First Author | Ohnishi K | Year | 2000 |
Journal | J Biol Chem | Volume | 275 |
Issue | 40 | Pages | 31134-44 |
PubMed ID | 10906147 | Mgi Jnum | J:67710 |
Mgi Id | MGI:1931288 | Doi | 10.1074/jbc.M005901200 |
Citation | Ohnishi K, et al. (2000) The identification of a nonclassical cadherin expressed during B cell development and its interaction with surrogate light chain. J Biol Chem 275(40):31134-44 |
abstractText | A 130-kDa glycoprotein (p130) has been found to be associated with surrogate light chain on pro- and pre-B I cells. Using peptide sequences obtained from purified p130 we have cloned its gene. The gene encodes a typical cadherin type 1 membrane protein with six extracellular cadherin domains (one pseudo domain) but lacking the catenin-binding site in its cytoplasmic part. Even without this catenin-binding site, p130 mediates Ca(2+)-dependent homotypic adhesion of cells. The interaction of p130 with surrogate light chain is confirmed by co-transfection and co-immunoprecipitation experiments. The expression of p130 is biphasic during the B cell development. Reverse transcriptase-polymerase chain reaction and flow cytometric analyses revealed that it is expressed on B220(+)c-Kit(+) pro-B and pre-B-I cells as well as on B220(+)CD25(-)IgM(+) immature and mature B cells but not on B220(+)CD25(+) pre-B-II cells. It is also expressed in fetal liver, at low levels in myeloid cells, and strongly in intestinal epithelial cells. In the spleen, p130-expressing cells are mainly localized in the marginal zone. We call this B lineage-, intestine-, liver- and leukocyte-expressed gene BILL-cadherin. The possible functions of BILL-cadherin in B cell development are discussed. |