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Originally published In Press as doi:10.1074/jbc.M302529200 on September 2, 2003
J. Biol. Chem., Vol. 278, Issue 47, 46337-46348, November 21, 2003
Evidence of Regio-specific Glycosylation in Human Intestinal Mucins
PRESENCE OF AN ACIDIC GRADIENT ALONG THE INTESTINAL TRACT*
Catherine Robbe ,
Calliope Capon ,
Emmanuel Maes ,
Monique Rousset¶,
Alain Zweibaum¶,
Jean-Pierre Zanetta , and
Jean-Claude Michalski ||
From the
Unité de Glycobiologie Structurale et Fonctionnelle, Unité Mixte de Recherche (UMR) CNRS/USTL 8576, IFR 118, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq Cedex, France, Laboratoire de Biochimie, Faculté des Sciences Pharmaceutiques et Biologiques de Lille 2, 59006 Lille Cedex, France, and ¶UMR INSERM U505/UPMC, Institut Biomédical des Cordeliers, 15 rue de l'Ecole de Médecine, 75006 Paris, France
Mucin glycans were isolated from different regions of the normal human intestine (ileum, cecum, transverse and sigmoid colon, and rectum) of two individuals with ALeb blood group. A systematic study of the monosaccharides and oligosaccharide alditols released by reductive -elimination from mucins was performed using gas chromatography, matrix-assisted laser desorption ionization time-of-flight mass spectrometry, and nuclear magnetic resonance spectroscopy techniques. Important variations were observed in the mucin-associated oligosaccharide content with an increasing gradient of sialic acid from the ileum to the colon associated with a reverse gradient of fucose. Moreover, a comparative study of the Sda/Cad and ABH blood group determinants along the gastrointestinal tract showed the same reverse distribution in the two kinds of antigens. In addition, besides their heterogeneity, sialic acids presented considerable variations in the degree of O-acetylation in relation to glycan sialylation level. These data are discussed in view of recent concepts suggesting that the oligosaccharide composition of the gut constitutes a varied ecosystem for microorganisms that are susceptible to adapt there and possess the specific adhesion system and specific enzymes able to provide a carbohydrate nutrient.
Received for publication, March 12, 2003
, and in revised form, September 2, 2003.
* This investigation was supported in part by the CNRS (Unité Mixte de Recherche CNRS/USTL 8576; Director: Dr. Jean-Claude Michalski) and by the Minist re de la Recherche et de l'Enseignement Supérieur. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
|| To whom correspondence should be addressed. Tel.: 33-3-20-43-41-46; Fax: 33-3-20-4365-55; E-mail: Jean-Claude.Michalski{at}univ-lille1.fr.

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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
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