3. 甲状腺ホルモンの受容体

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  • 浜田 哲
    京都大学放射性同位元素総合センター及び第二内科
  • 南野 正隆
    京都大学放射性同位元素総合センター及び第二内科
  • 中村 浩淑
    京都大学放射性同位元素総合センター及び第二内科

書誌事項

タイトル別名
  • Thyroid Hormone Receptors
  • 甲状腺ホルモンの受容体
  • コウジョウセン ホルモン ノ ジュヨウタイ

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Although the thyroid hormones are believed to exert their effects on intracellular sites of action, very little has been known so far of the receptors and mechanism of hormone action. Recently, however, much progress has been made in nuclear and cytosol binding proteins. In this symposium, therefore, recent advances in these fields were presented together with our newly obtained results.<BR>Cytosol binding proteins for thyroid hormones were demonstrated in animal tissues by various methods. Above all, multiple binding proteins specific for T4 and T3 were found in the liver cytosol by Pevikon thin-layer electrophoresis. The binding sites of cytosol proteins are relatively hormone-specific and large in capacity. The cytosol proteins competitively inhibit nuclear binding and degradation of hormones. Therefore, they are thought to participate in the intracellular transport of hormones and possibly in the regulation of hormone metabolism.<BR>Nuclear binding protein with a high-affinity, low-capacity site for T3 was found as a non-histone protein in the chromatin by Oppenheimer et al. The binding capacity is relatively large in hormone-responsive organs and small in non-responsive organs. The relative binding affinity for T4 analogues is very closely related with their hormonal activity. Furthermore, the nuclear occupancy of T3 was shown to be closely related with mitochondrial a-GPD activity. Our recently obtained results indicate that the T3-binding capacity was increased in T3-treated hyperthyroid rats. Therefore, it appears very likely that the nuclear T3-binding protein is a thyroid hormone receptor controlling hormonal action, although a molecular mechanism following T3-binding remains to be elucidated.

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