Determination of major sialylated N-glycans and identification of branched sialylated N-glycans that dynamically change their content during development in the mouse cerebral cortexReportar como inadecuado




Determination of major sialylated N-glycans and identification of branched sialylated N-glycans that dynamically change their content during development in the mouse cerebral cortex - Descarga este documento en PDF. Documentación en PDF para descargar gratis. Disponible también para leer online.

Glycoconjugate Journal

, Volume 31, Issue 9, pp 671–683

First Online: 23 November 2014Received: 16 July 2014Revised: 03 October 2014Accepted: 23 October 2014

Abstract

Oligosaccharides of glycoproteins expressed on the cell surface play important roles in cell-cell interactions, particularly sialylated N-glycans having a negative charge, which interact with sialic acid-binding immunoglobulin-like lectins siglecs. The entire structure of sialylated N-glycans expressed in the mouse brain, particularly the linkage type of sialic acid residues attached to the backbone N-glycans, has not yet been elucidated. An improved method to analyze pyridylaminated sugar chains using high performance liquid chromatography HPLC was developed to determine the entire structure of sialylated N-linked sugar chains expressed in the adult and developing mouse cerebral cortices. Three classes of sialylated sugar chains were prevalent: 1 N-glycans containing α2-3-sialyl linkages on a type 2 antennary Galβ1-4GlcNAc, 2 sialylated N-glycans with α2-6-sialyl linkages on a type 2 antennary, and 3 a branched sialylated N-glycan with a Galβ1-3{NeuAcα2-6}GlcNAc- structure, which was absent at embryonic day 12 but then increased during development. This branched type sialylated N-glycan structure comprised approximately 2 % of the total N-glycans in the adult brain. Some N-glycans containing type 2 antennary were found to change their type of sialic acid linkage from α2-6-Gal to α2-3-Gal. Thus, the linkages and expression levels of sialylated N-glycans change dramatically during brain development.

KeywordsSialylated N-glycan Mouse brain development Pyridylamination Siglec AbbreviationsFucfucose

Galgalactose

GlcNAcN-acetylglucosamine

GUglucose unit value on the reverse-phase column

HPLCHigh performance liquid chromatography

MALDI-TOF-MSmatrix assisted laser desorption-ionization time-of-flight mass spectrometry

Manmannose

MUmannose unit value on the normal-phase column

NeuAcN-acetylneuraminic acid

ODSoctadecylsilyl

Tomohiro Torii and Takeshi Yoshimura contributed equally to this work.

FootnotesThe nomenclature of oligosaccharide structures is as follows: An where n = 0-2 indicates the number of antennae linked to the trimannosyl core M3B; Gn where n = 0-4, the number of galactose residues attached via β1,4-linkage to non-reducing ends; G’n where n = 1-2, the number of galactose residues attached via β1,3-linkage to the non-reducing ends; F, with core fucosylation; Fo, with outer fucosylation attached via a α1,3-linkage to N-acetylglucosamine residues; B, with bisecting N-acetylglucosamine residues.

Electronic supplementary materialThe online version of this article doi:10.1007-s10719-014-9566-2 contains supplementary material, which is available to authorized users.

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Autor: Tomohiro Torii - Takeshi Yoshimura - Mai Narumi - Seiji Hitoshi - Yoshie Takaki - Shuichi Tsuji - Kazuhiro Ikenaka

Fuente: https://link.springer.com/







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