Virgolini I
Nuklearmedizinische Abteilung an der 2. Medizinischen Universitätsklinik, Wien.
Wien Klin Wochenschr. 1988 Apr 1;100(7):216-7.
This study is concerned with the identification and the pharmacological properties of PGI2 receptor binding sites on human thyroid membrane fractions. Scatchard analysis is not linear, revealing a high- and a low-affinity receptor binding site. (3 H)Iloprost binding experiments were performed under various clinical conditions: in thyroid cancer the low-affinity binding sites disappear totally and the specific high-affinity binding sites are diminished according to the grade of differentiation of the cancer. An alteration in Bmax and Kd is also observed in cold nodules, in Hashimoto's and Riedl's thyroiditis and in hyperthyroidism, whereas hot nodules exhibit an increase in both the receptor subpopulations. The data provide evidence for specific PGI2 binding sites and support the suggestion of a direct regulatory key-role of PGI2 in thyroid intermediary metabolism.
本研究关注人甲状腺膜组分上前列环素（PGI2）受体结合位点的鉴定及其药理学特性。Scatchard分析呈非线性，显示出一个高亲和力和一个低亲和力受体结合位点。在各种临床情况下进行了（3H）伊洛前列素结合实验：在甲状腺癌中，低亲和力结合位点完全消失，特异性高亲和力结合位点根据癌症的分化程度而减少。在冷结节、桥本氏甲状腺炎和里德尔氏甲状腺炎以及甲状腺功能亢进症中也观察到最大结合容量（Bmax）和解离常数（Kd）的改变，而热结节中两种受体亚群均增加。这些数据为特异性PGI2结合位点提供了证据，并支持PGI2在甲状腺中间代谢中起直接调节关键作用的观点。
