG is best known for its role in promoting tumor progression and metastasis by stimulating the production of matrix metalloproteinases (MMPs) in tumor and stromal cells, facilitating extracellular matrix remodeling and invasion. It also regulates cellular metabolism by interacting with monocarboxylate transporters (MCTs), mediating the transport of lactate and pyruvate, which are critical for glycolytic metabolism in rapidly proliferating cells. BSG is expressed at high levels in tumor tissues and is considered a biomarker for cancer aggressiveness and poor prognosis. In addition to its role in cancer, BSG participates in immune modulation, acting as a co-stimulatory molecule in T-cell activation and playing roles in viral infections, such as acting as a receptor for certain pathogens, including the malaria parasite Plasmodium falciparum. Structurally, BSG contains two Ig-like domains that mediate interactions with a wide array of ligands and partner proteins, enabling its multifunctional roles. Its upregulation in inflammatory and fibrotic diseases further underscores its significance in pathological conditions beyond cancer. Basigin's central role in cellular communication and its overexpression in disease states make it an attractive target for therapeutic interventions, with ongoing research exploring monoclonal antibodies and small molecule inhibitors to modulate its activity.