Use of a library of mutated Maackia amurensis hemagglutinin for profiling the cell lineage and differentiation.
Thirty-five variant lectins were prepared by mutations of two amino acids within the carbohydrate-recognition domain of Maackia amurensis hemagglutinin (MAH). Each lectin showed unique carbohydrate specificity according to their bindings to soluble polyacrylamide with various mono- and oligosaccharides and to glycophorin A. The relative intensity of the bindings of carcinoma, myeloid, fibroblastic, and melanoma cells to immobilized MAH variant lectins was examined. Each cell line showed distinct profiles regarding the number of cells bound to wild-type and 35 MAH variants and the differences and the similarities in these binding profiles were quantitatively documented by the cluster analysis. The cell lines were classified into several groups and these groups surprisingly corresponded to the lineage of the cells. These results indicated that a library of mutated MAH is useful as a tool for the profiling of various cells based on the variations of the surface glycans.
Maenuma
Keisuke
K
Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Japan.
Yim
Mijung
M
Komatsu
Kunimitsu
K
Hoshino
Mayumi
M
Takahashi
Yoriko
Y
Bovin
Nicolai
N
Irimura
Tatsuro
T
D000818:Animals; D001665:Binding Sites; D002454:Cell Differentiation; D002460:Cell Line; D045744:Cell Line, Tumor; D019070:Cell Lineage; D016000:Cluster Analysis; D018922:HL-60 Cells; D006801:Humans; D029901:Maackia / Q000235:genetics / Q000378:metabolism*; D051379:Mice; D009154:Mutation; D041681:NIH 3T3 Cells; D037121:Plant Lectins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D020298:U937 Cells
D037121:Plant Lectins