Characterization of the major core structures of the alpha2-->8-linked polysialic acid-containing glycan chains present in neural cell adhesion molecule in embryonic chick brains.
To gain more insight into the possible functional significance of the core glycan chain(s) on which polysialylation takes place in polysialic acid (poly-Sia)-containing glycoproteins, the structure of the core glycans in the embryonic form of chick brain neural cell adhesion molecule (N-CAM) were examined using chemical and instrumental techniques. The following new structural features, which had not been reported by the early pioneering study by Finne (Finne, J. (1982) J. Biol. Chem. 257, 11966-11970), were revealed (Structure I). (i) Two distinct types of multiantennary N-linked glycans, i.e. tri- and tetra-antennary structures, are present; (ii) an alpha1-->6-linked fucosyl residue is attached to the proximal GlcNAc residue of the di-N-acetylchitobiosyl unit; (iii) that the action of GlcNAc-transferase V, which catalyzes the attachment of the beta-(1-->6)-linked GlcNAc residue on the (1-->6)-alpha-linked mannose (Man) arm, appears to be essential for polysialylation to occur on the core glycan chain is suggested by the fact that the Man residue alpha1-->6-linked to the beta-linked Man residue is invariably 2,6-di-O-substituted by the GlcNAc residue; (iv) both type 1 (Galbeta1-->3GlcNAc) and type 2 (Galbeta1-->4 GlcNAc) sequences are present in the peripheral portion of the core glycan structure. An extended form of the type 2 chain, i.e. Galbeta1-->4GlcNAcbeta1-->3Galbeta1-->4GlcNAc, is also expressed on the (1-->3)- and (1-->6)-alpha-linked Man arms; (v) on average about 1.4 mol of sulfate is attached to the type 2 N-acetyllactosamine chain(s), where in the extended form the sulfate group is probably substituted at the O-3 position of the outmost GlcNAc residue, i.e. Galbeta1-->4(HSO3-->3)GlcNAcbeta1-->3Galbeta1--> 4GlcNAcbeta1-->Man. It is possible that the unusual structural features identified in this study might play a role in the initiation of polysialylation and our data should facilitate future research regarding the signals that control polysialylation.
Kudo
M
M
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Hongo-7, Tokyo 113, Japan. syinoue@gate.sinica.edu.tw
Kitajima
K
K
Inoue
S
S
Shiokawa
K
K
Morris
H R
HR
Dell
A
A
Inoue
Y
Y
D000107:Acetylation; D000818:Animals; D002240:Carbohydrate Sequence; D002642:Chick Embryo; D006026:Glycoside Hydrolases; D009682:Magnetic Resonance Spectroscopy; D008745:Methylation; D008969:Molecular Sequence Data; D019006:Neural Cell Adhesion Molecules / Q000737:chemistry*; D009439:Neuraminidase / Q000378:metabolism; D010084:Oxidation-Reduction; D010504:Periodic Acid / Q000737:chemistry; D011134:Polysaccharides / Q000737:chemistry; D012486:Salmonella typhimurium / Q000201:enzymology; D012794:Sialic Acids / Q000737:chemistry; D013431:Sulfates
D019006:Neural Cell Adhesion Molecules; D011134:Polysaccharides; D012794:Sialic Acids; D013431:Sulfates; D010504:Periodic Acid; D006026:Glycoside Hydrolases; C090534:endo-alpha-sialidase; D009439:Neuraminidase