Mehdi S Q, Badger J, Kriss J P
Endocrinology. 1977 Jul;101(1):59-65. doi: 10.1210/endo-101-1-59.
The ability of various thyroid subcellular fractions to bind [125I]iodo TSH and to absorb long-acting thyroid stimulator (LATS) and thyroid stimulating immunoglobulins (TSI) activities was examined. Membranes purified from thyroid homogenates or isolated thyroid cells absorbed LATS/TSI activities and specifically bound [125I]iodo TSH. Purified thyroglobulin, nuclei, mitochondria and ribosomes did not bind [125I]iodo TSH nor did they absorb LATS/TSI activities. Cell sap obtained by gentle lysis of isolated thyroid cells failed to absorb LATS/TSI activities and to bind labeled hormone. However, freeze-thawing of the cells fragmented the membranes, releasing [125I]iodo TSH binding as well as LATS/TSI absorbing activities into the soluble (cell sap) fraction. The results suggest that the LATS/TSI antigen is of cell surface origin, includes the TSH receptor or larger membrane fragments containing the receptor, and that its release into the soluble fraction is due to the fragmentation of the thyroid membrane during homogenization and preparative procedures.
研究了甲状腺不同亚细胞组分结合[125I]碘促甲状腺激素(TSH)以及吸收长效甲状腺刺激素(LATS)和甲状腺刺激免疫球蛋白(TSI)活性的能力。从甲状腺匀浆或分离的甲状腺细胞中纯化得到的膜吸收了LATS/TSI活性,并特异性结合[125I]碘TSH。纯化的甲状腺球蛋白、细胞核、线粒体和核糖体既不结合[125I]碘TSH,也不吸收LATS/TSI活性。通过温和裂解分离的甲状腺细胞获得的细胞液不能吸收LATS/TSI活性,也不能结合标记的激素。然而,细胞的冻融使膜破碎,将[125I]碘TSH结合活性以及LATS/TSI吸收活性释放到可溶性(细胞液)组分中。结果表明,LATS/TSI抗原起源于细胞表面,包括TSH受体或含有该受体的更大膜片段,并且其释放到可溶性组分中是由于在匀浆和制备过程中甲状腺膜的破碎。