Lectin binding pattern of Hodgkin disease-derived cell lines in comparison to other human cell lines.

The three Hodgkin disease-derived cell lines L 428, L 540, and L 591 were characterized in their carbohydrate epitope composition by a panel of lectins. Nine other human cell lines were tested in comparison to the Hodgkin (H) and Sternberg Reed (SR) cells: promyelocytic (HL 60), lymphoblastoid, myeloma, histiocytic lymphoma (U 937), and other non-Hodgkin lymphoma cell lines. Twenty-four different fluoresceinated lectins bound to the Hodgkin and other cell lines in different percentages of positive cells and with varying intensities. Lotus lectin and a monoclonal anti-Lewis blood group X antibody showed very similar binding patterns (L 428, L 540, HL 60, U 937). Soybean agglutinin stained only L 428 and L 540, although nearly all were positive after neuraminidase treatment. Cell lysis of the three H cell lines resulted in a very similar electrophoretic mobility pattern of proteins. In addition, staining of transblotted glycoproteins with biotinylated concanavalin A by avidin peroxidase reaction revealed corresponding bands. Differences were seen with Lotus staining. In summary, the origin of H cells is still unknown, but there is obviously some relationship in the glycoconjugate profile to the myelohistiocytic lineage.