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垂体糖皮质激素结合的异质性:存在类皮质素转运蛋白样化合物的证据

Heterogeneity of pituitary glucocorticoid binding evidence for a transcortin-like compound.

作者信息

Koch B, Lutz B, Briaud B, Mialhe C

出版信息

Biochim Biophys Acta. 1976 Sep 24;444(2):497-507. doi: 10.1016/0304-4165(76)90393-7.

Abstract

Scatchard analysis, as well as sucrose gradient centrifugation demonstrate that at least two classes of specific glucocorticoid binding sites occur in the adenohypophysis. One, exhibited high affinity for both corticosterone and dexamethasone (receptor D), while the other bound only corticosterone. The latter binder revealed physico-chemical properties closely similar to those of plasma transcortin, but was shown not to be due to simple blood contamination of cytosol. This transcortin-like (TL) component, however, seemed to be carried over from plasma, since the concentration of pituitary binding sites strikingly paralleled physiological variations of plasma transcortin. Furthermore, experiments carried out with isolated pituitary cells suggested an intracellular location of that binder, although sticking to the cell membrane cannot be excluded. Finally, it was shown that the TL compound was unable, unlike the receptor D, to transfer glucocorticoids into the nuclei. One of its possible roles could be to modulate the interaction between steroids and compound D.

摘要

斯卡查德分析以及蔗糖梯度离心法表明,腺垂体中至少存在两类特异性糖皮质激素结合位点。一类对皮质酮和地塞米松均表现出高亲和力(受体D),而另一类仅结合皮质酮。后一种结合蛋白显示出与血浆皮质激素转运蛋白极为相似的物理化学性质,但研究表明它并非简单地源于细胞溶胶的血液污染。然而,这种类皮质激素转运蛋白(TL)成分似乎是从血浆中携带而来的,因为垂体结合位点的浓度与血浆皮质激素转运蛋白的生理变化显著平行。此外,对分离的垂体细胞进行的实验表明该结合蛋白位于细胞内,尽管不能排除其黏附于细胞膜的可能性。最后,研究表明与受体D不同,TL化合物无法将糖皮质激素转运至细胞核。其可能的作用之一可能是调节类固醇与化合物D之间的相互作用。

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