Ishigaki S, Abramovitz M, Listowsky I
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461.
Arch Biochem Biophys. 1989 Sep;273(2):265-72. doi: 10.1016/0003-9861(89)90483-9.
Thyroid hormone binding proteins of rat liver cytosol were characterized. Glutathione-S-transferases were identified among major cytosolic proteins adsorbed by thyroxine affinity matrices. The Ya and Yb subunits of the glutathione-S-transferases were also principal proteins of cytosol covalently labeled with 3,3',5-triiodo-L-thyronine (T3) or 3,3',5,5'-tetraiodo-L-thyronine (T4) by photoaffinity methods. T3 and T4, but not L-thyronine or iodinated tyrosines, were bound with high affinity to purified glutathione-S-transferases and were potent inhibitors of their enzymatic activities. These results suggest that glutathione-S-transferases have the potential to function in the intracellular binding and transport of thyroid hormones. The proteins provide a means for regulating the action and metabolism of thyroid hormones by acting as high capacity binding components.
对大鼠肝脏胞质溶胶中的甲状腺激素结合蛋白进行了表征。在甲状腺素亲和基质吸附的主要胞质蛋白中鉴定出了谷胱甘肽-S-转移酶。谷胱甘肽-S-转移酶的Ya和Yb亚基也是通过光亲和方法与3,3',5-三碘-L-甲状腺原氨酸（T3）或3,3',5,5'-四碘-L-甲状腺原氨酸（T4）共价标记的胞质溶胶的主要蛋白质。T3和T4，而非L-甲状腺原氨酸或碘化酪氨酸，以高亲和力与纯化的谷胱甘肽-S-转移酶结合，并且是其酶活性的有效抑制剂。这些结果表明，谷胱甘肽-S-转移酶具有在细胞内结合和转运甲状腺激素的潜力。这些蛋白质通过作为高容量结合成分，为调节甲状腺激素的作用和代谢提供了一种方式。
