Binding of thyrotropin to lentil lectin is unchanged by thyrotropin-releasing hormone administration in three patients with thyrotropin-producing pituitary adenomas.
Binding of thyrotropin to lentil lectin is unchanged by thyrotropin-releasing hormone administration in three patients with thyrotropin-producing pituitary adenomas.
复制标题
在三名产生促甲状腺素的垂体腺瘤患者中,给予促甲状腺素释放激素后,促甲状腺素与扁豆凝集素的结合没有改变。
DOI:
10.1080/07435809209026675
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发表时间:
1992
影响因子:
2.1
通讯作者:
Kane,J
中科院分区:
文献类型:
--
作者:
Magner,JA;Kane,J
Glycoproteins have increased affinity for lentil lectin when fucose residues are bound to N-acetylglucosamine in the “core region” of their asparagine-linked oligosaccharides. In three patients with thyrotropin (TSH)-producing pituitary tumors, the proportion of serum TSH isoforms that bound to lentil (70.8% ± 15%) was higher than that seen for TSH from normal persons (32.5 ± 8%). Unlike normal subjects, the concentration of TSH circulating in the tumor patients after acute administration of TSH-releasing hormone (TRH) did not rise, and the TSH did not exhibit increased binding to lentil compared to basal TSH. The TSH binding to lentil in one tumor patient decreased after metoclopramide, but TSH binding to lentil generally remained unchanged after metoclopramide or L-dopa administration. We conclude that human thyrotropic tumor tissue, unlike normal thyrotrophs, generally fails to release more highly fucosylated isoforms of TSH after pharmacologic stimulation, perhaps because the tumor tissue is less readily modulated by endocrine stimuli, or because the TSH is already relatively highly fucosylated.