| First Author | Miyake K | Year | 1995 |
| Journal | J Immunol | Volume | 154 |
| Issue | 7 | Pages | 3333-40 |
| PubMed ID | 7897216 | Mgi Jnum | J:25726 |
| Mgi Id | MGI:75739 | Doi | 10.4049/jimmunol.154.7.3333 |
| Citation | Miyake K, et al. (1995) RP105, a novel B cell surface molecule implicated in B cell activation, is a member of the leucine-rich repeat protein family. J Immunol 154(7):3333-40 |
| abstractText | The RP105 Ag is a murine B cell surface molecule that transmits an activation signal into B cells following ligation with anti-RP105 mAb. The activation leads to protection of B cells from irradiation- or dexamethasone-induced apoptosis, and to B cell proliferation. A cDNA encoding the RP105 Ag was isolated. An encoded protein is a type I transmembrane protein consisting of 641 amino acids in a mature form. Northern hybridization with a probe specific for the cDNA clone detected a transcript with a size of approximately 3 kb. The transcript was observed in spleen, but not in thymus, kidney, muscle, heart, brain, or liver. Stable transfection of the cDNA clone conferred the expression of the RP105 Ag on a pro-B cell line, which was confirmed by immunofluorescence staining and immunoprecipitation with anti-RP105 mAb. The RP105 molecule possesses 22 tandem repeats of a leucine-rich motif. These repeated motifs are observed in members of the leucine-rich repeat protein family, and have been implicated in protein-protein interactions, such as cell adhesion or receptor-ligand binding. Amino- and carboxyl-flanking regions that are characteristically conserved among members of the family are located on both sides of tandemly repeated leucine-rich motifs in RP105 molecule. These results demonstrate that RP105 is a novel member of the leucine-rich repeat protein family, and the first member that is specifically expressed on B cells. |
