Inhibition by chlorpromazine of thyroxine modulation of flavin metabolism in liver, cerebrum and cerebellum.
Inhibition by chlorpromazine of thyroxine modulation of flavin metabolism in liver, cerebrum and cerebellum.
复制标题
氯丙嗪抑制甲状腺素调节肝脏、大脑和小脑中的黄素代谢。
DOI：
10.1016/0006-2952(85)90105-4
复制
发表时间：
1985
影响因子：
5.8
通讯作者：
Rivlin,RS
中科院分区：
文献类型：
--
作者：
Pinto,J;Huang,YP;Rivlin,RS
在已经用甲状腺素治疗的成年大鼠的肝脏中，放射性标记的核黄素掺入黄素腺嘌呤单核苷酸（FAD）和共价连接到特定脱辅基黄素酶的FAD的速率显著增强。相比之下，甲状腺素减少核黄素纳入到FAD在大脑和小脑，但继续提高纳入到共价结合部分的FAD。减少净纳入核黄素到FAD在成年大鼠的大脑中可能反映了增加利用这部分共价连接到特定的脱辅基黄素酶，而不是下调FAD生物合成酶，黄素激酶和FAD焦磷酸化酶，因为共价连接FAD发生后，形成FAD。精神药物，氯丙嗪，在一个很宽的剂量范围内，产生了抑制作用的核黄素纳入FAD和利用FAD纳入共价结合的flavoenzymes在肝脏，大脑和小脑。因此，无论甲状腺素作用的方向如何，氯丙嗪对FAD代谢的抑制作用都发生了，并且与观察到的该药物对黄素生物合成酶的抑制作用相一致。
In livers of adult rats that have been treated with thyroxine, the rate of incorporation of radiolabeled riboflavin into both flavin adenine clinucleotide (FAD) and FAD covalently attached to specific apoflavoenzymes was enhanced markedly. By contrast, thyroxine diminished riboflavin incorporation into FAD in cerebrum and cerebellum but continued to enhance incorporation into the covalently bound fraction of FAD. Diminished net incorporation of riboflavin into FAD in brains of adult rats may reflect increased utilization of this fraction for covalent attachment into specific apoflavoenzymes rather than down regulation of the FAD biosynthetic enzymes, flavokinase and FAD pyrophosphorylase, inasmuch as covalent attachment of FAD occurs subsequent to the formation of FAD. The psychotropic drug, chlorpromazine, over a wide dose range, exerted an inhibitory effect on both incorporation of riboflavin into FAD and the utilization of FAD for incorporation into covalently bound flavoenzymes in liver, cerebrum, and cerebellum. Thus, chlorpromazine inhibition of FAD metabolism occurred regardless of the direction of the thyroxine effect and was compatible with an observed inhibitory effect by this drug upon the flavin biosynthetic enzymes.