| First Author | Koskinen R | Year | 1998 |
| Journal | J Immunol | Volume | 160 |
| Issue | 10 | Pages | 4943-50 |
| PubMed ID | 9590242 | Mgi Jnum | J:47484 |
| Mgi Id | MGI:1203536 | Doi | 10.4049/jimmunol.160.10.4943 |
| Citation | Koskinen R, et al. (1998) The structure of avian CD5 implies a conserved function. J Immunol 160(10):4943-50 |
| abstractText | The chicken CD5 cDNA was isolated by COS cell expression cloning utilizing a novel mAb 2-191. The cDNA contains a 1422-nucleotide open reading frame encoding a mature protein with 32% and 30% identity to mouse and human CD5 polypeptides, respectively. The molecule consists of a 330-amino acid extracellular region with three repeats of the scavenger receptor cysteine-rich domain, a 29-amino acid hydrophobic transmembrane domain, and a 93-amino acid cytoplasmic tail. The cytoplasmic region contains motifs that are highly conserved between species, including several potential phosphorylation sites. The chicken CD5 is a 64-kDa phosphorylated glycoprotein with a protein core of 57 kDa as determined by immunoprecipitation and SDS-PAGE analysis. Alphabeta T cells express a homogeneously high level of CD5, whereas low or intermediate CD5 expression on gammadelta T cells depends on their tissue location. In contrast to human and mouse, CD5 is found at low levels on all chicken B cells. The high conservation of structural features, as well as signaling motifs, implies a conserved role for CD5 both in lymphocyte development and function. |
