Thyroid carcinoma: interrelationships between local thyroid hormone metabolism by the type I 5'-deiodinase and the expression of thyroid hormone receptors and other thyroid-specific (de-)differentiation markers.
Thyroid carcinoma: interrelationships between local thyroid hormone metabolism by the type I 5'-deiodinase and the expression of thyroid hormone receptors and other thyroid-specific (de-)differentiation markers.
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甲状腺癌：I 型 5-脱碘酶的局部甲状腺激素代谢与甲状腺激素受体和其他甲状腺特异性（去）分化标记物的表达之间的相互关系。
DOI：
10.1007/978-3-642-60531-4_8
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
Josef Köhrle
中科院分区：
文献类型：
--
作者：
Josef Köhrle
人类甲状腺和大多数其他产生甲状腺激素的物种的甲状腺表达高水平的I型5′-脱碘酶（5′-DI），该同工酶催化激素原L-甲状腺素（3，3 ′ 5，5 ′-四碘-L-甲状腺原氨酸，T4）脱碘为生物活性形式3，3 ′，5-三碘-L-甲状腺原氨酸（L-T3）（图1）。第二种同工酶II型5′-脱碘酶（5′-DII）催化相同的反应，但具有不同的生化特性，已排除在甲状腺组织中表达（综述见（Kohrle 1994 a））。到目前为止，还没有证据表明甲状腺组织中存在第三种脱碘酶同工酶5-脱碘酶（5-D）。5-D通过从碘代甲状腺原氨酸酪氨酰环的5-或3-位去除碘原子来催化T4、T3和其他碘代甲状腺原氨酸的失活。在某些体外反应条件下，如碱性pH值，5′-DI也能够从酪氨酰环上除去碘原子，这是由于活性位点中的某种“摆动”，可能是由5′-DI活性位点中咪唑鎓硒离子对的pH依赖性改变引起的（Kohrle et al. 1991; Kohrle 1994 a）。然而，在体内，5′-DI对于从酚环的5′-（或化学等价的3′-）位置去除碘原子是相当特异的。5′-DI仅存在于甲状腺细胞中，而不存在于产生降钙素的C细胞中（Boye and Laurberg 1984）。与其他组织和同工酶一样，甲状腺5′DI也是一种完整的膜蛋白，但其在甲状腺细胞中的亚细胞定位尚不清楚。培养物中的几种人类和大鼠甲状腺细胞系表达5′-DI（表1），这使得研究甲状腺特异性表达和5′-DI活性调节的机制成为可能（Schreck et al. 1994; Kohrle 1994 a）。
The human thyroid and the thyroid glands of most other species which produce thyroid hormones express high levels of type I 5′-deiodinase (5′-DI), the isoenzyme that catalyses the deiodination of the prohormone l-thyroxine (3,3′5,5′-tetraiodo-l-thyronine, T4) to the biologically active form 3,3′,5-triiodo-l-thyronine (L-T3) (Fig. 1). Expression of the second isozyme, type II 5′-deiodinase (5′-DII), which catalyses the same reaction but with different biochemical characteristics, has been ruled out in thyroid tissues (for review see (Kohrle 1994a)). So far, no evidence for the presence of the third deiodinase isozyme, 5-deiodinase (5-D), in thyroid tissue has been presented either. 5-D catalyses the inactivation of T4, T3, and other iodothyronines by removing iodine atoms from the 5- or 3-position of the tyrosyl ring of iodothyronines. Under certain in vitro reaction conditions, such as alkaline pH, 5′-DI is also able to remove iodine atoms from the tyrosyl ring, due to a certain “wobble” in the active site, possibly induced by a pH-dependent alteration of-the imidazolium selenolate ion pair in the active site of 5′-DI (Kohrle et al. 1991; Kohrle 1994a). However, in vivo, 5′-DI is rather specific tor the removal of iodine atoms from the 5′- (or chemically equivalent 3′-) position of the phenolic ring. 5′-DI is solely found in the thyrocytes, not in calcitonin-producing C cells (Boye and Laurberg 1984). Like the other tissues and isozymes, thyroid 5′DI is also an integral membrane protein, but its subcellular location in the thyrocyte has not yet been studied. Several human and rat thyroid cell lines in culture express 5′-DI (Table 1) which allows the mechanism of thyroid-specific expression and regulation of 5′-DI activity to be studied (Schreck et al. 1994; Kohrle 1994a).
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DOI：
10.1210/jcem.75.2.1639933
发表时间：
1992-08
期刊：
The Journal of clinical endocrinology and metabolism
影响因子：
--
作者：
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影响因子：
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The Journal of clinical endocrinology and metabolism
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作者：
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