The hydrocortisone-induced transcriptional down-regulation of beta-galactoside alpha2,6-sialyltransferase in the small intestine of suckling rats is suppressed by mifepristone (RU-38.486).

The progressive loss of sialic acids of the brush-border membrane glycoproteins is one of the major biochemical changes which occur in the rat small intestine during the transition from suckling to weaning, and this process is speeded up by an injection of glucocorticoids to the suckling animals. We used the rat liver beta-galactoside alpha2,6-sialyltransferase (ST6(N), EC 2.4.

Coordinate expression of beta-galactoside alpha 2,6-sialyltransferase mRNA and enzyme activity in suckling rat jejunum cultured in different media: transcriptional induction by dexamethasone.

In attempting to elucidate the molecular basis of the expression of alpha 2,6-sialyltransferase (alpha 2,6-ST) in jejunal explants of 7-day-old rats during cultivation, the total jejunal RNA was analysed by hybridization using a cDNA clone encoding rat liver alpha 2,6-ST. Under cultivation in both serum-free and serum-containing media jejunal alpha 2,6-ST mRNA closely paralleled the bound (100,000 g pellet) as well as the soluble (100,000 g supernatant) alpha 2,6-ST activity, the correlation coefficients being 0.976 and 0.

Alpha 2,6-sialyltransferase predominates in cultured jejunum of suckling rats: it is up-regulated by dexamethasone and secreted during cultivation.

The alpha 2,6-sialyltransferase (alpha 2,6-ST) acting on N-acetyllactosamine is the major sialyltransferase of suckling rat jejunum. Jejunal explants of 7-day-old rats maintained in serum-free or serum-containing organ culture secreted alpha 2,6-ST into the cultivation medium. Dexamethasone (80 nM) stimulates primarily the secreted pool of alpha 2,6-ST.