Pammenter M, Albrecht C, Liebenberg W, van Jaarsveld P
Endocrinology. 1978 Mar;102(3):954-65. doi: 10.1210/endo-102-3-954.
The morphology and some properties of the complex iodoprotein pattern of the genetically determined congenital goiter in Afrikander cattle is described. The goiter contained irregularly shaped follicles which were devoid of colloid and the follicular epithelial cells were elongated, measuring about 20 micrometer in length compared to 10 micrometer for normal thyroid cells. The goiter cells contained apical clusters of larger and more numerous lysosomes than normal thyroid cells. Apical vesicles containing electron-dense material which were in contact with the plasma membrane could be seen in most normal thyroid cells, but were extremely scarce in the goiter. In 36 cell profiles studied none was found. The endoplasmic reticulum cisternae of the goiter differed significantly from normal thyroid cells. Fewer ribosomes were seen to be attached to the membranes of goiter cells. Furthermore, unlike normal thyroid cells, many free polysomes were seen in goiter cells. The characteristics of the unusual iodoprotein pattern of the goiter extract, resolved by gel chromatography and sucrose density gradient centrifugation, were qualitatively and quantitatively similar to that described previously (Endocrinology 91, 470, 1972). A relatively small amount of the total soluble protein was iodinated. Of these, only a 12S sedimenting species was precipitated by antithyroglobulin immunoglobulin. When separated on polyacrylamide gels containing sodium dodecyl sulfate and mercaptoethanol, this 12S species was resolved into at least 14 polypeptide components ranging in molecular weights from less than 66,000--330,000. Three of the bands, representing a small percentage of the total protein, seemed to comigrate with the major polypeptides of thyroglobulin and were also precipitated with rabbit antihyroglobulin immunoglobulin. The data indicate that glycosylation of iodoproteins was not affected although 19S thyroglobulin synthesis and subsequent storage were drastically impaired.
描述了非洲瘤牛遗传性先天性甲状腺肿复合碘蛋白模式的形态及一些特性。甲状腺肿含有形状不规则的滤泡,其中没有胶体,滤泡上皮细胞拉长,长度约为20微米,而正常甲状腺细胞为10微米。甲状腺肿细胞顶端的溶酶体簇比正常甲状腺细胞更大且数量更多。在大多数正常甲状腺细胞中可见含有与质膜接触的电子致密物质的顶端小泡,但在甲状腺肿中极为稀少。在所研究的36个细胞轮廓中未发现。甲状腺肿的内质网池与正常甲状腺细胞有显著差异。在甲状腺肿细胞的膜上可见附着的核糖体较少。此外,与正常甲状腺细胞不同,在甲状腺肿细胞中可见许多游离多核糖体。通过凝胶色谱和蔗糖密度梯度离心解析的甲状腺肿提取物异常碘蛋白模式的特征,在定性和定量上与先前描述的相似(《内分泌学》91卷,470页,1972年)。总可溶性蛋白中碘化的量相对较少。其中,只有一种12S沉降物种可被抗甲状腺球蛋白免疫球蛋白沉淀。当在含有十二烷基硫酸钠和巯基乙醇的聚丙烯酰胺凝胶上分离时,这种12S物种可分解为至少14种多肽成分,分子量范围从小于66,000到330,000。其中三条带占总蛋白的比例较小,似乎与甲状腺球蛋白的主要多肽迁移一致,并且也可被兔抗甲状腺球蛋白免疫球蛋白沉淀。数据表明,尽管19S甲状腺球蛋白的合成及随后的储存受到严重损害,但碘蛋白的糖基化未受影响。