Lectin-binding pattern in human non-Hodgkin lymphoma xenografts.
The glycan profile of cell surface proteins has been studied on three human non-Hodgkin lymphoma xenografts of B-cell origin using a panel of biotinylated lectins. All three lines showed a more heterogeneous lectin-binding pattern than normal peripherial blood lymphocytes (PBLs) involving both the inner core and antenna part of the glycans. The conservative inner core (N-N-acetylchitobiose and oligomannose) was similar but fucosylated to various extents in the different lymphomas. The structure of the antennae of PBLs was characterized by glcNac-gal and galNac-gal-Sa sequences, while in lymphomas additional asialo as well as sialylated galNac containing antennae have been identified. This study suggests that NHLs sharing many immunophenotypic features show intertumoral differences in their lectin-binding pattern.
Kopper
L
L
1st Institute of Pathology and Experimental Cancer Research, Semmelweis Medical University, Budapest, Hungary.
Timar
J
J
Bankfalvi
A
A
D000818:Animals; D002460:Cell Line; D006031:Glycosylation; D006801:Humans; D037102:Lectins; D008214:Lymphocytes / Q000032:analysis / Q000166:cytology; D008228:Lymphoma, Non-Hodgkin / Q000032:analysis* / Q000473:pathology; D008562:Membrane Glycoproteins / Q000032:analysis*; D051379:Mice; D009368:Neoplasm Transplantation; D009844:Oligosaccharides / Q000032:analysis; D014183:Transplantation, Heterologous
D037102:Lectins; D008562:Membrane Glycoproteins; D009844:Oligosaccharides