Molecular and cellular properties of the rat AA4 antigen, a C-type lectin-like receptor with structural homology to thrombomodulin.

The murine fetal stem cell marker AA4 has recently been cloned and is known to be the homolog of the human phagocytic C1q receptor involved in host defense. We herein report the molecular cloning and the cellular expression pattern of the rat AA4 antigen. Modular architecture analysis indicated that the rat AA4 is a member of C-type lectin-like family and, interestingly, displays similar domain composition and organization to thrombomodulin. Northern blot and reverse transcriptase-polymerase chain reaction analyses indicated that rat AA4 was encoded by a single transcript of 7 kilobases expressed constitutively in all tissues. In situ hybridization showed that AA4 was expressed predominantly by pneumocytes and vascular endothelial cells. Using an affinity purified polyclonal antibody raised against a rat AA4-Fc fusion protein, AA4 was identified as a glycosylated protein of 100 kDa expressed by endothelial cells > platelets > NK cells and monocytes (ED1+ cells). The staining was associated to the cell surface and intracytoplasmic vesicles. Conversely, erythrocytes, T and B lymphocytes, neutrophils, and macrophages (ED2+ cells) were consistently negative for AA4. As expected, the macrophage cell line NR8383 expressed weak levels of AA4. Taken together, our results support the idea that AA4/C1qRp is involved in some cell-cell interactions.