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Titolo:
Structural study of N-linked oligosaccharides of human intercellular adhesion molecule-3 (CD50)
Autore:
Funatsu, O; Sato, T; Kotovuori, P; Gahmberg, CG; Ikekita, M; Furukawa, K;
Indirizzi:
Tokyo Metropolitan Inst Gerontol, Dept Biosignal Res, Itabashi Ku, Tokyo 1730015, Japan Tokyo Metropolitan Inst Gerontol Tokyo Japan 1730015 okyo 1730015, Japan Sci Univ Tokyo, Fac Sci & Technol, Dept Appl Biol Sci, Chiba, Japan Sci Univ Tokyo Chiba Japan & Technol, Dept Appl Biol Sci, Chiba, Japan Univ Helsinki, Dept Biosci, Div Biochem, FIN-00014 Helsinki, Finland Univ Helsinki Helsinki Finland FIN-00014 em, FIN-00014 Helsinki, Finland
Titolo Testata:
EUROPEAN JOURNAL OF BIOCHEMISTRY
fascicolo: 4, volume: 268, anno: 2001,
pagine: 1020 - 1029
SICI:
0014-2956(200102)268:4<1020:SSONOO>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
FUNCTION-ASSOCIATED ANTIGEN-1; SUGAR CHAINS; IMMUNE-RESPONSES; LEUKOCYTE ADHESION; ICAM-3; LFA-1; CLONING; LIGAND; FRACTIONATION; PURIFICATION;
Keywords:
ICAM-3; human leukocytes; N-linked oligosaccharides;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Furukawa, K Tokyo Metropolitan Inst Gerontol, Dept Biosignal Res, ItabashiKu, Tokyo 1730015, Japan Tokyo Metropolitan Inst Gerontol Tokyo Japan 1730015 , Japan
Citazione:
O. Funatsu et al., "Structural study of N-linked oligosaccharides of human intercellular adhesion molecule-3 (CD50)", EUR J BIOCH, 268(4), 2001, pp. 1020-1029

Abstract

The N-linked oligosaccharides were released from purified human intercellular adhesion molecule (ICAM)-3 by hydrazinolysis. Approximately 6 mol of oligosaccharides were released from 1 mol of ICAM-3. The oligosaccharides reduced with NaB[H-3](4) were separated into neutral and acidic fractions by paper electrophoresis. Most Of the acidic oligosaccharides were converted toneutral ones by digestion with sialidase, indicating that they are sialyl derivatives. The neutral and sialidase-treated acidic oligosaccharides werefractionated by serial lectin column chromatography followed by Bio-Gel P-4 column chromatography. Structural studies of each oligosaccharide by sequential exo- and endo-glycosidase digestion and by methylation analysis revealed that N-linked oligosaccharides of ICAM-3 are mainly of tri- and tetra-antennary complex-type, about 60% of which contain two to three poly N-acetyllactosamine chains terminated with the type 1 structure and those withoutthe type 1 structure per oligosaccharide. In addition, a small amount of the high mannose-type oligosaccharide with six alpha -mannose residues, which could act as a ligand for the dendritic cell-specific ICAM-3 grabbing nonintegrin, was detected.

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Documento generato il 23/01/21 alle ore 03:01:18