Lax E R, Ghraf R, Schriefers H, Herrmann M, Petutschnigk D
Acta Endocrinol (Copenh). 1976 Aug;82(4):774-84. doi: 10.1530/acta.0.0820774.
A crude human hypophyseal extract (HE), as well as human growth hormone (GH), ovine prolactin (PRL) and commercial preparations of ACTH, TSH, pregnant mare's serum gonadotrophins (PMS) and chorionic gonadotrophin (CG) were tested for their ability to induce the activities of cytoplasmic 17 beta-hydroxysteroid dehydrogenase and microsomal delta 4-5alpha-hydrogenase and to repress the activities of microsomal 3alpha- and 3beta-hydroxysteroid dehydrogenases in the liver of hypophysectomized rats. The activity of 17beta-hydroxysteroid dehydrogenase was not affected by any of the administered hormones. For the other enzymes, only PRL was effective in causing changes in the activities; the repressive effect on 3alpha-hydroxysteroid dehydrogenase activity was highly significant (P less than 0.001). These results indicate that PRL is involved in the regulation of at least some of the enzyme activities of hepatic steroid hormone metabolism.
对一种粗制人垂体提取物(HE)、人生长激素(GH)、羊催乳素(PRL)以及促肾上腺皮质激素(ACTH)、促甲状腺激素(TSH)、孕马血清促性腺激素(PMS)和绒毛膜促性腺激素(CG)的商业制剂进行了测试,检测它们在垂体切除大鼠肝脏中诱导细胞质17β-羟类固醇脱氢酶和微粒体Δ4-5α-氢化酶活性以及抑制微粒体3α-和3β-羟类固醇脱氢酶活性的能力。17β-羟类固醇脱氢酶的活性不受任何一种所给予激素的影响。对于其他酶,只有PRL能有效引起活性变化;对3α-羟类固醇脱氢酶活性的抑制作用非常显著(P<0.001)。这些结果表明,PRL至少参与了肝脏类固醇激素代谢中某些酶活性的调节。