| First Author | Maliszewski CR | Year | 1994 |
| Journal | J Immunol | Volume | 153 |
| Issue | 8 | Pages | 3574-83 |
| PubMed ID | 7930580 | Mgi Jnum | J:20864 |
| Mgi Id | MGI:68931 | Doi | 10.4049/jimmunol.153.8.3574 |
| Citation | Maliszewski CR, et al. (1994) The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol 153(8):3574-83 |
| abstractText | CD39, a 70- to 100-kDa molecule expressed primarily on activated lymphoid cells, was previously shown to mediate B cell homotypic adhesion when ligated with a subset of anti-CD39 mAbs. In the present study, we describe the cloning and molecular characterization of human and murine CD39. The nucleotide sequence of human CD39 includes an open reading frame encoding a putative 510 amino acid protein with six potential N-linked glycosylation sites, 11 Cys residues, and two potential transmembrane regions. Murine CD39 shares 75% amino acid sequence identity with human CD39 but fails to cross-react with anti-human CD39 mAbs. Although there were no significant similarities with other mammalian genes, considerable homology was found between CD39 and a guanosine diphosphatase from yeast. A series of mouse-human hybrid molecules was constructed to determine the general topology of CD39 and the location of a biologically functional epitope. These findings and supporting evidence from an anti-CD39 mAb-selected phage peptide display library indicate a likely model wherein a short intracellular N-terminus is followed by a large extracellular loop containing the epitope recognized by stimulatory anti-CD39 mAbs, and a short intracellular C terminus. The results demonstrate that CD39 is a novel cell surface glycoprotein with unusual structural characteristics. |
