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Developmental changes in intestinal glycosyl-transferase activities.

M C Biol¹, A Martin, M Richard

¹Department of General and Medical Biochemistry, INSERM, CNRS U. 189, Lyon-Sud Medical School, Oullins, France.

Pediatric Research

|September 1, 1987

Summary

During rat intestinal development, glycosyl-transferase activities change significantly, impacting carbohydrate structures. These enzymatic shifts are linked to the weaning period and nutritional changes.

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Area of Science:

Biochemistry
Developmental Biology
Gastroenterology

Background:

Carbohydrate composition of intestinal glycoproteins changes during development.
Glycosylation is a key enzymatic process in modifying glycoproteins.

Purpose of the Study:

To investigate the role of glycosyl-transferases in postnatal intestinal development.
To characterize the developmental changes in N-acetylgalactosaminyl-, sialyl-, and fucosyl-transferase activities in rat intestinal mucosa.

Main Methods:

Studied soluble and microsomal glycosyl-transferase activities during postnatal development in rat intestinal mucosa.
Assessed enzyme activities in suckling, pre-weaning, and post-weaning rats.

Main Results:

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Membrane-bound N-acetylgalactosaminyl-, sialyl-, and fucosyl-transferases showed varied activities before weaning.

Sialyl-transferase activity decreased before weaning, while fucosyl-transferase activity declined progressively.

All three enzyme activities increased post-weaning, reaching adult levels.

Conclusions:

Developmental modifications in intestinal glycosylation patterns are linked to nutritional status changes during weaning.
Variable enzyme behaviors suggest the presence of multiple transferases with distinct specificities and age-dependent regulation.