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Originally published In Press as doi:10.1074/jbc.M109958200 on October 25, 2001

J. Biol. Chem., Vol. 277, Issue 1, 424-431, January 4, 2002
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Tumor Necrosis Factor alpha  Increases the Expression of Glycosyltransferases and Sulfotransferases Responsible for the Biosynthesis of Sialylated and/or Sulfated Lewis x Epitopes in the Human Bronchial Mucosa*

Philippe Delmotte, Sophie Degroote, Jean-Jacques Lafitte, Geneviève Lamblin, Jean-Marc Perini, and Philippe RousselDagger

From INSERM U 377 and Université de Lille 2, 59045 Lille Cedex, France

There is increasing evidence that inflammation may affect glycosylation and sulfation of various glycoproteins. The present study reports the effect of tumor necrosis factor alpha  (TNF-alpha ), a proinflammatory cytokine, on the glycosyl- and sulfotransferases of the human bronchial mucosa responsible for the biosynthesis of Lewis x epitope and of its sialylated and/or sulfated derivatives, which are expressed in human bronchial mucins. Fragments of macroscopically normal human bronchial mucosa were exposed to TNF-alpha at a concentration of 20 ng/ml. TNF-alpha was shown to increase alpha 1,3-fucosyltransferase activity as well as expression of the two alpha 1,3-fucosyltransferase genes expressed in the human airway, FUT3 and FUT4. It had no influence on alpha 1,2-fucosyltransferase activity or FUT2 expression. It also increased alpha 2,3-sialyltransferase activity and the expression of ST3Gal-III and, more importantly, ST3Gal-IV and both N-acetylglucosamine 6-O-sulfotransferase and galactose 3-O-sulfotransferase. These results are consistent with the observation of oversialylation and increased expression sialyl-Lewis x epitopes on human airway mucins secreted by patients with severe lung infection such as those with cystic fibrosis, whose airways are colonized by Pseudomonas aeruginosa. However, other cytokines may also be involved in this process.

* This work was supported by the Association Vaincre la Mucoviscidose and the Conseil Régional de la région Nord-Pas de Calais.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: INSERM U 377 and Université de Lille 2, Place de Verdun, 59045 Lille Cedex, France. Tel.: 33-3-20-63-68-19; Fax: 33-3-20-44-47-29; E-mail: proussel@univ-lille2.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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