Sinadinović J, Kraincanić M, Mićić J V, Kostić G, Matić G
Endokrinologie. 1978 May;72(2):155-65.
The relationships among the thyroid iodoproteins, their biosynthesis in vitro in thyroid slices and the histological structure of a multinodular, sporadic goitre was examined after strumectomy from a euthyroid 51-year-old woman. Using sedimentation methods 27S, thyroglobulin (TG), 12S and 3--8S proteins were found. Besides these, 4 to 5 other proteins with molecular weights between 165,000 and 36,000 daltons were detected by polyacrylamide gel electrophoresis. The concentration of soluble proteins was very low (3 mg/100 mg wet tissue), particularly TG (0.69 MG/100 MG). The sedimentation constant (18.3S) of goitrous TG was lower than mature 19S-TG and it was poorly iodinated (0.06% w/w). 27S iodoprotein was present in the goitre extract. Thyroid slices of goitre tissue incorporated 14C-leucine into proteins and synthesized TG and its subunits. Newly synthesized proteins were rapidly released from the microsomes. Pathohistologically, struma colloido-microfolliculare with dystrophic-proliferative changes was noted. In the large follicles which were filled with colloid, dystrophic alterations in thyrocytes and desquamation of the follicular epithelium were observed. In conclusion, it is suggested that the presence of poorly iodinated, immature TG in nontoxic multinodular, sporadic goitre, in the absence of iodine deficiency, probably results in disturbances in the utilization of TG from the follicular lumen. In the follicular lumen under these conditions it is possible that 27S protein is formed from pre-existing poorly iodinated TG. These findings suggest that inability to resorb colloid may be a cause of nodule formation.
对一名51岁甲状腺功能正常女性的多结节性散发性甲状腺肿进行甲状腺切除术后,研究了甲状腺碘蛋白之间的关系、其在甲状腺切片中的体外生物合成以及该甲状腺肿的组织结构。采用沉降法发现了27S甲状腺球蛋白(TG)、12S和3 - 8S蛋白。除此之外,通过聚丙烯酰胺凝胶电泳检测到4至5种其他分子量在165,000至36,000道尔顿之间的蛋白。可溶性蛋白浓度非常低(3mg/100mg湿组织),尤其是TG(0.69mg/100mg)。甲状腺肿TG的沉降常数(18.3S)低于成熟的19S - TG,且碘化程度低(0.06% w/w)。甲状腺肿提取物中存在27S碘蛋白。甲状腺肿组织的甲状腺切片将14C - 亮氨酸掺入蛋白质中,并合成TG及其亚基。新合成的蛋白质迅速从微粒体中释放出来。病理组织学上,观察到胶体微滤泡性甲状腺肿伴有营养不良性增生性改变。在充满胶体的大滤泡中,观察到甲状腺细胞的营养不良性改变和滤泡上皮的脱落。总之,提示在无碘缺乏的情况下,非毒性多结节性散发性甲状腺肿中存在碘化不足的未成熟TG,可能导致滤泡腔内TG利用的紊乱。在这些条件下的滤泡腔内,可能由预先存在的碘化不足的TG形成27S蛋白。这些发现提示无法吸收胶体可能是结节形成的一个原因。