Abstract

This review focuses on the regulation of the glycoprotein glycosylation process in small intestine and colon during postnatal development. Glycoproteins play a prominent part in intestine as mucins secreted by the goblet cells and as molecules of biological interest largely present in the microvillus membrane of the enterocytes (digestive enzymes, transporters). The age-related changes in the intestinal glycosylation control the quality of glycan chains of glycoproteins. Postnatal maturation is observed at all stages of the glycoprotein glycosylation. But it is essentially characterised in the external glycosylation by a shift from sialylation to fucosylation depending on the transcriptional regulation of the corresponding glycosyltransferases, but also on coordinate changes in the activities of glycosyltransferases and of their regulatory proteins, in nucleotide-sugar bioavailability and in product degradation by oxidases. Many factors have been evoked to trigger these changes, among which are hormonal (glucocorticoids, insulin) and dietary factors. Changes in the structure of the glycoprotein glycans might be important for the transport, the barrier function, the implantation of the immune defences and of the microflora and even probably for the biological activity of some digestive enzymes.

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