CD47 is a transmembrane receptor that interacts laterally in the membrane with certain integrins and through its cytoplasmic face with heterotrimeric G proteins (Frazier et al., 1999).

CD47 is a 50 kDa membrane receptor that has extracellular N-terminal IgV domain, five transmembrane domains, and a short C-terminal intracellular tail.

A monoclonal antibody targeting the human cell surface antigen CD47, with potential phagocytosis-inducing and antineoplastic activities.

CD47, or integrin-associated protein, is a cell surface ligand expressed in low levels by nearly all cells of the body. It plays an integral role in various immune responses as well as autoimmunity, by sending a potent “don’t eat me” signal to prevent phagocytosis.

CD47 is a kind of protein that is found on the surface of many cells in the body. It tells circulating immune cells called macrophages not to eat these cells.

Here we show that CD47 (integrin-associated protein) functions as a marker of self on murine red blood cells. Red blood cells that lacked CD47 were rapidly cleared from the bloodstream by splenic red pulp macrophages.

Recent studies have shown that blockade of CD47-SIRPα interaction enhances the phagocytic activity of phagocytes such as macrophages toward tumor cells in vitro as well as resulting in the efficient eradication of tumor cells in a variety of xenograft or syngeneic mouse models of cancer.

Targeting of the CD47-SIRPα signaling system is thus a promising strategy for cancer treatment based on modulation of both innate and acquired immune responses to tumor cells. Abbreviations ADCC antibody-dependent cellular cytotoxicity

The Cluster of Differentiation 47 (CD47) protein, expressed on both healthy and cancer cells, plays a pivotal role in this balance by delivering a “don’t eat me signal” upon binding to the Signal-regulatory protein alpha (SIRPα) receptor on myeloid cells.

The CD47 protein (also known as IAP, MER6 or OA3) consists of a single extracellular V-set IgSF domain, a presenilin domain with five membrane-spanning sections and a short cytoplasmic domain that is subject to alternative splicing, thereby giving rise to four isoforms (Campbell et al., 1992; Mushegian, 2002; Reinhold et al., 1995).