S. Desruisseau et al., THYROTROPIN CONTROLS DOLICHOL-LINKED SUGAR POOLS AND OLIGOSACCHARYLTRANSFERASE ACTIVITY IN THYROID-CELLS, Molecular and cellular endocrinology, 122(2), 1996, pp. 223-228
We previously showed that thyroglobulin (Tg) glycosylation is enhanced
1.5-fold under thyrotropin (TSH) stimulation, corresponding to an inc
reased number of oligosaccharide chains per molecule of Tg. Now the st
eps involving dolichol components and oligosaccharyltransferase activi
ty have been studied. Porcine thyroid cells were cultured on porous bo
ttom filters with or without TSH and incubated with [C-14]mevalonate.
Under TSH regulation, the level of the whole of dolichol components wa
s increased 1.25-fold without modifying their distribution. Dolichol,
and free and monosaccharide-linked dolichyl-phosphate, represented res
pectively 40% and 45% of total dolichol components while dolichyl-pyro
phosphate-oligosaccharide represented 3% only. A marked enhancement (4
.2-fold) of oligosaccharyltransferase activity occurred in stimulated
cells, which could correspond to the addition of the two TSH effects:
stimulation of Tg synthesis (3-fold) and of Tg glycosylation (1.5-fold
). The amount of lipid carriers appeared to be insufficiently increase
d but no component is a limiting step, suggesting that the turnover of
dolichol derivatives may be increased under TSH control through their
use by higher amounts of Tg.