Griffin M J, Cox R P
J Cell Biol. 1966 Apr;29(1):1-9. doi: 10.1083/jcb.29.1.1.
Increased alkaline phosphatase activity is induced in certain epithelial cell cultures by hormones with adrenal glucocorticoid activity or their analogues such as prednisolone (Delta(I)-hydrocortisone). Enzyme induction occurs in two distinct phases. During the first 12 hr after the addition of prednisolone, there is a small increase in alkaline phosphatase levels. After 15 to 24 hr, the enzyme activity shows a sudden, marked linear rise, reaching a maximum at 60 to 80 hr. Puromycin blocks enzyme induction immediately, even when added during the period of rapid increase of enzyme. Actinomycin D blocks induction when added no later than 8 hr after the addition of prednisolone. On the other hand, Actinomycin D added during the phase of rapid enzyme induction has no effect for at least 12 hr. These findings suggest that de novo protein synthesis is involved in prednisolone induction of alkaline phosphatase and that the RNA messenger for this enzyme is relatively stable.
具有肾上腺糖皮质激素活性的激素或其类似物（如泼尼松龙（Δ¹-氢化可的松））可在某些上皮细胞培养物中诱导碱性磷酸酶活性增加。酶诱导过程分为两个不同阶段。在加入泼尼松龙后的最初12小时内，碱性磷酸酶水平略有升高。15至24小时后，酶活性突然显著线性上升，在60至80小时达到最大值。嘌呤霉素即使在酶快速增加期间添加也能立即阻断酶诱导。放线菌素D在加入泼尼松龙后不迟于8小时添加时可阻断诱导。另一方面，在酶快速诱导阶段添加的放线菌素D至少12小时内无作用。这些发现表明，碱性磷酸酶的泼尼松龙诱导涉及从头合成蛋白质，并且该酶的RNA信使相对稳定。
