basigin

Basigin, also known as CD147 and extracellular matrix metalloproteinase inducer (EMMPRIN), is a transmembrane glycoprotein of the immunoglobulin superfamily. It is encoded by the BSG gene and is widely expressed in many tissues, where it participates in a range of physiological and pathological processes.

Basigin consists of two immunoglobulin-like extracellular domains, a single-pass transmembrane region, and a cytoplasmic tail. It exists in multiple glycoforms resulting from post-translational glycosylation, and several splice variants add to functional diversity.

Functionally, basigin acts as a signaling receptor and as a chaperone for other membrane proteins. It stimulates the production of matrix metalloproteinases (MMPs) in neighboring cells, earning its name as an inducer of extracellular matrix remodeling (EMMPRIN). It also serves as a chaperone for monocarboxylate transporters MCT1 and MCT4, promoting lactate transport and metabolic coupling in tissues. In infectious disease, basigin is a critical receptor for Plasmodium falciparum on erythrocytes, enabling parasite entry during invasion. In reproductive biology, it has roles in spermatogenesis, fertilization, and embryo development. It is also involved in immune cell activation and inflammatory signaling.

Clinical relevance includes frequent overexpression in cancers, where high basigin levels are associated with invasion, metastasis, angiogenesis, and poor prognosis. As a surface molecule with multiple interactions, basigin is investigated as a potential therapeutic target in oncology, infectious disease, and metabolic disorders.