Identity of PB76 differentiation antigen and lymphocyte alkaline phosphatase.

Alkaline phosphatases (APases, EC 3.1.3.1) are ecto-enzymes bound to cell membranes by a phosphatidyl-inositol anchor. We have previously shown that APase is present on activated murine B cells and its expression correlates with the process of B cell differentiation into immunoglobulin secretion. Recently, a monoclonal antibody (mAb), G-5-2, that recognizes a 76-kDa molecule preferentially expressed on the surface of pre-B and plasma cells (PB76) was described. Some features shared by APase and PB76 differentiation antigen suggest that the G-5-2 mAb might be specific for lymphocyte APase. Here, we have analyzed this possibility and found an absolute correlation between PB76 expression in cells and their APase activity. Although PB76 has been described as a B cell-restricted marker, PB76 is also expressed on some T cells, such as the YAC-1 T cell lymphoma, that are known to bear APase. Treatment of YAC-1 cells with phosphatidylinositol-specific phospholipase C resulted in a quantitatively correlated removal of both APase and PB76 antigens. Moreover, we demonstrate that PB76 antigen has APase activity using an enzyme-antigen immunoassay with the G-5-2 mAb. We conclude that PB76 and lymphocyte APase are one and the same antigen.