Li Q L, Yamamoto N, Inoue A, Morisawa S
Department of Biochemistry, Osaka City University Medical School.
J Biochem. 1990 May;107(5):699-702. doi: 10.1093/oxfordjournals.jbchem.a123111.
We report that long-chain fatty acyl-CoAs are potent inhibitors of the thyroid hormone (T3) receptor isolated from rat liver nuclei. Both saturated and unsaturated fatty acyl-CoAs were similarly potent. Fifty per cent inhibition of T3 binding by the receptor was observed at an oleoyl-CoA concentration as low as 1.3 microM, and the affinity of oleoyl-CoA for the receptor (Ki) was estimated to be 0.45 microM. Fatty acyl-CoAs also promoted dissociation of the hormone bound to the receptor. The action of fatty acyl-CoAs was competitive for the hormone binding site, resulting in a reduction in the receptor's affinity for T3. These observations suggest that fatty acyl-CoAs modulate the binding of the thyroid hormone to its nuclear receptor, in vitro. Whether or not such events occur in vivo remains to be determined.
我们报告称，长链脂肪酰辅酶A是从大鼠肝细胞核中分离出的甲状腺激素（T3）受体的有效抑制剂。饱和脂肪酰辅酶A和不饱和脂肪酰辅酶A的抑制效力相似。在油酰辅酶A浓度低至1.3微摩尔时，观察到受体对T3结合的50%抑制，并且油酰辅酶A对受体的亲和力（Ki）估计为0.45微摩尔。脂肪酰辅酶A还促进与受体结合的激素解离。脂肪酰辅酶A的作用对激素结合位点具有竞争性，导致受体对T3的亲和力降低。这些观察结果表明，在体外，脂肪酰辅酶A调节甲状腺激素与其核受体的结合。此类事件在体内是否发生仍有待确定。
