Yiannakouris N, Valcana T
Department of Biology, University of Patras, Greece.
Horm Metab Res. 1998 Jan;30(1):7-11. doi: 10.1055/s-2007-978823.
Our study aimed to determine whether tetraiodothyronine (T4) binds to chromatin associated receptors and to compare such binding with that of triiodothyronine (T3). We found that the in vitro binding profile of both hormones to receptor-containing fragments released from chromatin by micrococcal nuclease was similar, with the exception of the well known lower T4 affinity. In contrast, the in vivo experiments revealed differences in the sedimentation profile of T3 and T4 bound receptors. More specifically, while T3-bound receptors are excised by micrococcal nuclease as an abundant approximately 6.2 S chromatin-receptor complex, T4-bound receptors are released as fragments of lower sedimentation coefficient (approximately 5.4 S) and as free receptors (not bound to DNA) (approximately 3.9 S). These data indicate that, in vivo, T4 binds with receptors which are differently organized in chromatin than those of T3 and could have a special, as yet undefined, intrinsic nuclear activity.
我们的研究旨在确定四碘甲状腺原氨酸(T4)是否与染色质相关受体结合,并将这种结合与三碘甲状腺原氨酸(T3)的结合进行比较。我们发现,两种激素与微球菌核酸酶从染色质释放的含受体片段的体外结合情况相似,只是T4的亲和力较低这一情况众所周知。相比之下,体内实验揭示了T3和T4结合受体的沉降情况存在差异。更具体地说,当T3结合受体被微球菌核酸酶切割成丰富的约6.2 S染色质 - 受体复合物时,T4结合受体则以沉降系数较低的片段(约5.4 S)和游离受体(不与DNA结合)(约3.9 S)形式释放。这些数据表明,在体内,T4与染色质中组织方式不同于T3结合受体的受体结合,并且可能具有特殊的、尚未明确的内在核活性。