Leukocyte surface antigen CD47 (CD47) (CD47)

Leukocyte surface antigen CD47 (CD47) is a ubiquitously expressed transmembrane protein belonging to the immunoglobulin superfamily, featuring an extracellular IgV domain, five transmembrane domains, and a short intracellular tail. It functions as a "marker of self" by binding signal-regulatory protein alpha (SIRPα) on macrophages, delivering an anti-phagocytic "don't eat me" signal that prevents immune clearance of healthy cells. CD47 also interacts with thrombospondin-1 and integrins to regulate cell adhesion, migration, proliferation, apoptosis, and angiogenesis. In disease, CD47 is overexpressed on various cancer cells, enabling immune evasion, and has been implicated in inflammation, immune thrombocytopenia, and pulmonary fibrosis. Therapeutic strategies target CD47 blockade with antibodies or bispecifics to unleash macrophage phagocytosis against tumors, showing preclinical and clinical promise in hematologic malignancies and solid tumors like AML, lymphoma, and brain cancers, often in combinations to mitigate toxicity from its broad expression.

Other names

integrin-associated protein (IAP)antigenic surface determinant protein OA3protein MER6

blocking CD47-SIRPα interaction to promote phagocytosis of cancer cells, inhibiting anti-phagocytic "don't eat me" signal, enhancing macrophage-mediated tumor cell removal, dual-targeting with tumor antigens for selective immune activation