Dietary Regulation of Intestinal Glycosyl-Transferase Activities: Relation between Developmental Changes and Weaning in Rats

Abstract

Activities of rat intestinal fucosyl-transferase (GDP-fucose: glycoprotein fucosyl-transferase; EC 2.4.1.68) and sialyl-transferase (N-acetylneuraminyl-transferase; EC 2.4.99.1) respectively exhibited a significant increase following weaning and a steady decrease between birth and weaning. The variations of the two glycosyl-transferase activities with age could not be explained by the presence of inhibitory factors in microsomes or cytosol, nor were they due to a natural modification of the milk composition at the end of lactation. The increase in fucosyl-transferase activity that followed weaning was prematurely induced by early weaning. Prolonged nursing prevented the normal increase in fucosyl-transferase activity, and late weaning delayed the increase. The sensitivity to the modification of the time of weaning indicated a major effect of dietary changes, related to the introduction of a solid carbohydrate-rich diet, on the developmental pattern of this enzyme. However, a stress response could not be excluded after early weaning since the corticosterone level of the early weaned rats was enhanced as compared to that of suckling rats. For sialyl-transferase, early weaning caused a slightly greater than normal decrease in the activity, whereas prolonged nursing only weakly diminished the normal decrease in the activity. Moreover, late weaning had no effect on the sialyl-transferase activity. The age-related variations of this enzyme likely are due to factors independent of diet. Thus, the developmental variations of the fucosyl- and sialyl-transferases appear to be differently regulated.

Exploring the interplay of barrier function and leukocyte recruitment in intestinal inflammation by targeting fucosyltransferase VII and trefoil factor 3

“…The ␣1,2/3-fucosyltransferase activity was measured using asialofetuin type-1 as the exogenous acceptor as previously described (5). Briefly, the enzyme activity was carried out in a reaction mixture (total volume of 0.1 ml) that contained 5 mM ATP, 10 mM L-fucose, 25 mM MnCl2, 50 mM NaCl2, 50 mM HEPES (pH 7.0), 60 nM GDP-fucose, 10 nCi GDP-[…”

The development of the small intestine of piglets - chosen aspects

“…Before weaning, most of mucins in the intestinal epithelium contains sialic acid residues which are replaced by fucose after weaning (Shub et al, 1983;Torres-Pinedo and Mahmood, 1984;Taatjes and Roth, 1990). These modifications are parallel with alterations in activities of enzymes responsible for fucosylation and sialylation (Biol et al, 1991). Both sugars, fucose and sialic acid, in the glycan chains of glycoproteins are linked to the nonreducing end of the external saccharide, which often is galactose.…”

Effect of nonpathogenic Escherichia coli monoassociation on small intestinal brush-border glycoconjugate moieties and cytokine production after colonization in ex-germ-free rats and pigs

“…The supernatant was centrifuged at 100,000 × g for 60 minutes. The pellet containing vesicles from brush-border membranes was resuspended in 10 For the BBMV ELISA lectin labeling was performed in 96 well microtiter plates (Nalge Nunc International, Rochester, NY, USA). BBMV (protein content 10 ng per well or 50 ng per well for MAL II labeling) were fixed onto the plate in 100 µl 0.05 M carbonate buffer, pH 9.25 overnight at 4°C under a slight shaking condition.…”

“…The results strongly agree with the developmental pattern of sialyltransferase and fucosyltransferase activities in the small intestine. [8][9][10] The highly expressed sialyltransferase of suckling rat intestine has been attributed to α2,6-sialyltransferase, a major enzyme of suckling rat small intestine. [11][12][13] The production of fucosylated glycoconjugates is associated with accumulation of α1,2-fucosyltransferase mRNA.…”