Crepin K M, Darville M I, Hue L, Rousseau G G
Hormone and Metabolic Research Unit, International Institute of Cellular and Molecular Pathology, Brussels, Belgium.
FEBS Lett. 1988 Jan 25;227(2):136-40. doi: 10.1016/0014-5793(88)80884-6.
In rat liver, the activity of 6-phosphofructo-2-kinase (PFK-2) decreases upon starvation and in diabetes. Cyclic AMP-dependent phosphorylation of the enzyme is not sufficient to account for this decrease. PFK-2 content was therefore measured by immunotitration and relative PFK-2 mRNA levels were determined by hybridization with cDNA probes. The data are compatible with a posttranscriptional mechanism of regulation that involves decreased translational efficiency of PFK-2 mRNA and (or) increased turnover of the PFK-2 protein.
在大鼠肝脏中，6-磷酸果糖-2-激酶（PFK-2）的活性在饥饿和糖尿病状态下会降低。该酶的环磷酸腺苷（cAMP）依赖性磷酸化不足以解释这种降低。因此，通过免疫滴定法测定了PFK-2的含量，并通过与cDNA探针杂交来确定相对PFK-2 mRNA水平。这些数据与一种转录后调控机制相符，该机制涉及PFK-2 mRNA翻译效率降低和（或）PFK-2蛋白周转增加。
