Comparative biochemical and tissue distribution study of four distinct CD45 antigen specificities.

Studies on the antigenic structure of the human CD45 glycoproteins using mAb have revealed the existence of four reactivity patterns defined specifically by distinct biochemical, cellular, and histochemical distributions. In addition to the two well characterized Ag specificities, CD45 and CD45R, present on the four glycoproteins (220, 205, 190, and 180 kDa) and on the 220-kDa member, respectively, we have identified two novel specificities. These have been defined by two different mAb, UCHL1 and PD7/26/16, that recognize an epitope exclusively expressed on the 180-kDa lowest molecular sized polypeptide and an epitope shared by the three higher molecular sized polypeptides (220, 205, 190 kDa) of the complex, respectively. It has been demonstrated that they are also part of the CD45 complex by immunoprecipitation, immunoblotting, and binding assays with purified CD45 molecules. Comparative analysis by flow cytometry and immunoperoxidase techniques also showed a distinct pattern of cell distribution for each specificity. The 180-kDa specificity is present on a subset of T cells but absent on B lymphocytes, whereas the 220-kDa specificity is mainly expressed by B cells and a subpopulation of T lymphocytes. On the other hand, the cell distribution of the epitope common to the three higher members is slightly different to the conventional pan-leukocyte CD45 specificity. Thus, certain CD45+ cell types such as cutaneous Langerhans' cells, sinusoidal lymph node macrophages, and a small subset of T cells in both lymph node and tonsil did not express the 220/205/190-kDa specificity. These results further support that CD45 glycoproteins constitute a very heterogeneous molecular complex with epitopes that are selectively expressed by different cell types and by T cells at different stages of maturation.