Cell type and maturation stage-dependent polymorphism of N-linked oligosaccharides on murine lymphocytes and lymphoma cells.
We analyzed the overall structures of N-linked oligosaccharides on glycoproteins of various murine lymphocytic and lymphoma cells employing a newly developed method which was performed on high-performance liquid chromatography after derivatization of oligosaccharides with 2-aminopyridine. A total of 15 types of bi, tri- and tetra-antennary N-acetyllactosamine-type oligosaccharides with or without fucose and oligomannose-type oligosaccharides were identified on these cells in variable amounts depending on the type and maturation stage of the cells. It was found that all murine lymphocytic cells carry N-acetyllactosamine-type oligosaccharides with the additional alpha-linked galactose residue on the non-reducing ends. Thymocytes had exceptionally large amounts of oligosaccharides with one or even two alpha-galactose residues per molecule. In contrast, peripheral resting T cells possessed those oligosaccharides only in a small amount, although the cells produced more the oligosaccharides after stimulation with Con A. Two thymoma lines such as BW 5147 and EL-4 and one B cell lymphoma line WEHI231 contained relatively large amount of oligosaccharides with alpha-galactose residues. Significant change of the molar ratio of component carbohydrates by cell activation was observed also in oligommanose-type oligosaccharides which were few in resting T cells but were markedly increased in Con A activated cells. Molar ratio of triantennary oligosaccharides in total N-acetyllactosamine type oligosaccharides was high in thymocytes and low in resting T cells, but was increased in T cells after Con A activation. It was also very high in WEHI 231 B cell lymphoma. Although BW 5147 and EL-4 thymoma did not contain tri-antennary oligosaccharides in high proportion, they carried larger tetra-antennary oligosaccharides with an N-acetyllactosamine repeating unit in definitive amounts. It is suggested from these results that overall structures of oligosaccharides on cell surface proteins of lymphocytes are finely controlled with link to cell differentiation, activation and transformation.
Department of Immunology, Nagoya University School of Medicine, Japan.
T
T
Yoshida
N
N
Takahashi
I
I
Nakashima
D000818:Animals; D001216:Asparagine / Q000737:chemistry; D002240:Carbohydrate Sequence; D002448:Cell Adhesion; D002462:Cell Membrane / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D006001:Glycoconjugates / Q000737:chemistry*; D016131:Lymphocyte Subsets / Q000737:chemistry*; D008562:Membrane Glycoproteins / Q000737:chemistry*; D051379:Mice; D008815:Mice, Inbred Strains; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000737:chemistry; D011110:Polymorphism, Genetic; D013945:Thymoma / Q000737:chemistry*; D013950:Thymus Gland / Q000737:chemistry; D014407:Tumor Cells, Cultured
D006001:Glycoconjugates; D008562:Membrane Glycoproteins; D009844:Oligosaccharides; D001216:Asparagine