Expression of galectin 4 in the rat small intestine during postnatal development.

We determined the expression of an endogenous lectin, galectin 4, in the rat small intestine during postnatal development. The mRNA levels of galectin 4 did not change significantly between birth and adulthood. In contrast, the protein was present at higher levels after than before weaning, and the potential ligands for galectin 4 were more highly represented in the enterocyte microvilli of weaned than of suckling rats.

Expression and localization of galectin 4 in rat stomach during postnatal development.

Galectins are lectins implicated in cell-cell or cell-matrix adhesion, cell growth, the cell cycle, transcription processes, and apoptosis, and some of them are differentially regulated during pre- or post-natal development. The purpose of the present study was to determine whether the expression of galectin 4 is relevant to developmental processes during postnatal development in the rat stomach. Galectin 4 expression in the rat gastric mucosa, between birth and adulthood, was studied at the protein and mRNA levels by western and northern blotting, respectively.

Glucocorticoid-induced maturation of glycoprotein galactosylation and fucosylation processes in the rat small intestine.

We determined the role of glucocorticoids in the maturation of glycoprotein galactosylation and fucosylation processes in the rat small intestine during postnatal development. Treatment of suckling rats with hydrocortisone (HC) increased activities of an O-glycan: galactosyltransferase, and of an alpha-1,2-fucosyltransferase, through transcriptional regulation of the FTB gene. The activities of a fucosyltransferase inhibitor and of the enzymes responsible for the synthesis and degradation of GDP-fucose were unaffected by the treatment, whereas a fall in the activity of alpha-L-fucosidase was observed.

Dietary spermidine and spermine participate in the maturation of galactosyltransferase activity and glycoprotein galactosylation in rat small intestine.

This study considered the role of dietary polyamines in the maturation of intestinal glycoprotein galactosylation during postnatal development. In the rat small intestine, O-glycan: beta-1,3-galactosyltransferase and N-glycan: beta-1,4-galactosyltransferase are, respectively, involved in the glycan chain biosynthesis of mucins and of glycoproteins in the brush border membranes. Their activities increase significantly at weaning, in parallel with a rise in the intestinal content of spermidine and spermine (as determined by high performance liquid chromatography) and in proportion to the polyamine increase in food intake.