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Lectin binding pattern of Hodgkin disease-derived cell lines in comparison to other human cell lines
M Schwonzen1, G Uhlenbruck, M Schaadt
1Medizinische Klinik I der Universität zu Köln, Federal Republic of Germany.
Insights
Researchers characterized Hodgkin (H) disease cell lines using lectins to analyze carbohydrate epitopes. Results suggest a relationship between H cells and the myelohistiocytic lineage, despite their unknown origin.
Area of Science:
- Glycobiology
- Hematologic Malignancies
- Cell Line Characterization
Background:
- Hodgkin (H) disease cell lines (L 428, L 540, L 591) were analyzed for their carbohydrate epitope composition.
- Comparison was made with nine other human cell lines, including promyelocytic (HL 60), lymphoblastoid, myeloma, histiocytic lymphoma (U 937), and non-Hodgkin lymphoma cell lines.
Purpose of the Study:
- To characterize the carbohydrate epitope composition of Hodgkin disease-derived cell lines.
- To investigate potential relationships between Hodgkin cells and other hematopoietic lineages based on glycoconjugate profiles.
Main Methods:
- Utilized a panel of 24 different fluoresceinated lectins for binding studies on cell lines.
- Analyzed protein electrophoretic mobility patterns after cell lysis.
- Stained transblotted glycoproteins using biotinylated concanavalin A and avidin peroxidase.
Main Results:
- Lectins exhibited varying binding patterns and intensities across different cell lines.
- Lotus lectin and anti-Lewis blood group X antibody showed similar binding to L 428, L 540, HL 60, and U 937 cells.
- Soybean agglutinin primarily stained L 428 and L 540 cells, with increased staining after neuraminidase treatment.
- Electrophoretic analysis revealed similar protein patterns for the three Hodgkin cell lines, with some differences observed in Lotus staining.
Conclusions:
- The origin of Hodgkin disease cells remains undetermined.
- Glycoconjugate profiles suggest a relationship between Hodgkin cells and the myelohistiocytic lineage.
Abstract:
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.