Ascoli M, Liddle R A, Puett D
Mol Cell Endocrinol. 1976 May;4(5):297-310. doi: 10.1016/0303-7207(76)90047-2.
Following an intravenous injection of tritiated ovine lutenizing hormone (LH) into mature male rats, the liver and kidneys accumulate a significant portion of the non-excreted hormone. The subcellular distribution of total radioactivity in both tissues was found to be similar to that of beta-galactosidase, a lysosomal enzyme marker. Moreover, the subcellular fraction with the highest relative specific activity of beta-galactosidase exhibited the highest degradation rate of endogenous hormone under in vitro conditions. Based on these and other observations, it is concluded that the intracellular catabolism of LH by these tissues is due to lysosomal enzymes. An analysis of the radioactive degradation products produced by a lysosomal-rich subcellular fraction showed the presence of free amino acids and oligopeptides. Thus, the uptake and degradation of the hormone by these tissues appear to occur by endocytosis followed by lysosomal catabolism. This phenomenon may represent a regulatory role in the control of (circulating) hormone concenttrations.
给成年雄性大鼠静脉注射氚标记的绵羊促黄体激素（LH）后，肝脏和肾脏会蓄积相当一部分未排出的激素。发现这两种组织中总放射性的亚细胞分布与溶酶体酶标志物β-半乳糖苷酶的分布相似。此外，在体外条件下，β-半乳糖苷酶相对比活性最高的亚细胞组分对内源性激素的降解速率也最高。基于这些及其他观察结果，得出结论：这些组织中LH的细胞内分解代谢是由溶酶体酶引起的。对富含溶酶体的亚细胞组分产生的放射性降解产物的分析表明存在游离氨基酸和寡肽。因此，这些组织对激素的摄取和降解似乎是通过内吞作用随后进行溶酶体分解代谢来发生的。这种现象可能在控制（循环）激素浓度方面发挥调节作用。
