Structural basis of the heterogeneity of asparagine-linked oligosaccharides of a waldenstrom's macroglobulinemia immunoglobulin M

• Published in: Biochimica et biophysica acta Vol. 802; no. 2; pp. 188 - 196
• Main Authors: Cahour, Annie, Debeire, Philippe, Paz Parente, José, Hartmann, Lucien, Montreuil, Jean
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 28.11.1984; Elsevier; North-Holland
• Subjects: Asparagine; Asparagine link; Biological and medical sciences; Carbohydrate Conformation; Chromatography, Affinity; Humans; Immunodeficiencies. Immunoglobulinopathies; Immunoglobulin M; Immunoglobulin M - analysis; Immunoglobulinopathies; Immunopathology; Macroglobulinemia; Magnetic Resonance Spectroscopy; Medical sciences; Oligosaccharide structure; Oligosaccharides - analysis; Waldenstrom Macroglobulinemia - immunology; Immunoglobulin M; Oligosaccharide structure; Asparagine link; Macroglobulinemia; Human; Heterogeneity; Linkage; Immunoglobulinopathy; Chemical structure; Asparagine; Hemopathy; Molecular biology; Waldenstrom macroglobulinemia; Glycan; IgM
• ISSN: 0304-4165; 0006-3002; 1872-8006
• DOI: 10.1016/0304-4165(84)90160-0

The extent of glycans heterogeneity in a pathological human immunoglobulin M ZAJ has been studied on oligosaccharides released by hydrazinolysis from the purified glycoprotein. After reduction with NaB 3H 4, asparagine-linked carbohydrate chains were separated by affinity chromatography on concanavalin A-Sepharose into oligomannosidic and N-Acetyllactosaminic types. Glycans of the oligomannosidic type were further fractionated by HPLC and those of the N-acetyllactosamine type by preparative high-voltage electrophoresis. The primary structure of the main oligosaccharides was investigated on the basis of micro-methylation analysis, mass spectrometry and sequential exo-glycosidase digestion. Glycans of the oligomannosidic type varied in size from Man 5GlcNAc 2 to Man 9GlcNAc 2. N-Acetyllactosaminic glycans were found of the biantennary, bisected-biantennary and triantennary types. They presented a higher degree of heterogeneity due to the presence of a variable number of NeuAc and fucose residues. The new structures we report here were in addition to the major biantennary one we previously described on the basis of methylation analysis and 500 MHz 1H-NMR spectroscopy (Cahour, A., Debeire, P., Hartmann, L., Montreuil, J., Van Halbeek, H. and Vliegenthart, J.F.G. (1984) FEBS Lett. 170, 343–349): NeuAc(α2–6)Gal(β1–4)GlcNAc(β1–2)Man(α1–3)[Gal(β1–4)Glc-NAc(β1–2)Man(α1–6)]Man(β1–4)Glc-NAc(β1–4)[Fuc(α1–6)]Glc NAc.