Epplen J T, Engel W, Schmidtke J
Hum Genet. 1980;53(3):393-9. doi: 10.1007/BF00287062.
Cyclic AMP phosphodiesterase (PDE; E.C.: 3.1.4.17) plays a crucial role in the regulation of intracellular cAMP levels arising from the hormonal activation of membrane-bound adenylcyclase in the target cell. In the present study, we revealed a complex sequence of appearance and disappearance of individual molecular electrophoretic forms of PDE during the development of the rat testis. Kinetic analysis of cAMP hydrolysis in crude testis homogenates of developmental stages where multiple PDE isozymes are expressed revealed complex kinetic behavior of PDE. After separation of individual isozymes by elution from starch gel blocks, several enzymatic forms still act with complex kinetics, indicating negatively cooperative behavior. The stage specificity of the kinetic properties of PDE appears to be related to the hormonally regulated events leading to the initiation of male puberty.
环磷酸腺苷磷酸二酯酶(PDE;酶学委员会编号:3.1.4.17)在调节靶细胞中膜结合腺苷酸环化酶的激素激活所产生的细胞内cAMP水平方面起着关键作用。在本研究中,我们揭示了大鼠睾丸发育过程中PDE各个分子电泳形式出现和消失的复杂序列。对表达多种PDE同工酶的发育阶段的睾丸粗匀浆中cAMP水解的动力学分析揭示了PDE的复杂动力学行为。通过从淀粉凝胶块上洗脱分离出各个同工酶后,几种酶形式仍以复杂的动力学起作用,表明存在负协同行为。PDE动力学特性的阶段特异性似乎与导致男性青春期开始的激素调节事件有关。