Ortiz-Caro J, Yusta B, Montiel F, Villa A, Aranda A, Pascual A
Endocrinology. 1986 Nov;119(5):2163-7. doi: 10.1210/endo-119-5-2163.
High affinity-low capacity binding sites for thyroid hormone have been identified in the nuclei of glial (C6) and neuronal (Neuro 2A) cultured cells. Equilibrium dissociation constants, determined by Scatchard analysis, were very similar in both types of cells (0.2-0.3 nM). The relative affinity of hormonal analogs was also similar: the affinity for T3 was lower than for triiodothyroacetic acid and higher than for T4 or tetraiodothyroacetic acid. The sedimentation coefficients obtained by gradient centrifugation of nuclear receptor extracted with 0.4 M KCl or excised by micrococcal nuclease digestion were 3.5 S and 6.5 S, respectively. These results suggest that the thyroid hormone receptor is not restricted to neuronal cells, but also appears in cells of glial origin.
在胶质(C6)细胞和神经元(Neuro 2A)细胞培养物的细胞核中已鉴定出甲状腺激素的高亲和力低容量结合位点。通过Scatchard分析测定的平衡解离常数在两种细胞类型中非常相似(0.2 - 0.3 nM)。激素类似物的相对亲和力也相似:对T3的亲和力低于对三碘甲状腺乙酸的亲和力,高于对T4或四碘甲状腺乙酸的亲和力。用0.4 M KCl提取或经微球菌核酸酶消化切除的核受体经梯度离心获得的沉降系数分别为3.5 S和6.5 S。这些结果表明,甲状腺激素受体不仅限于神经元细胞,也出现在胶质起源的细胞中。