| First Author | Miyauchi T | Year | 1990 |
| Journal | J Biochem | Volume | 107 |
| Issue | 2 | Pages | 316-23 |
| PubMed ID | 2361961 | Mgi Jnum | J:10584 |
| Mgi Id | MGI:59032 | Doi | 10.1093/oxfordjournals.jbchem.a123045 |
| Citation | Miyauchi T, et al. (1990) Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the beta-chain of major histocompatibility complex class II antigen. J Biochem 107(2):316-23 |
| abstractText | Lotus tetragonolobus agglutinin (LTA) binds preferentially to early embryonic cells in the mouse. The affinity-purified antibody raised against LTA receptors from embryonal carcinoma cells were used to screen a lambda gt11 expression library of F9 embryonal carcinoma cells, resulting in detection of a cDNA clone specifying a new glycoprotein termed basigin. The glycoprotein has been suggested to be a transmembrane one, and was found to be a new member of the immunoglobulin (Ig) superfamily. The molecular weight of basigin was largely in the range between 43,000 and 66,000, while that of the peptide portion with a putative signal sequence was inferred to be about 30,000. Significant levels of basigin mRNA were detected not only in embryonal carcinoma cells, but also in mouse embryos at 9-15 days of gestation and in various organs of the adult mouse. The Ig-like domain of basigin is unique, since it has strong homology to both the beta-chain of major histocompatibility class II antigen and the Ig V domain. The number of amino acids between the two conserved cysteine residues is intermediate between those of the Ig V and C domains. Therefore, basigin is an interesting protein in connection with the molecular evolution of the superfamily. |
