Richardson S C, Aspbury R A, Fisher M J
Department of Biochemistry, University of Liverpool, U.K.
Biochem J. 1993 Jun 1;292 ( Pt 2)(Pt 2):419-24. doi: 10.1042/bj2920419.
Reversible phosphorylation is the major mechanism underlying the short-term hormonal control of phenylalanine hydroxylase activity in the liver. We report here, for the first time, the impact of a range of hormonal effectors on both the phosphorylation state and enzymic activity of phenylalanine hydroxylase present in isolated rat proximal kidney tubules. The most potent stimulator of enzyme phosphorylation was found to be parathyroid hormone, which is known to stimulate the production of cyclic AMP in proximal-tubule cells. In addition, adrenergic amines also stimulated enzyme phosphorylation, although to a lesser extent, through interaction with a mixed alpha 1 and beta receptor population.
可逆磷酸化是肝脏中苯丙氨酸羟化酶活性短期激素调控的主要机制。我们在此首次报告了一系列激素效应物对分离的大鼠近端肾小管中苯丙氨酸羟化酶的磷酸化状态和酶活性的影响。发现最有效的酶磷酸化刺激剂是甲状旁腺激素,已知它能刺激近端小管细胞中环状AMP的产生。此外,肾上腺素能胺也能刺激酶的磷酸化,尽管程度较小,是通过与混合的α1和β受体群体相互作用实现的。