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CD47 is a integrin-associated protein originally discovered as a plasma membrane molecule that co-purified with the integrin ·vs3 from leukocytes and placenta (Brown et al., 1990). CD47 is an unusual member of the immunoglobulin (Ig) superfamily of membrane proteins, with a single IgV-like domain at its N-terminus, a highly hydrophobic stretch with five membrane-spanning segments and an alternatively spliced cytoplasmic C-terminus ranging in length from 3 to 36 amino acids (Schwartz and Baron, 1999). In human, CD47 is a receptor for thrombospondin family members, a ligand for the transmembrane signaling protein SIRP· and a component of a supramolecular complex containing specific integrins, heterotrimeric G proteins and cholesterol (Brown and Frazier, 2001). Mouse, rat, porcine and bovine CD47 molecules have been cloned and show about 70% overall amino acid identity with the human molecule suggesting that this gene might play a similar role in different species. Materials and methods

Assignment of the CD47 gene to pig chromosome band 13q42→1/2q46 with somatic cell hybrids