Mj. Papandreou et al., VARIABLE CARBOHYDRATE STRUCTURES OF CIRCULATING THYROTROPIN AS STUDIED BY LECTIN AFFINITY-CHROMATOGRAPHY IN DIFFERENT CLINICAL CONDITIONS, The Journal of clinical endocrinology and metabolism, 77(2), 1993, pp. 393-398
Carbohydrate structures of intrapituitary and circulating were studied
by Concanavalin-A (Con A) and ricin lectin chromatography under diffe
rent clinical conditions. Con A permits the separation of molecules di
ffering in the extent of their carbohydrate branching, whereas ricin g
ives an estimation of the degree of their sialylation. Intrapituitary
TSH was more retained on Con A and less sialylated than circulating ho
rmone, suggesting that carbohydrate chains of intrapituitary molecules
are less mature than those present in the circulation. A greater prop
ortion of TSH firmly bound to Con A, compared to control values, was f
ound in sera from fetuses and patients with uremia, TSH-secreting aden
omas, and central hypothyroidism. In primary hypothyroid patients, TSH
binding to Con A was similar to that found in controls, but a greater
percentage of sialylated forms was seen. In central hypothyroidism pa
tients, TSH released in response to TRH was less sialylated. Interesti
ngly, no sialylated TSH was found in normal fetuses. In conclusion, th
e present data show that both TSH carbohydrate branching and sialylati
on may vary in different clinical conditions. As some of the above cli
nical conditions are known to be accompanied by variations in the bioa
ctivity of circulating TSH, the finding of changes in TSH carbohydrate
structures further supports the view that glycosylation modulates the
expression of TSH biological activity.