Cell surface protein and glycoprotein electrophoretic patterns in some human hemopoietic malignancies

Surface proteins radiolabeled by lactoperoxidase catalyzed radioiodination and/or sialoglycoproteins tritium-labeled by sodium metaperiodate/NaB3H4 technique, obtained from neoplastic cells of more than 50 patients with malignant hemopoietic disease have been analyzed with acrylamide gradient gel electrophoresis under denaturing conditions (SDS-PAGE). Electrophoretic protein and glycoprotein patterns were essentially similar within the group of examined chronic lymphocytic leukemia (CLL) patients with major surface glycoproteins gp44 and gp29,35. Glycoprotein gp29,35 corresponds by its electrophoretic mobility to Ia-like (HLA-DR antigen), which was identified on some CLL cells also by immunoprecipitation with a conventional anti-Ia antigen serum and subsequent electrophoretic analysis of immuno-precipitated antigen. Electrophoretic patterns of cell surface proteins and glycoproteins of CLL cells were markedly different from those of acute lymphoblastic leukemia (ALL) and acute myeloblastic leukemia (AML) cells which possessed a characteristic major cell surface glycoprotein gp95 (with relative molecular weight of 95-105k). This glycoprotein was markedly decreased or absent on examined CLL cells. Electrophoretic glycoprotein patterns revealed variations in the expression of several glycoproteins, as well as in the electrophoretic mobility of major glycoprotein gp95 also within the examined groups, particularly in acute myeloblastic leukemia.