CD47 molecule (CD47)

CD47, also known as Cluster of Differentiation 47 or integrin-associated protein, is a widely expressed integral membrane glycoprotein and member of the immunoglobulin superfamily[1][2][3][4]. The receptor features an extracellular IgV-like domain, five transmembrane domains, and a short cytoplasmic tail, and acts as an immune checkpoint by interacting with signal-regulatory protein alpha (SIRPα) on macrophages to transmit a "don't eat me" signal, thereby inhibiting phagocytosis of self cells[1][2][3][4][5][6]. CD47 is also involved in various cellular processes including cell adhesion, migration, apoptosis, proliferation, and angiogenesis[1][4][6]. It is ubiquitously expressed but upregulated in many tumor types, making it a prominent therapeutic target in oncology, especially as blockade of CD47 can enhance anti-tumor immunity by enabling macrophage-mediated cancer cell clearance[1][3][4][5][6]. Targeting CD47 is also being explored in other conditions such as fibrosis and neurodegenerative diseases, but risks include anemia from red blood cell clearance and immune-related side effects[5]. CD47 has multiple alternatively spliced isoforms and is extensively glycosylated, contributing to structural heterogeneity[2][3].

Other names

Integrin-associated proteinIAPProtein OX-101OA3/GP42antigen CD47leukocyte surface antigen CD47

Blockade of CD47/SIRPα interaction to promote macrophage-mediated phagocytosis of tumor cells - Immune checkpoint inhibition - Stimulation of anti-tumor immunity (innate and adaptive)