Butyrate regulation of glycosylation-related gene expression: evidence for galectin-1 upregulation in human intestinal epithelial goblet cells.

Glycosylation of mucins produced by human intestinal goblet cells plays a crucial role in their functions: mucus gel physico-chemical protective properties, host-bacteria interactions, cell-cell adhesion, cell migration, and cell signaling. Colonic mucin glycosylation can be modified by luminal metabolites of fiber fermentation like butyrate. Our aim was to assess the effect of butyrate on the expression of a large panel of glycosylation-related genes in human intestinal epithelial goblet cells HT29-Cl.16E. We found that only a very scarce group of genes: 9 out of 252 were evidenced by microarray screening, and only three had their modulation significantly confirmed by real time PCR quantification. The most striking effect of butyrate was its 8- to 18-fold increase of galectin-1 gene expression, which was confirmed at the protein level, specifically with a central and apical intracellular localization. Significant butyrate effects will be discussed in regard to their possible link with mucins expressed by HT29-Cl.16E cells.